PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32103024-6 2020 The C-terminus of Galpha is ejected from its beta sheet core, thereby dismantling the GDP binding site. Guanosine Diphosphate 86-89 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 18-24 32092921-2 2020 In starfish, the hormone 1-methyladenine binds to an unidentified receptor on the plasma membrane of oocytes, inducing a conformational change in the heterotrimeric GTP-binding protein alpha-subunit (Galpha), so that the alpha-subunit binds GTP in exchange of GDP on the plasma membrane. Guanosine Diphosphate 260-263 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 200-206 29777099-1 2018 G protein-coupled receptors (GPCRs) activate heterotrimeric G proteins by mediating a GDP to GTP exchange in the Galpha subunit. Guanosine Diphosphate 86-89 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 113-119 31624147-5 2019 The resulting interface involved the Galpha alpha5-helix bound to the concave surface of Ric8A and the Galpha beta-sheet that wraps around the C-terminal part of the Ric8A armadillo domain, leading to a severe disruption of the GDP-binding site. Guanosine Diphosphate 228-231 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 37-43 31624147-5 2019 The resulting interface involved the Galpha alpha5-helix bound to the concave surface of Ric8A and the Galpha beta-sheet that wraps around the C-terminal part of the Ric8A armadillo domain, leading to a severe disruption of the GDP-binding site. Guanosine Diphosphate 228-231 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 103-109 30406994-2 2018 As guanine nucleotide dissociation inhibitors (GDIs), they bind Galpha GDP and inhibit GDP to GTP exchange. Guanosine Diphosphate 71-74 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 64-70 27483005-1 2016 Agonist-activated G protein-coupled receptors (GPCRs) interact with GDP-bound G protein heterotrimers (Galphabetagamma) promoting GDP/GTP exchange, which results in dissociation of Galpha from the receptor and Gbetagamma. Guanosine Diphosphate 68-71 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 103-109 27871057-4 2016 Rather, an activated receptor promotes GDP release by allosterically disrupting the nucleotide-binding site via interactions with the Galpha N-termini and C-termini. Guanosine Diphosphate 39-42 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 134-140 28760338-3 2017 Release of GDP requires a structural rearrangement between the GTPase domain and helical domain of the Galpha subunit. Guanosine Diphosphate 11-14 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 103-109 28223697-2 2017 Mutations in the G protein alpha-subunit (Galpha) that accelerate guanosine diphosphate (GDP) dissociation cause hyperactivation of the downstream effector proteins, leading to oncogenesis. Guanosine Diphosphate 66-87 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 42-48 28223697-2 2017 Mutations in the G protein alpha-subunit (Galpha) that accelerate guanosine diphosphate (GDP) dissociation cause hyperactivation of the downstream effector proteins, leading to oncogenesis. Guanosine Diphosphate 89-92 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 42-48 28223697-4 2017 Here, we use magnetic field-dependent nuclear magnetic resonance relaxation analyses to investigate the structural and dynamic properties of GDP bound Galpha on a microsecond timescale. Guanosine Diphosphate 141-144 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 151-157 28223697-5 2017 We show that Galpha rapidly exchanges between a ground-state conformation, which tightly binds to GDP and an excited conformation with reduced GDP affinity. Guanosine Diphosphate 98-101 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 13-19 28223697-5 2017 We show that Galpha rapidly exchanges between a ground-state conformation, which tightly binds to GDP and an excited conformation with reduced GDP affinity. Guanosine Diphosphate 143-146 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 13-19 27911799-2 2016 The signal is encoded into surface alterations of the Galpha subunit that carries GTP in its active state and GDP in its inactive state. Guanosine Diphosphate 110-113 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 54-60 27498775-6 2016 The mutations weakened the hydrogen bonding network between GDP/GTP and the binding pocket residues, and increased the interactions in the Galpha-Gbetagamma interface. Guanosine Diphosphate 60-63 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 139-145 27558716-1 2016 Resistance to Inhibitors of Cholinesterase A (Ric-8A) is a 60-kDa cytosolic protein that has chaperone and guanine nucleotide exchange (GEF) activity toward heterotrimeric G protein alpha subunits of the i, q, and 12/13 classes, catalyzing the release of GDP from Galpha and subsequent binding of GTP. Guanosine Diphosphate 255-258 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 264-270 27558716-2 2016 In the absence of GTP or GTP analogs, and subsequent to GDP release, Galpha forms a stable nucleotide-free complex with Ric-8A. Guanosine Diphosphate 56-59 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 69-75 26996924-2 2016 The high energy of GTP binding is used to restrain and stabilize the conformation of the Galpha switch segments, particularly switch II, to afford stable complementary to the surfaces of Galpha effectors, while excluding interaction with Gbetagamma, the regulatory binding partner of GDP-bound Galpha. Guanosine Diphosphate 284-287 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 89-95 26996924-2 2016 The high energy of GTP binding is used to restrain and stabilize the conformation of the Galpha switch segments, particularly switch II, to afford stable complementary to the surfaces of Galpha effectors, while excluding interaction with Gbetagamma, the regulatory binding partner of GDP-bound Galpha. Guanosine Diphosphate 284-287 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 187-193 26996924-2 2016 The high energy of GTP binding is used to restrain and stabilize the conformation of the Galpha switch segments, particularly switch II, to afford stable complementary to the surfaces of Galpha effectors, while excluding interaction with Gbetagamma, the regulatory binding partner of GDP-bound Galpha. Guanosine Diphosphate 284-287 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 187-193 27483005-2 2016 The GTPase activity of Galpha hydrolyzes GTP to GDP, and the GDP-bound Galpha interacts with Gbetagamma, forming a GDP-bound G protein heterotrimer. Guanosine Diphosphate 48-51 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 23-29 27483005-2 2016 The GTPase activity of Galpha hydrolyzes GTP to GDP, and the GDP-bound Galpha interacts with Gbetagamma, forming a GDP-bound G protein heterotrimer. Guanosine Diphosphate 61-64 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 23-29 27483005-2 2016 The GTPase activity of Galpha hydrolyzes GTP to GDP, and the GDP-bound Galpha interacts with Gbetagamma, forming a GDP-bound G protein heterotrimer. Guanosine Diphosphate 61-64 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 71-77 27483005-2 2016 The GTPase activity of Galpha hydrolyzes GTP to GDP, and the GDP-bound Galpha interacts