PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7721742-8 1995 The stimulation in GDP dissociation inhibitor-treated membranes could be partially recovered by the addition of recombinant Rho proteins (RhoA, Rac1, CDC42Hs). Guanosine Diphosphate 19-22 cell division cycle 42 Homo sapiens 150-157 8798610-0 1996 Phosphatidylinositol 4,5-bisphosphate provides an alternative to guanine nucleotide exchange factors by stimulating the dissociation of GDP from Cdc42Hs. Guanosine Diphosphate 136-139 cell division cycle 42 Homo sapiens 145-152 8798610-4 1996 Among a variety of lipids tested, only PIP2 was able to stimulate GDP release from Cdc42Hs in a dose-dependent manner, with a half-maximum effect at approximately 50 microM. Guanosine Diphosphate 66-69 cell division cycle 42 Homo sapiens 83-90 8798610-5 1996 Unlike the Dbl oncoprotein, which requires the presence of (free) guanine nucleotide in the medium to replace the GDP bound to Cdc42Hs, PIP2 stimulates GDP release from Cdc42Hs in the absence of free guanine nucleotide. Guanosine Diphosphate 152-155 cell division cycle 42 Homo sapiens 169-176 8626553-5 1996 The GDI-induced quenching is only observed when Mant-GDP is bound to Spodoptera frugiperda-expressed Cdc42Hs and is not detected when the Mant nucleotide is bound to Escherichia coli-expressed Cdc42Hs and thus shows the same requirement for isoprenylated GTP-binding protein as that observed when assaying GDI activity. Guanosine Diphosphate 53-56 cell division cycle 42 Homo sapiens 101-108 8626553-5 1996 The GDI-induced quenching is only observed when Mant-GDP is bound to Spodoptera frugiperda-expressed Cdc42Hs and is not detected when the Mant nucleotide is bound to Escherichia coli-expressed Cdc42Hs and thus shows the same requirement for isoprenylated GTP-binding protein as that observed when assaying GDI activity. Guanosine Diphosphate 53-56 cell division cycle 42 Homo sapiens 193-200 8626553-7 1996 Thus, the GDI-induced quenching of Mant-GDP provides a direct read-out for the binding of the GDI to Cdc42Hs. Guanosine Diphosphate 40-43 cell division cycle 42 Homo sapiens 101-108 8626553-8 1996 Titration profiles of the GDI-induced quenching of the Mant-GDP fluorescence are saturable and are well fit to a simple 1:1 binding model for Cdc42Hs-GDI interactions with an apparent Kd value of 30 nM. Guanosine Diphosphate 60-63 cell division cycle 42 Homo sapiens 142-149 8626553-10 1996 These results suggest that the GDI can bind to the GDP-bound and GTP-bound forms of Cdc42Hs equally well. Guanosine Diphosphate 51-54 cell division cycle 42 Homo sapiens 84-91 8605211-3 1996 We find that the sNBD-labeled Cdc42Hs undergoes a fluorescence enhancement at 545 nm when Cdc42Hs exchanges bound GDP for GTP. Guanosine Diphosphate 114-117 cell division cycle 42 Homo sapiens 30-37 8605211-3 1996 We find that the sNBD-labeled Cdc42Hs undergoes a fluorescence enhancement at 545 nm when Cdc42Hs exchanges bound GDP for GTP. Guanosine Diphosphate 114-117 cell division cycle 42 Homo sapiens 90-97 8240325-2 1993 The GDI protein inhibited the dissociation of GDP from G25K. Guanosine Diphosphate 46-49 cell division cycle 42 Homo sapiens 55-59 7918454-5 1994 The exchange of mant-dGDP for GDP bound to Cdc42Hs, as read-out either by the enhancement of the mant fluorescence or by energy transfer, is inhibited by physiological (mM) Mg2+ concentrations and correlates exactly to the rate of [3H]GDP exchange observed in filter-binding assays. Guanosine Diphosphate 22-25 cell division cycle 42 Homo sapiens 43-50 7918454-5 1994 The exchange of mant-dGDP for GDP bound to Cdc42Hs, as read-out either by the enhancement of the mant fluorescence or by energy transfer, is inhibited by physiological (mM) Mg2+ concentrations and correlates exactly to the rate of [3H]GDP exchange observed in filter-binding assays. Guanosine Diphosphate 30-33 cell division cycle 42 Homo sapiens 43-50 7918454-7 1994 A second fluorescence read-out for