with Gbetagamma, forming a GDP-bound G protein heterotrimer. Guanosine Diphosphate 61-64 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 23-29 27483005-2 2016 The GTPase activity of Galpha hydrolyzes GTP to GDP, and the GDP-bound Galpha interacts with Gbetagamma, forming a GDP-bound G protein heterotrimer. Guanosine Diphosphate 61-64 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 71-77 27483005-8 2016 Our simulation data suggests that activated receptors trigger conformational changes of the Galpha subunit that are thermodynamically favorable for opening of the nucleotide-binding pocket and GDP release. Guanosine Diphosphate 193-196 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 92-98 25414258-9 2015 We propose that a GPCR via its intracellular loop 2 directly interacts with the beta2/beta3 loop of Galpha to communicate to Linker 2, resulting in the opening and closing of the alpha-helical domain and the release of GDP during G-protein activation. Guanosine Diphosphate 219-222 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 100-106 26667172-4 2016 AGS3 binds the Gi family of G proteins via its G-protein regulatory (GoLoco) motif, stabilizing the Galpha subunit in its GDP-bound conformation. Guanosine Diphosphate 122-125 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 100-106 25480567-1 2015 Activator of G protein signaling 3 (AGS3) is a guanine nucleotide dissociation inhibitor (GDI) which stabilizes the Galpha(i/o) subunits as an AGS3/Galpha(i/o)-GDP complex. Guanosine Diphosphate 160-163 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 116-122 25480567-1 2015 Activator of G protein signaling 3 (AGS3) is a guanine nucleotide dissociation inhibitor (GDI) which stabilizes the Galpha(i/o) subunits as an AGS3/Galpha(i/o)-GDP complex. Guanosine Diphosphate 160-163 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 148-154 25480567-2 2015 It has recently been demonstrated in reconstitution experiments that the AGS3/Galpha(i/o)-GDP complex may act as a substrate of resistance to inhibitors of cholinesterase 8A (Ric-8A), a guanine exchange factor (GEF) for heterotrimeric Galpha proteins. Guanosine Diphosphate 90-93 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 78-84 25480567-2 2015 It has recently been demonstrated in reconstitution experiments that the AGS3/Galpha(i/o)-GDP complex may act as a substrate of resistance to inhibitors of cholinesterase 8A (Ric-8A), a guanine exchange factor (GEF) for heterotrimeric Galpha proteins. Guanosine Diphosphate 90-93 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 235-241 25605908-1 2015 Heterotrimeric G proteins are activated by exchange of GDP for GTP at the G protein alpha subunit (Galpha), most notably by G protein-coupled transmembrane receptors. Guanosine Diphosphate 55-58 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 99-105 25605908-7 2015 Moreover, the Ras-like domain exhibits structural plasticity within and around the nucleotide-binding cavity, and the switch I and switch II regions, which are known to adopt different conformations in the GDP- and GTP-bound states of Galpha, undergo structural rearrangements. Guanosine Diphosphate 206-209 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 235-241 25666614-1 2015 RGS14 contains distinct binding sites for both active (GTP-bound) and inactive (GDP-bound) forms of Galpha subunits. Guanosine Diphosphate 80-83 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 100-106 25666614-9 2015 Finally, a preformed RGS14 Galphai1-GDP complex exhibits full capacity to stimulate the GTPase activity of Galphao-GTP, demonstrating that RGS14 can functionally engage two distinct forms of Galpha subunits simultaneously. Guanosine Diphosphate 36-39 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 27-33 23771857-5 2014 Finally, Galpha hydrolyzes the bound GTP to GDP and returns to the resting state by re-associating with Gbetagamma. Guanosine Diphosphate 44-47 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 9-15 26179037-3 2015 The assay relies on receptor-promoted exchange of GDP for [(35)S]GTPgammaS on the Galpha subunit. Guanosine Diphosphate 50-53 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 82-88 25036778-3 2014 Investigations into its mode of action reveal that BIM traps Galphaq in the empty pocket conformation by permitting GDP exit but interdicting GTP entry, a molecular mechanism not yet assigned to any other small molecule Galpha inhibitor to date. Guanosine Diphosphate 116-119 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 61-67 23415100-3 2013 Regulator of G protein signaling proteins and G protein signaling modifier proteins respectively promote GTPase activity and hinder GTP/GDP exchange to limit Galpha activation. Guanosine Diphosphate 136-139 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 158-164 24583286-2 2014 The GTP/GDP binding status of Galpha transmits information about the ligand binding state of the GPCR to intended signal transduction pathways. Guanosine Diphosphate 8-11 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 30-36 24583286-7 2014 In addition, other proteins such as AGS3-6 can compete with Gbetagamma for binding to GDP bound Galpha. Guanosine Diphosphate 86-89 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 96-102 23626793-2 2013 Activation of these receptors results in the exchange of bound GDP for GTP in the Galpha subunit of the heterotrimeric G-protein. Guanosine Diphosphate 63-66 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 82-88 24292645-2 2014 In silico analysis demonstrated energetic changes when the Galpha C-terminal helix (alpha5) interacts with the R* cytoplasmic pocket, thus leading to displacement of the helical domain and GDP release. Guanosine Diphosphate 189-192 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 59-65 24386514-4 2013 An agonist-activated receptor interacts with specific sites on G proteins and promotes the release of GDP from the Galpha subunit. Guanosine Diphosphate 102-105 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 115-121 23576747-2 2013 Agonist-stimulated guanine nucleotide exchange activity of G-protein-coupled receptors results in the exchange of G-protein-bound GDP to GTP and the dissociation and activation of the complex into Galpha-GTP and a Gbetagamma dimer. Guanosine Diphosphate 130-133 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 197-203 23200849-6 2013 In rat C6 glioma cells that express endogenous Galpha(h)/TG2, cAMP accumulation induced by isoproterenol or forskolin was significantly inhibited by overexpression of Galpha(h)/TG2-C277V, a dominant-negative mutant that lacks transglutaminase activity, but was not inhibited by the Galpha(h)/TG2-S171E mutant that cannot bind GTP/GDP. Guanosine Diphosphate 330-333 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 47-53 23200849-6 2013 In rat C6 glioma cells that express endogenous Galpha(h)/TG2, cAMP accumulation induced by isoproterenol or forskolin was significantly inhibited by overexpression of Galpha(h)/TG2-C277V, a dominant-negative mutant that lacks transglutaminase activity, but was not inhibited by the Galpha(h)/TG2-S171E mutant that cannot bind GTP/GDP. Guanosine Diphosphate 330-333 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 167-173 23200849-6 2013 In rat C6 glioma cells that express endogenous Galpha(h)/TG2, cAMP accumulation induced by isoproterenol or forskolin was significantly inhibited by overexpression of Galpha(h)/TG2-C277V, a dominant-negative mutant that lacks transglutaminase activity, but was not inhibited by the Galpha(h)/TG2-S171E mutant that cannot bind GTP/GDP. Guanosine Diphosphate 330-333 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 167-173 22274999-2 2012 In the resting state, G protein forms a heterotrimer, consisting of GDP-bound form of the G protein alpha subunit (Galpha(GDP)) and G protein betagamma subunit (Gbetagamma). Guanosine Diphosphate 68-71 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 115-121 22952234-2 2012 GLs of LGN are also known to bind the GDP form of Galpha(i/o) during asymmetric cell division. Guanosine Diphosphate 38-41 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 50-56 22952234-3 2012 Here, we show that the C-terminal GL domain of LGN binds four molecules of Galpha(i) GDP. Guanosine Diphosphate 85-88 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 75-81 22952234-4 2012 The crystal structures of Galpha(i) GDP in complex with LGN GL3 and GL4, respectively, reveal distinct GL/Galpha(i) interaction features when compared with the only high resolution structure known with GL/Galpha(i) interaction between RGS14 and Galpha(i1.) Only a few residues C-terminal to the conserved GL sequence are required for LGN GLs to bind to Galpha(i) GDP. Guanosine Diphosphate 36-39 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 26-32 22952234-4 2012 The crystal structures of Galpha(i) GDP in complex with LGN GL3 and GL4, respectively, reveal distinct GL/Galpha(i) interaction features when compared with the only high resolution structure known with GL/Galpha(i) interaction between RGS14 and Galpha(i1.) Only a few residues C-terminal to the conserved GL sequence are required for LGN GLs to bind to Galpha(i) GDP. Guanosine Diphosphate 36-39 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 106-112 22952234-4 2012 The crystal structures of Galpha(i) GDP in complex with LGN GL3 and GL4, respectively, reveal distinct GL/Galpha(i) interaction features when compared with the only high resolution structure known with GL/Galpha(i) interaction between RGS14 and Galpha(i1.) Only a few residues C-terminal to the conserved GL sequence are required for LGN GLs to bind to Galpha(i) GDP. Guanosine Diphosphate 36-39 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 106-112 22952234-4 2012 The crystal structures of Galpha(i) GDP in complex with LGN GL3 and GL4, respectively, reveal distinct GL/Galpha(i) interaction features when compared with the only high resolution structure known with GL/Galpha(i) interaction between RGS14 and Galpha(i1.) Only a few residues C-terminal to the conserved GL sequence are required for LGN GLs to bind to Galpha(i) GDP. Guanosine Diphosphate 36-39 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 106-112 22952234-4 2012 The crystal structures of Galpha(i) GDP in complex with LGN GL3 and GL4, respectively, reveal distinct GL/Galpha(i) interaction features when compared with the only high resolution structure known with GL/Galpha(i) interaction between RGS14 and Galpha(i1.) Only a few residues C-terminal to the conserved GL sequence are required for LGN GLs to bind to Galpha(i) GDP. Guanosine Diphosphate 363-366 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 26-32 22952234-5 2012 A highly conserved "double Arg finger" sequence (RPsi(D/E)(D/E)QR) is responsible for LGN GL to bind to GDP bound to Galpha(i). Guanosine Diphosphate 104-107 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 117-123 22274999-5 2012 Finally, Galpha hydrolyzes the bound GTP to GDP and returns to the resting state by re-associating with Gbetagamma. Guanosine Diphosphate 44-47 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 9-15 22167191-3 2012 Although GPSM3 is known to bind Galpha(i) GDP subunits via its GoLoco motifs, here we report that GPSM3 also interacts with the Gbeta subunits Gbeta1 to Gbeta4, independent of Ggamma or Galpha GDP subunit interactions. Guanosine Diphosphate 42-45 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 32-38 22167191-3 2012 Although GPSM3 is known to bind Galpha(i) GDP subunits via its GoLoco motifs, here we report that GPSM3 also interacts with the Gbeta subunits Gbeta1 to Gbeta4, independent of Ggamma or Galpha GDP subunit interactions. Guanosine Diphosphate 42-45 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 186-192 22167191-3 2012 Although GPSM3 is known to bind Galpha(i) GDP subunits via its GoLoco motifs, here we report that GPSM3 also interacts with the Gbeta subunits Gbeta1 to Gbeta4, independent of Ggamma or Galpha GDP subunit interactions. Guanosine Diphosphate 193-196 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 32-38 21375271-2 2011 After activation, receptors interact with heterotrimeric G proteins and catalyze GDP release from the Galpha subunit, the rate limiting step in G protein activation, to form a high affinity nucleotide-free GPCR-G protein complex. Guanosine Diphosphate 81-84 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 102-108 19820068-3 2009 However, measuring GAP activity is complicated by slow guanosine diphosphate (GDP) release from Galpha and lack of solution phase assays for detecting free GDP in the presence of excess guanosine triphosphate (GTP). Guanosine Diphosphate 78-81 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 96-102 21390270-5 2011 Indeed, S(GDP) of Galpha(t), is characterized by a more extensive energy coupling between nucleotide binding site and distal regions involved in GEF recognition compared to small G proteins, which attenuates in the active state. Guanosine Diphosphate 10-13 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 18-24 21390270-9 2011 Collectively, nucleotide binding changes the information flow through the conserved Ras-like domain, where GDP enhances the flexibility of mechanically distinct portions involved in nucleotide switch, and favors long distance allosteric communication (in Galpha proteins), compared to GTP. Guanosine Diphosphate 107-110 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 255-261 21853086-1 2011 Heterotrimeric G protein alpha subunits are activated upon exchange of GDP for GTP at the nucleotide binding site of Galpha, catalyzed by guanine nucleotide exchange factors (GEFs). Guanosine Diphosphate 71-74 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 117-123 20075078-1 2010 Active G protein-coupled receptors activate heterotrimeric Galphabetagamma proteins by catalyzing the exchange of GDP by GTP at the Galpha subunit. Guanosine Diphosphate 114-117 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 59-65 19703944-3 2009 Lubrol PX, a non-ionic detergent, which has been widely used in nucleotide dissociation/binding assays, was found to accelerate both GDP dissociation and GTPgammaS binding from/to Galpha in parallel at above its critical micelle concentration (cmc). Guanosine Diphosphate 133-136 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 180-186 19783621-1 2009 According to accepted doctrine, agonist-bound