the nucleotide-bound state of Cdc42Hs involves the measurements of intrinsic fluorescence of a single tryptophan residue (W97) which is highly sensitive to whether GDP or GTP is bound in the nucleotide pocket. Guanosine Diphosphate 199-202 cell division cycle 42 Homo sapiens 65-72 7918454-8 1994 The hydrolysis of GTP to GDP by Cdc42Hs results in an approximately 30% enhancement of the protein fluorescence. Guanosine Diphosphate 25-28 cell division cycle 42 Homo sapiens 32-39 7476460-0 1995 Solubilization of Cdc42Hs from membranes by Rho-GDP dissociation inhibitor. Guanosine Diphosphate 48-51 cell division cycle 42 Homo sapiens 18-25 8276860-4 1994 We show here that Dbl specifically complexes with the GDP-bound forms of CDC42Hs and RhoA, but not Rac1 or TC10, and that this specificity correlates with the ability of Dbl to act as a GDP-releasing factor. Guanosine Diphosphate 54-57 cell division cycle 42 Homo sapiens 73-80 8276860-6 1994 Finally, the Dbl domain itself, when expressed and purified as a recombinant protein, was shown to stimulate GDP dissociation from purified, recombinant CDC42Hs. Guanosine Diphosphate 109-112 cell division cycle 42 Homo sapiens 153-160 7512369-0 1993 Identification of a novel protein with GDP dissociation inhibitor activity for the ras-like proteins CDC42Hs and rac I. Guanosine Diphosphate 39-42 cell division cycle 42 Homo sapiens 101-118 8240325-3 1993 G25K and the GDI protein form a heterodimer and remain associated with either GDP or GTP gamma S bound. Guanosine Diphosphate 78-81 cell division cycle 42 Homo sapiens 0-4 8240325-4 1993 The GDI protein inhibited carboxyl methylation of G25K in the presence of magnesium and GDP. Guanosine Diphosphate 88-91 cell division cycle 42 Homo sapiens 50-54 8240325-5 1993 The GDI protein appears to be an important regulator of G25K methylation by blocking methylation of G25K in the inactive GDP-bound conformation. Guanosine Diphosphate 121-124 cell division cycle 42 Homo sapiens 56-60 8240325-5 1993 The GDI protein appears to be an important regulator of G25K methylation by blocking methylation of G25K in the inactive GDP-bound conformation. Guanosine Diphosphate 121-124 cell division cycle 42 Homo sapiens 100-104 1429634-11 1992 This effect by the GDI protein is observed whether the membrane-associated CDC42Hs is preincubated with GDP, GTP gamma S, or no guanine nucleotides, and occurs over a similar concentration range as that necessary for the inhibition of the intrinsic GDP dissociation. Guanosine Diphosphate 104-107 cell division cycle 42 Homo sapiens 75-82 1429634-2 1992 In attempting to isolate and biochemically characterize mammalian proteins capable of regulating various activities of CDC42Hs, we have identified an activity in bovine brain cytosol which effectively inhibits the dissociation of [3H]GDP from the platelet- or the Spodoptera frugiperda-expressed CDC42Hs protein. Guanosine Diphosphate 234-237 cell division cycle 42 Homo sapiens 119-126 1429634-2 1992 In attempting to isolate and biochemically characterize mammalian proteins capable of regulating various activities of CDC42Hs, we have identified an activity in bovine brain cytosol which effectively inhibits the dissociation of [3H]GDP from the platelet- or the Spodoptera frugiperda-expressed CDC42Hs protein. Guanosine Diphosphate 234-237 cell division cycle 42 Homo sapiens 296-303 1429634-7 1992 These findings suggest either that a common regulatory protein (GDI) is capable of inhibiting GDP dissociation from the rho and CDC42Hs proteins or that these two GTP-binding proteins interact with GDI proteins of very similar structure. Guanosine Diphosphate 94-97 cell division cycle 42 Homo sapiens 128-135 1429634-11 1992 This effect by the GDI protein is observed whether the membrane-associated CDC42Hs is preincubated with GDP, GTP gamma S, or no guanine nucleotides, and occurs over a similar concentration range as that necessary for the inhibition of the intrinsic