G protein-coupled receptors catalyze the exchange of GDP for GTP and facilitate the dissociation of Galpha and Gbetagamma, which in turn regulate their respective effectors. Guanosine Diphosphate 99-102 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 146-152 19783621-5 2009 GDP-bound Galpha(s) and Gbetagamma did not compete, but rather facilitated their interaction with 5NT, consistent with the isolation of a ternary complex (5NT, Galpha(s), and Gbetagamma) by gel filtration. Guanosine Diphosphate 0-3 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 10-16 19783621-5 2009 GDP-bound Galpha(s) and Gbetagamma did not compete, but rather facilitated their interaction with 5NT, consistent with the isolation of a ternary complex (5NT, Galpha(s), and Gbetagamma) by gel filtration. Guanosine Diphosphate 0-3 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 160-166 19760664-2 2009 Galpha(t) exhibits a low rate of basal (uncatalyzed) nucleotide exchange and an ordered Switch II region in the GDP-bound state, unlike Galpha(i), which exhibits higher basal exchange and a disordered Switch II region in Galpha(i)GDP structures. Guanosine Diphosphate 112-115 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 0-6 19760664-2 2009 Galpha(t) exhibits a low rate of basal (uncatalyzed) nucleotide exchange and an ordered Switch II region in the GDP-bound state, unlike Galpha(i), which exhibits higher basal exchange and a disordered Switch II region in Galpha(i)GDP structures. Guanosine Diphosphate 230-233 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 0-6 19513240-2 2008 This property is achieved by a guanine nucleotide cycle wherein the inactive, signaling-incompetent Galpha subunit is normally bound to GDP; activation to signaling-competent Galpha occurs through the exchange of GDP for GTP (typically catalyzed via seven-transmembrane domain G-protein coupled receptors [GPCRs]), which dissociates the Gbetagamma dimer from Galpha-GTP and initiates signal transduction. Guanosine Diphosphate 136-139 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 100-106 19686126-2 2009 A key point of regulation in G protein-mediated signaling is the interconversion between the active GTP-bound and inactive GDP-bound states of the Galpha subunit, which regulatory proteins, such as guanine nucleotide exchange factors (GEFs), can control. Guanosine Diphosphate 123-126 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 147-153 19513240-2 2008 This property is achieved by a guanine nucleotide cycle wherein the inactive, signaling-incompetent Galpha subunit is normally bound to GDP; activation to signaling-competent Galpha occurs through the exchange of GDP for GTP (typically catalyzed via seven-transmembrane domain G-protein coupled receptors [GPCRs]), which dissociates the Gbetagamma dimer from Galpha-GTP and initiates signal transduction. Guanosine Diphosphate 213-216 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 100-106 19513240-2 2008 This property is achieved by a guanine nucleotide cycle wherein the inactive, signaling-incompetent Galpha subunit is normally bound to GDP; activation to signaling-competent Galpha occurs through the exchange of GDP for GTP (typically catalyzed via seven-transmembrane domain G-protein coupled receptors [GPCRs]), which dissociates the Gbetagamma dimer from Galpha-GTP and initiates signal transduction. Guanosine Diphosphate 213-216 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 175-181 19513240-2 2008 This property is achieved by a guanine nucleotide cycle wherein the inactive, signaling-incompetent Galpha subunit is normally bound to GDP; activation to signaling-competent Galpha occurs through the exchange of GDP for GTP (typically catalyzed via seven-transmembrane domain G-protein coupled receptors [GPCRs]), which dissociates the Gbetagamma dimer from Galpha-GTP and initiates signal transduction. Guanosine Diphosphate 213-216 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 175-181 19513240-3 2008 The hydrolysis of GTP, greatly accelerated by "Regulator of G-protein Signaling" (RGS) proteins, returns Galpha to its inactive GDP-bound form and terminates signaling. Guanosine Diphosphate 128-131 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 105-111 19513240-4 2008 Through extensive characterization of mammalian Galpha isoforms, the rate-limiting step in this cycle is currently considered to be the GDP/GTP exchange rate, which can be orders of magnitude slower than the GTP hydrolysis rate. Guanosine Diphosphate 136-139 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 48-54 18541531-10 2008 The action of Ric-8A on AGS3:Galpha(i1).GDP ensures unidirectional activation of Galpha subunits that cannot be reversed by AGS3. Guanosine Diphosphate 40-43 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 29-35 18541531-3 2008 Ric-8A, acting as a guanine nucleotide exchange factor, catalyzes the release of GDP from various Galpha.GDP subunits and forms a stable nucleotide-free Ric-8A:Galpha complex. Guanosine Diphosphate 81-84 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 98-104 18541531-3 2008 Ric-8A, acting as a guanine nucleotide exchange factor, catalyzes the release of GDP from various Galpha.GDP subunits and forms a stable nucleotide-free Ric-8A:Galpha complex. Guanosine Diphosphate 81-84 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 160-166 18541531-3 2008 Ric-8A, acting as a guanine nucleotide exchange factor, catalyzes the release of GDP from various Galpha.GDP subunits and forms a stable nucleotide-free Ric-8A:Galpha complex. Guanosine Diphosphate 105-108 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 98-104 18541531-3 2008 Ric-8A, acting as a guanine nucleotide exchange factor, catalyzes the release of GDP from various Galpha.GDP subunits and forms a stable nucleotide-free Ric-8A:Galpha complex. Guanosine Diphosphate 105-108 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 160-166 18541531-4 2008 AGS3, a guanine nucleotide dissociation inhibitor (GDI), binds and stabilizes Galpha subunits in their GDP-bound state. Guanosine Diphosphate 103-106 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 78-84 18537558-2 2008 This characteristic is achieved by the adoption of two principal states: an inactive state in which GDP-bound Galpha is complexed with the Gbetagamma dimer, and an active state in which GTP-bound Galpha is freed of its Gbetagamma binding partner. Guanosine Diphosphate 100-103 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 110-116 18537558-4 2008 Discrete differences in conformation between GDP- and GTP-bound Galpha underlie its nucleotide-dependent protein-protein interactions (e.g., with Gbetagamma/receptor and effectors, respectively) that are critical for maintaining their proper nucleotide cycling and signaling properties. Guanosine Diphosphate 45-48 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 64-70 17430994-1 2007 G-protein-coupled receptors (GPCRs) serve as catalytic activators of heterotrimeric G-proteins (Galphabetagamma) by exchanging GTP for the bound GDP on the Galpha subunit. Guanosine Diphosphate 145-148 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 96-102 17962409-1 2007 The heterotrimeric G protein alpha subunit (Galpha) functions as a molecular switch by cycling between inactive GDP-bound and active GTP-bound states. Guanosine Diphosphate 112-115 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 44-50 17962409-2 2007 When bound to GDP, Galpha interacts with high affinity to a complex of the beta and gamma subunits (Gbetagamma), but when bound to GTP, Galpha dissociates from this complex to activate downstream signaling pathways. Guanosine Diphosphate 14-17 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 19-25 17430994-7 2007 We highlight several recent results shedding new light on the structural changes in Galpha that may underlie GDP release. Guanosine Diphosphate 109-112 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 84-90 17854654-15 2007 It is possible that the collapse of the switch regions, associated with Galpha deactivation, also encounters a kinetic barrier, and is coupled to product (Pi) release or an event preceding formation of the GDP*Pi complex. Guanosine Diphosphate 206-209 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 72-78 17644194-5 2007 This coupling promotes the exchange of GDP for GTP on the Galpha subunit, leading to effector activation by both Galpha-GTP and Gbetagamma. Guanosine Diphosphate 39-42 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 58-64 17644194-5 2007 This coupling promotes the exchange of GDP for GTP on the Galpha subunit, leading to effector activation by both Galpha-GTP and Gbetagamma. Guanosine Diphosphate 39-42 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 113-119 16923326-2 2006 In the resting state, the G-protein alpha subunit (Galpha) binds GDP and Gbetagamma. Guanosine Diphosphate 65-68 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 51-57 17011013-4 2006 Binding of CTalpha by R* then triggers GDP/GTP exchange in the Galpha subunit. Guanosine Diphosphate 39-42 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 63-69 17053066-2 2006 Crystal structures indicate that conformational changes in "switch" sequences of Galpha, controlled by the identity of the bound nucleotide (GDP and GTP), modulate binding affinities to the Gbetagamma subunits, receptor, and effector proteins. Guanosine Diphosphate 141-144 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 81-87 16892066-1 2006 Heptahelical receptors activate intracellular signaling pathways by catalyzing GTP for GDP exchange on the heterotrimeric G protein alpha subunit (G alpha). Guanosine Diphosphate 87-90 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 122-154 16923326-3 2006 Receptors activate G proteins by catalyzing GTP for GDP exchange on Galpha, leading to a structural change in the Galpha(GTP) and Gbetagamma subunits that allows the activation of a variety of downstream effector proteins. Guanosine Diphosphate 52-55 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 68-74 16923326-3 2006 Receptors activate G proteins by catalyzing GTP for GDP exchange on Galpha, leading to a structural change in the Galpha(GTP) and Gbetagamma subunits that allows the activation of a variety of downstream effector proteins. Guanosine Diphosphate 52-55 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 114-120 16923326-7 2006 However, relatively little is known about the receptor-G protein complex and how this interaction leads to GDP release from Galpha. Guanosine Diphosphate 107-110 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 124-130 16407201-5 2006 GDP/GTP exchange catalyzed by receptor requires Gbetagamma in amounts approximately equimolar to Galpha, but GAP inhibition was observed with superstoichiometric Gbetagamma. Guanosine Diphosphate 0-3 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 97-103 15665133-1 2005 Activation of phospholipase Cbeta (PLCbeta) by G-proteins results in increased intracellular Ca(2+) and activation of protein kinase C. We have previously found that activated PLCbeta-Gbetagamma complex can be rapidly deactivated by Galpha(GDP) subunits without dissociation, which led to the suggestion that Galpha(GDP) binds to PLCbeta-Gbeta gamma and perturbs the activating interaction without significantly affecting the PLCbeta-Gbeta gamma binding energy. Guanosine Diphosphate 240-243 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 233-239 16051611-5 2005 Binding of R6A-1 is generally specific to the GDP-bound state of the Galpha subunits and excludes association with Gbetagamma. Guanosine Diphosphate 46-49 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 69-75 15983037-10 2005 Because AlF4- complexes with GDP to stabilize an activated state of the Galpha subunit, these results suggest that the Galpha carboxyl terminus is highly mobile in its GDP-bound state but adopts an ordered conformation upon activation by AlF4-. Guanosine Diphosphate 29-32 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 119-125 15983037-10 2005 Because AlF4- complexes with GDP to stabilize an activated state of the Galpha subunit, these results suggest that the Galpha carboxyl terminus is highly mobile in its GDP-bound state but adopts an ordered conformation upon activation by AlF4-. Guanosine Diphosphate 168-171 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 119-125 16225870-1 2005 Signaling via G-protein coupled receptors is initiated by receptor-catalyzed nucleotide exchange on Galpha subunits normally bound to GDP and Gbetagamma. Guanosine Diphosphate 134-137 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 100-106 16190775-2 2005 G proteins are stimulated by cell surface receptors (GPCR) that catalyze the exchange of GDP, bound to Galpha subunit, with GTP and can per se be the target of drugs. Guanosine Diphosphate 89-92 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 103-109 16004878-7 2005 Structural determination of the Galpha(i1)/peptide complex reveals unique changes in the Galpha switch regions predicted to enhance nucleotide exchange by creating a GDP dissociation route. Guanosine Diphosphate 166-169 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 32-38 15665133-7 2005 In the presence of Galpha(s)(GDP), the volume change associated with PLCbeta-Gbeta gamma interaction is reduced to 25 +/- 1 ml/mol. Guanosine Diphosphate 29-32 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 19-25 15007073-6 2004 A holo-G protein with a high affinity Galpha C terminus shows a specific change of the reaction rate in the GDP release and GTP uptake steps of catalysis. Guanosine Diphosphate 108-111 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 38-44 15368366-8 2004 Because the guanine nucleotide binding site is deeply buried in this cleft and those interdomain interactions are playing an important role in regulating the basal GDP/GTP nucleotide exchange rate of Galpha subunits, we studied the role of these highly conserved R and E residues in Galpha function. Guanosine Diphosphate 164-167 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 200-206 15271992-10 2004 Overall, these findings highlight a new class of activated Galpha mutants that constitutively exchange GDP for GTP and should prove valuable in studying different G protein-signaling systems. Guanosine Diphosphate 103-106 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 59-65 15007073-7 2004 We