GDP dissociation. Guanosine Diphosphate 249-252 cell division cycle 42 Homo sapiens 75-82 35215978-4 2022 Vav proteins have guanine exchange activity in converting GDP to GTP on proteins such as Rac1, Cdc42 and RhoA to stimulate intracellular signaling pathways. Guanosine Diphosphate 58-61 cell division cycle 42 Homo sapiens 95-100 1956381-4 1991 Here we show that dbl specifically catalyses the dissociation of GDP from CDC42Hs and thereby qualifies as a highly selective guanine nucleotide exchange factor for the GTP-binding protein. Guanosine Diphosphate 65-68 cell division cycle 42 Homo sapiens 74-81 1439791-0 1992 A GDP dissociation inhibitor that serves as a GTPase inhibitor for the Ras-like protein CDC42Hs. Guanosine Diphosphate 2-5 cell division cycle 42 Homo sapiens 88-95 35583642-8 2022 The typical RHO family members include the classical RHOA, RAC1 and CDC42 proteins, which cycle between an active GTP-bound and inactive GDP-bound conformation, under the coordinated action of three types of regulators: GEFs, GAPs and GDIs. Guanosine Diphosphate 137-140 cell division cycle 42 Homo sapiens 68-73 31474712-5 2019 Phosphorylation of IQGAP1 on serine (Ser)-1443, a site recognized by protein kinase Cepsilon (PKCepsilon), inhibited the interaction of GDP-bound Rab27a with IQGAP1 in a Cdc42-independent manner. Guanosine Diphosphate 136-139 cell division cycle 42 Homo sapiens 170-175 31330900-0 2019 The Intrinsic GDP/GTP Exchange Activities of Cdc42 and Rac1 Are Critical Determinants for Their Specific Effects on Mobilization of the Actin Filament System. Guanosine Diphosphate 14-17 cell division cycle 42 Homo sapiens 45-50 33347888-5 2021 The G2 loop and Switch I at the effector lobe of the catalytic domain exhibit large conformational changes in both the GDP- and GTP-bound systems, but in the GTP-bound Cdc42 the Switch I interactions with GTP are retained. Guanosine Diphosphate 119-122 cell division cycle 42 Homo sapiens 168-173 33347888-12 2021 We propose that the differences are due to a network of hydrogen bonds that gets disrupted when Cdc42 is bound to GDP, a disruption that does not exist in other Rho GTP-ases. Guanosine Diphosphate 114-117 cell division cycle 42 Homo sapiens 96-101 30714195-0 2019 Dissociation mechanism of GDP from Cdc42 via DOCK9 revealed by molecular dynamics simulations. Guanosine Diphosphate 26-29 cell division cycle 42 Homo sapiens 35-40 30714195-6 2019 Molecular dynamics (MD) simulations and molecular mechanics-Poisson-Boltzmann surface area (MM-PBSA) calculations were employed to investigate the central step of the activation of Cdc42: the dissociation mechanism of GDP from Cdc42 via DOCK9. Guanosine Diphosphate 218-221 cell division cycle 42 Homo sapiens 181-186 30714195-6 2019 Molecular dynamics (MD) simulations and molecular mechanics-Poisson-Boltzmann surface area (MM-PBSA) calculations were employed to investigate the central step of the activation of Cdc42: the dissociation mechanism of GDP from Cdc42 via DOCK9. Guanosine Diphosphate 218-221 cell division cycle 42 Homo sapiens 227-232 30714195-8 2019 In the GDP dissociation process, the Mg2+ ion leave first to result in a suitable conformation of Cdc42 for following DOCK9 binding to. Guanosine Diphosphate 7-10 cell division cycle 42 Homo sapiens 98-103 30714195-9 2019 When DOCK9 binds to Cdc42, it changes the orientations of residues Lys16, Thr17, Cys18 and Phe28 of Cdc42 to weaken the interactions between Cdc42 and GDP to release GDP. Guanosine Diphosphate 151-154 cell division cycle 42 Homo sapiens 20-25 30714195-9 2019 When DOCK9 binds to Cdc42, it changes the orientations of residues Lys16, Thr17, Cys18 and Phe28 of Cdc42 to weaken the interactions between Cdc42 and GDP to release GDP. Guanosine Diphosphate 151-154 cell division cycle 42 Homo sapiens 100-105 30714195-9 2019 When DOCK9 binds to Cdc42, it changes the orientations of residues Lys16, Thr17, Cys18 and Phe28 of Cdc42 to weaken the interactions