interpret the data by a sequential fit model where (i) the initial encounter between R* and the G protein occurs with the Gbetagamma subunit, and (ii) the Galpha C-terminal tail then interacts with R* to release bound GDP, thereby decreasing the affinity of R* for the Gbetagamma subunit. Guanosine Diphosphate 221-224 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 158-164 14656218-8 2004 Only the first and third GoLoco motifs within G18 are capable of interacting with Galpha subunits, and these bind with low micromolar affinity only to Galpha(i1) in the GDP-bound form, and not to Galpha(o), Galpha(q), Galpha(s) or Galpha12. Guanosine Diphosphate 169-172 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 151-157 15081806-2 2004 The modeled systems include the active and inactive forms of the wild-type Galpha(t) and three of its mutants (GDP-bound form only): F332A, A322S, and Q326A that are known to exhibit various degrees of enhancement of their basal and receptor-catalyzed rates of nucleotide exchange (150-fold, 70-fold and WT-like, respectively). Guanosine Diphosphate 111-114 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 75-81 15081806-8 2004 Taken together the results suggest a nucleotide exchange mechanism, analogous to that found in the Arf family GTPases, in which a partially activated state, achievable from a receptor-mediated action of the front to back communication device either by displacement of the C-terminal alpha(5) helix, of the N-terminal alpha(N) helix, or of the Gbetagamma subunit, could precede the dissociation of GDP from the native Galpha subunit. Guanosine Diphosphate 397-400 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 417-423 14656218-8 2004 Only the first and third GoLoco motifs within G18 are capable of interacting with Galpha subunits, and these bind with low micromolar affinity only to Galpha(i1) in the GDP-bound form, and not to Galpha(o), Galpha(q), Galpha(s) or Galpha12. Guanosine Diphosphate 169-172 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 151-157 12146960-10 2002 Site-directed spin-labeling studies showed that the N-terminus of the Galpha subunit is dynamically disordered in the GDP bound state, but adopts a structure consistent with an alpha-helix upon interaction with Gbetagamma. Guanosine Diphosphate 118-121 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 70-76 15313557-1 2004 G-protein-coupled receptors (GPCRs) activate heterotrimeric G proteins by inducing the G-protein alpha (Galpha) subunit to exchange guanosine diphosphate for guanosine triphosphate. Guanosine Diphosphate 132-153 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 104-110 15488186-2 2004 GPCR activation by an agonist promotes the exchange of GDP for GTP on the Galpha subunit of the heterotrimeric G protein. Guanosine Diphosphate 55-58 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 74-80 14609727-2 2003 Activation of receptor by agonist leads to the dissociation of GDP from Galpha of the Galphabetagamma heterotrimer, followed by the binding of GTP to Galpha and subsequent modulation of downstream effectors. Guanosine Diphosphate 63-66 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 72-78 14609727-2 2003 Activation of receptor by agonist leads to the dissociation of GDP from Galpha of the Galphabetagamma heterotrimer, followed by the binding of GTP to Galpha and subsequent modulation of downstream effectors. Guanosine Diphosphate 63-66 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 86-92 12831845-4 2003 This effect of BSA is mediated by decreasing the rate of GDP dissociation from Galpha(s) and decreasing the rate of GTP binding. Guanosine Diphosphate 57-60 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 79-85 12834345-2 2003 Thiol reactive EPR and fluorescent probes were attached to each site as local reporters of mobility and conformational changes upon activation of Galpha(i)GDP by AlF(4)(-), as well as binding to Gbetagamma. Guanosine Diphosphate 155-158 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 146-152 12719437-2 2003 Each GPR motif binds to the alpha subunit of Gi/Go (Gialpha > Goalpha) stabilizing the GDP-bound conformation of Galpha and apparently competing with Gbetagamma for GalphaGDP binding. Guanosine Diphosphate 90-93 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 116-122 12509430-7 2003 Ric-8A interacts with GDP-bound Galpha proteins, stimulates release of GDP, and forms a stable nucleotide-free transition state complex with the Galpha protein; this complex dissociates upon binding of GTP to Galpha. Guanosine Diphosphate 22-25 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 32-38 12598904-2 2003 Ligand-bound receptors catalyse GDP/GTP exchange on the G-protein alpha-subunit (Galpha), leading to alpha-GTP separation from the betagamma subunits and pathway activation. Guanosine Diphosphate 32-35 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 81-87 12598904-4 2003 Regulators of G-protein signalling (RGS proteins) are known to modulate the level and duration of ligand-induced signalling by accelerating the intrinsic GTPase activity of the Galpha subunit, and thus reformation of the inactive GDP-bound Galpha. Guanosine Diphosphate 230-233 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 177-183 12146960-11 2002 Interaction of the resulting spin-labeled Galphabetagamma with photoactivated rhodopsin, followed by rhodopsin-catalyzed GTPgammaS binding, caused the amino-terminal domain of Galpha to revert to a dynamically disordered state similar to that of the GDP-bound form. Guanosine Diphosphate 250-253 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 42-48 11583165-1 2001 Stoichiometric exchange of GTP for GDP on heterotrimeric G protein alpha (Galpha) subunits is essential to most hormone and neurotransmitter initiated signal transduction. Guanosine Diphosphate 35-38 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 74-80 11529678-0 2001 An intramolecular contact in Galpha transducin that participates in maintaining its intrinsic GDP release rate. Guanosine Diphosphate 94-97 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 29-35 11529678-2 2001 Spontaneous GDP release from Galpha can also lead to the active state, if GTP in solution binds the nucleotide binding pocket. Guanosine Diphosphate 12-15 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 29-35 11529678-3 2001 The purpose of this study is to evaluate the molecular determinants for maintaining the spontaneous GDP release rates between two Galpha subunits. Guanosine Diphosphate 100-103 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 130-136 11529678-6 2001 The C-terminal alpha4-helix, the N-terminal 56 residues and the Switch I/II regions of Galpha(t) were shown to affect the low spontaneous GDP release rate in Galpha(t). Guanosine Diphosphate 138-141 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 87-93 11529678-6 2001 The C-terminal alpha4-helix, the N-terminal 56 residues and the Switch I/II regions of Galpha(t) were shown to affect the low spontaneous GDP release rate in Galpha(t). Guanosine Diphosphate 138-141 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 158-164 11529678-8 2001 In two chimeras disrupting this interaction produced an