between Cdc42 and GDP to release GDP. Guanosine Diphosphate 151-154 cell division cycle 42 Homo sapiens 100-105 30714195-9 2019 When DOCK9 binds to Cdc42, it changes the orientations of residues Lys16, Thr17, Cys18 and Phe28 of Cdc42 to weaken the interactions between Cdc42 and GDP to release GDP. Guanosine Diphosphate 166-169 cell division cycle 42 Homo sapiens 20-25 30714195-9 2019 When DOCK9 binds to Cdc42, it changes the orientations of residues Lys16, Thr17, Cys18 and Phe28 of Cdc42 to weaken the interactions between Cdc42 and GDP to release GDP. Guanosine Diphosphate 166-169 cell division cycle 42 Homo sapiens 100-105 30714195-9 2019 When DOCK9 binds to Cdc42, it changes the orientations of residues Lys16, Thr17, Cys18 and Phe28 of Cdc42 to weaken the interactions between Cdc42 and GDP to release GDP. Guanosine Diphosphate 166-169 cell division cycle 42 Homo sapiens 100-105 30714195-10 2019 This study first elucidates the dissociation mechanism of GDP from Cdc42 via DOCK9 and identifies the essential residues of Cdc42 in this process. Guanosine Diphosphate 58-61 cell division cycle 42 Homo sapiens 67-72 30714195-10 2019 This study first elucidates the dissociation mechanism of GDP from Cdc42 via DOCK9 and identifies the essential residues of Cdc42 in this process. Guanosine Diphosphate 58-61 cell division cycle 42 Homo sapiens 124-129 30754684-4 2019 Cdc42 switches from inactive guanosine diphosphate (GDP)-bound to active GTP-bound though guanine-nucleotide-exchange factors (GEFs), results in activation of signaling cascades that regulate various cellular processes such as cytoskeletal changes, proliferation and polarity establishment. Guanosine Diphosphate 29-50 cell division cycle 42 Homo sapiens 0-5 30754684-4 2019 Cdc42 switches from inactive guanosine diphosphate (GDP)-bound to active GTP-bound though guanine-nucleotide-exchange factors (GEFs), results in activation of signaling cascades that regulate various cellular processes such as cytoskeletal changes, proliferation and polarity establishment. Guanosine Diphosphate 52-55 cell division cycle 42 Homo sapiens 0-5 30558664-1 2018 BACKGROUND: FGD4 (Frabin) is an F-actin binding protein with GTP/GDP exchange activity specific for CDC42. Guanosine Diphosphate 65-68 cell division cycle 42 Homo sapiens 100-105 25305482-2 2014 RacGTPase-activating protein 1 (RacGAP1) plays an important role during GTP hydrolysis to GDP in Rac1 and CDC42 protein and has been demonstrated to be upregulated in several cancers, including HCC. Guanosine Diphosphate 90-93 cell division cycle 42 Homo sapiens 106-111 26542736-5 2016 We applied amide hydrogen/deuterium exchange coupled with liquid chromatography mass spectrometry (HDXMS) to investigate the dynamic changes of apo-Cdc42 after GDP, GTP and GMP-PCP binding. Guanosine Diphosphate 160-163 cell division cycle 42 Homo sapiens 148-153 26542736-9 2016 Comparing the deuteration levels in three activation states of apo-Cdc42, Cdc42-GDP and Cdc42-GMP-PCP, the apo-Cdc42 has the most flexible structure, which can be stabilized by guanine nucleotide binding. Guanosine Diphosphate 80-83 cell division cycle 42 Homo sapiens 74-79 26542736-9 2016 Comparing the deuteration levels in three activation states of apo-Cdc42, Cdc42-GDP and Cdc42-GMP-PCP, the apo-Cdc42 has the most flexible structure, which can be stabilized by guanine nucleotide binding. Guanosine Diphosphate 80-83 cell division cycle 42 Homo sapiens 74-79 26542736-9 2016 Comparing the deuteration levels in three activation states of apo-Cdc42, Cdc42-GDP and Cdc42-GMP-PCP, the apo-Cdc42 has the most flexible structure, which can be stabilized by guanine nucleotide binding. Guanosine Diphosphate 80-83 cell division cycle 42 Homo sapiens 74-79 27628050-3 2016 The typical Rho family members, including RhoA, Rac1 and Cdc42, cycle between an active GTP-bound and inactive GDP-bound conformation, and are regulated by GEFs, GAPs and GDIs, whereas atypical Rho