increased spontaneous GDP release; restoring the contact present in Galpha(t) into these chimeras decreased the GDP release rate by half as compared to the original chimeras. Guanosine Diphosphate 78-81 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 124-130 11529678-8 2001 In two chimeras disrupting this interaction produced an increased spontaneous GDP release; restoring the contact present in Galpha(t) into these chimeras decreased the GDP release rate by half as compared to the original chimeras. Guanosine Diphosphate 168-171 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 124-130 11583165-4 2001 Inactivatable G protein has heretofore been thought to have become "denatured" during formation of the obligatory nucleotide-free or empty (MT) Galpha-state that is intermediary to GDP/GTP exchange at a single binding site. Guanosine Diphosphate 181-184 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 144-150 11583165-11 2001 A companion Galpha x GDP isomerization reaction is identified as the cause of the very slow spontaneous GDP dissociation that characterizes G protein nucleotide exchange and low spontaneous background activity in the absence of GPCR activation. Guanosine Diphosphate 21-24 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 12-18 11583165-11 2001 A companion Galpha x GDP isomerization reaction is identified as the cause of the very slow spontaneous GDP dissociation that characterizes G protein nucleotide exchange and low spontaneous background activity in the absence of GPCR activation. Guanosine Diphosphate 104-107 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 12-18 9892662-1 1999 Hormonal signals activate trimeric G proteins by substituting GTP for GDP bound to the G protein alpha subunit (Galpha), thereby generating two potential signaling molecules, Galpha-GTP and free Gbetagamma. Guanosine Diphosphate 70-73 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 112-118 11294858-1 2001 Regulator of G-protein signaling 3 (RGS3) enhances the intrinsic rate at which Galpha(i) and Galpha(q) hydrolyze GTP to GDP, thereby limiting the duration in which GTP-Galpha(i) and GTP-Galpha(q) can activate effectors. Guanosine Diphosphate 120-123 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 79-99 11294858-1 2001 Regulator of G-protein signaling 3 (RGS3) enhances the intrinsic rate at which Galpha(i) and Galpha(q) hydrolyze GTP to GDP, thereby limiting the duration in which GTP-Galpha(i) and GTP-Galpha(q) can activate effectors. Guanosine Diphosphate 120-123 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 79-85 11294858-1 2001 Regulator of G-protein signaling 3 (RGS3) enhances the intrinsic rate at which Galpha(i) and Galpha(q) hydrolyze GTP to GDP, thereby limiting the duration in which GTP-Galpha(i) and GTP-Galpha(q) can activate effectors. Guanosine Diphosphate 120-123 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 93-99 10611444-2 1999 At sub-anesthetic doses, halothane, isoflurane, enflurane and sevoflurane inhibit exchange of GTPgammaS for GDP bound to Galpha subunits and markedly enhance the dissociation of GTPgammaS, but fail to suppress GDPbetaS release. Guanosine Diphosphate 108-111 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 121-127 10403517-7 1999 The resulting GDP-free Galpha(q) was labile to rapid and irreversible denaturation, however (rate constant > or = 1 min(-1) at 20 degrees). Guanosine Diphosphate 14-17 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 23-29 10403517-9 1999 These findings reconcile the slowly reversible binding of GTPgammaS to Galpha(q) with the other behaviors that suggested lower affinity, and point out that events subsequent to GDP dissociation can markedly influence the rates and extents of guanine nucleotide binding to G protein alpha subunits. Guanosine Diphosphate 177-180 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 71-77 10366609-8 1999 The onset of the nonhydrolyzable GTP analog, guanylylimidodiphosphate-mediated facilitation was significantly delayed by overexpression of different GDP-bound Galpha subunits. Guanosine Diphosphate 149-152 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 159-165 9891006-7 1999 This COOH-terminal conformational change may provide the structural basis for communication between the GDP-binding site on Galpha and activated receptors, and may contribute to dissociation of activated Galpha subunit from activated receptor. Guanosine Diphosphate 104-107 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 124-130 9891006-7 1999 This COOH-terminal conformational change may provide the structural basis for communication between the GDP-binding site on Galpha and activated receptors, and may contribute to dissociation of activated Galpha subunit from activated receptor. Guanosine Diphosphate 104-107 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 204-210 11344266-1 2001 How receptors catalyze exchange of GTP for GDP bound to the Galpha subunit of trimeric G proteins is not known. Guanosine Diphosphate 43-46 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 60-66 9892662-1 1999 Hormonal signals activate trimeric G proteins by substituting GTP for GDP bound to the G protein alpha subunit (Galpha), thereby generating two potential signaling molecules, Galpha-GTP and free Gbetagamma. Guanosine Diphosphate 70-73 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 175-181 9419378-1 1998 Suramin acts as a G protein inhibitor because it inhibits the rate-limiting step in activation of the Galpha subunit, i.e., the exchange of GDP for GTP. Guanosine Diphosphate 140-143 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 102-108 9753695-2 1998 Upon stimulation by a receptor, Galpha subunits exchange GDP for GTP and dissociate from Gbetagamma, both Galpha and Gbetagamma then interact with downstream effectors. Guanosine Diphosphate 57-60 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 32-38 8611570-11 1996 These findings clearly demonstrate that G alpha h associates with a novel protein which modulates the affinity of G alpha h for guanine nucleotides and that the GDP-bound Gh is the ground state for the counterpart activator, the alpha 1-adrenoceptor, in this signaling system. Guanosine Diphosphate 161-164 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 40-47 9159128-1 1997 Hormonal signals activate trimeric G proteins by promoting exchange of GTP for GDP bound to the G protein"s alpha subunit (Galpha). Guanosine Diphosphate 79-82 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 123-129 9159128-7 1997 Although GDP release is usually the rate-limiting step in nucleotide exchange, the biochemical phenotype of this mutant alphas indicates that efficient G protein activation by receptors and other stimuli depends on the ability of Galpha to clasp tightly the GTP molecule that enters the binding site. Guanosine Diphosphate 9-12 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 230-236 8611570-4 1996 Present immunological and biochemical studies on the regulation of the GTPase cycle of G alpha h, which involves the alpha 1-adrenoceptor and 50 KDa G beta h, reveal that the 50 kDa protein is indeed a G alpha h-associated protein and down regulates functions of G alpha h. Thus, polyclonal antibody against G Beta h coimmunoprecipitates GDP-bound G alpha h but not the GDP-AlF4--bound form. Guanosine Diphosphate 338-341 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 87-94 8611570-4 1996 Present immunological and biochemical studies on the regulation of the GTPase cycle of G alpha h, which involves the alpha 1-adrenoceptor and 50 KDa G beta h, reveal that the 50 kDa protein is indeed a G alpha h-associated protein and down regulates functions of G alpha h. Thus, polyclonal antibody against G Beta h coimmunoprecipitates GDP-bound G alpha h but not the GDP-AlF4--bound form. Guanosine Diphosphate 338-341 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 202-209 8611570-4 1996 Present immunological and biochemical studies on the regulation of the GTPase cycle of G alpha h, which involves the alpha 1-adrenoceptor and 50 KDa G beta h, reveal that the 50 kDa protein is indeed a G alpha h-associated protein and down regulates functions of G alpha h. Thus, polyclonal antibody against G Beta h coimmunoprecipitates GDP-bound G alpha h but not the GDP-AlF4--bound form. Guanosine Diphosphate 338-341 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 202-209 8611570-4 1996 Present immunological and biochemical studies on the regulation of the GTPase cycle of G alpha h, which involves the alpha 1-adrenoceptor and 50 KDa G beta h, reveal that the 50 kDa protein is indeed a G alpha h-associated protein and down regulates functions of G alpha h. Thus, polyclonal antibody against G Beta h coimmunoprecipitates GDP-bound G alpha h but not the GDP-AlF4--bound form. Guanosine Diphosphate 338-341 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 202-209 8611570-6 1996 Supporting this notion, G beta h accelerated GTP gamma S release from G alpha h and changes the affinity of G alpha h from GTP to GDP. Guanosine Diphosphate 130-133 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 108-115 8939752-0 1996 Structure of the GDP-Pi complex of Gly203-->Ala gialpha1: a mimic of the ternary product complex of galpha-catalyzed GTP hydrolysis. Guanosine Diphosphate 17-20 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 103-109 8039765-3 1994 The switch turns on when GTP binds, in exchange for prebound GDP, to the alpha-subunit (G alpha), whereas it turns off upon the GTP hydrolysis due to the G alpha GTPase activity. Guanosine Diphosphate 61-64 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 73-95 31930311-4 2020 Classical G-protein coupled receptor (GPCR)-like proteins exist in plants and interact with the Galpha proteins, but their ability to activate Galpha by facilitating GDP to GTP exchange has not been demonstrated. Guanosine Diphosphate 166-169 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 96-102 34769272-2 2021 According to the classic G protein paradigm established in animal models, the bound guanine nucleotide on a Galpha subunit, either guanosine diphosphate (GDP) or guanosine triphosphate (GTP) determines the inactive or active mode, respectively. Guanosine Diphosphate 131-152 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 108-114 34769272-2 2021 According to the classic G protein paradigm established in animal models, the bound guanine nucleotide on a Galpha subunit, either guanosine diphosphate (GDP) or guanosine triphosphate (GTP) determines the inactive or active mode, respectively. Guanosine Diphosphate 154-157 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 108-114 34445383-5 2021 The G-protein is activated when Galpha releases GDP and binds to GTP, and the relationships with the GPCR and the downstream signal are also achieved by Galpha coupling. Guanosine Diphosphate 48-51 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 32-38 34445383-5 2021 The G-protein is activated when Galpha releases GDP and binds to GTP, and the relationships with the GPCR and the downstream signal are also achieved by Galpha coupling. Guanosine Diphosphate 48-51 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 153-159 34445383-7 2021 The existence of a self-activated Galpha in plants makes it unnecessary for the canonical GPCR to activate the G-protein by exchanging GDP with GTP. Guanosine Diphosphate 135-138 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 34-40 33876404-3 2021 Receptor coupling to G-proteins promotes the GDP/GTP exchange on Galpha subunits. Guanosine Diphosphate 45-48 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 65-71 32786510-0 2020 GDP Release from the Open Conformation of Galpha Requires Allosteric Signaling from the Agonist-Bound Human beta2 Adrenergic Receptor. Guanosine Diphosphate 0-3 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 42-48 32786510-7 2020 Interestingly, while GDP remained bound with the Galpha-protein for the two inactive systems (antagonist-bound and apo form), GDP dissociated from the open conformation of the Galpha protein for the agonist activated system. Guanosine Diphosphate 21-24 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 49-55 32786510-7 2020 Interestingly, while GDP remained bound with the Galpha-protein for the two inactive systems (antagonist-bound and apo form), GDP dissociated from the open conformation of the Galpha protein for the agonist activated system. Guanosine Diphosphate 126-129 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 176-182 32786510-9 2020 Based on residue interaction network analysis, we observed that engagement of agonist-bound beta2AR with an alpha5 helix of Galpha is essential for the GDP release and the residues in the phosphate-binding loop, alpha1 helix, and alpha5 helix play very important roles in the GDP release. Guanosine Diphosphate 152-155 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 124-130 32786510-9 2020 Based on residue interaction network analysis, we observed that engagement of agonist-bound beta2AR with an alpha5 helix of Galpha is essential for the GDP release and the residues in the phosphate-binding loop, alpha1 helix, and alpha5 helix play very important roles in the GDP release. Guanosine Diphosphate 276-279 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 124-130 32662237-3 2020 In this line, we present a method which may identify potential hits, with agonistic and/or antagonistic properties on GPCR receptors, integrating the knowledge on signaling events triggered by receptor activation (GPCRs binding to Galpha,beta,gamma proteins, and activating Galpha , exchanging GDP for GTP, leading to a decreased affinity of the Galpha for the GPCR). Guanosine Diphosphate 294-297 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 231-237 31930311-4 2020 Classical G-protein coupled receptor (GPCR)-like proteins exist in plants and interact with the Galpha proteins, but their ability to activate Galpha by facilitating GDP to GTP exchange has not been demonstrated. Guanosine Diphosphate 166-169 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 143-149 31967346-4 2020 Interaction of a conserved concave surface of its core domain with the Galpha C-terminus appears to mediate formation of the initial Ric-8A/GalphaGDP intermediate, followed by the formation of a stable nucleotide-free complex. Guanosine Diphosphate 140-149 succinate-CoA ligase GDP/ADP-forming subunit alpha Homo sapiens 71-77