family members have amino acid substitutions that alter their ability to interact with GTP/GDP and hence are regulated by different mechanisms. Guanosine Diphosphate 111-114 cell division cycle 42 Homo sapiens 57-62 27628050-3 2016 The typical Rho family members, including RhoA, Rac1 and Cdc42, cycle between an active GTP-bound and inactive GDP-bound conformation, and are regulated by GEFs, GAPs and GDIs, whereas atypical Rho family members have amino acid substitutions that alter their ability to interact with GTP/GDP and hence are regulated by different mechanisms. Guanosine Diphosphate 289-292 cell division cycle 42 Homo sapiens 57-62 26911374-1 2016 Among small GTPases from the Rho family, Cdc42, RAC, and Rho are well known to mediate a large variety of cellular processes linked with cancer biology through their ability to cycle between an inactive (GDP-bound) and an active (GTP-bound) state. Guanosine Diphosphate 204-207 cell division cycle 42 Homo sapiens 41-46 27010858-2 2016 ARHGAP10 is a member of RhoGAP proteins and inactivates Cdc42 by converting GTP-bound form to GDP-bound form. Guanosine Diphosphate 94-97 cell division cycle 42 Homo sapiens 56-61 24347642-1 2014 The Cdc42- and Rac-interactive binding motif (CRIB) of coronin binds to Rho GTPases with a preference for GDP-loaded Rac. Guanosine Diphosphate 106-109 cell division cycle 42 Homo sapiens 4-9 19890090-4 2010 The purpose of this article is to provide an overview of current understanding of the identity of small G proteins (e.g., Cdc42, Rac1, and ARF-6) and their corresponding regulatory factors (e.g., GDP/GTP-exchange factors, GDP-dissociation inhibitors) in the pancreatic beta-cell. Guanosine Diphosphate 196-199 cell division cycle 42 Homo sapiens 122-127 24286829-7 2013 Surprisingly, Cdc42-GDP is not inactive, but in the absence of Gic1 directly interacts with septin filaments resulting in their disassembly. Guanosine Diphosphate 20-23 cell division cycle 42 Homo sapiens 14-19 24067935-1 2013 Rho GTPase activating protein 26 (ARHGAP26) is a negative regulator of the Rho family that converts the small G proteins RhoA and Cdc42 to their inactive GDP-bound forms. Guanosine Diphosphate 154-157 cell division cycle 42 Homo sapiens 130-135 20028975-1 2010 Cdc42 cycling through GTP/GDP states is critical for its function in the second/granule mobilization phase of insulin granule exocytosis in pancreatic islet beta cells, although the identities of the Cdc42 cycling proteins involved remain incomplete. Guanosine Diphosphate 26-29 cell division cycle 42 Homo sapiens 0-5 24100016-3 2013 We found that IQGAP1 interacts with GDP-bound Rab27a when it forms a complex with GTP-bound Cdc42. Guanosine Diphosphate 36-39 cell division cycle 42 Homo sapiens 92-97 22705156-2 2012 We observe WNT-3a to differentially regulate small GTPase activity in platelets, promoting the GDP-bound form of Rap1b to inhibit integrin-alpha(IIb)beta(3) adhesion, while concomitantly increasing Cdc42 and Rac1-GTP levels thereby disrupting normal platelet spreading. Guanosine Diphosphate 95-98 cell division cycle 42 Homo sapiens 198-203 21549598-4 2011 Studies with a panel of five sensor analogs revealed a derivative that exhibits a 32-fold increase in fluorescence intensity in the presence of activated Cdc42 compared to incubation with the inactive GDP-bound form of the protein. Guanosine Diphosphate 201-204 cell division cycle 42 Homo sapiens 154-159 19745154-3 2009 Through structural analysis of DOCK9-Cdc42 complexes, we identify a nucleotide sensor within the alpha10 helix of the DHR2 domain that contributes to release of guanine diphosphate (GDP) and then to discharge of the activated GTP-bound Cdc42. Guanosine Diphosphate 182-185 cell division cycle 42 Homo sapiens 37-42 19745154-3 2009 Through structural analysis of DOCK9-Cdc42 complexes, we identify a nucleotide sensor within the alpha10 helix of the DHR2 domain that contributes to release of guanine diphosphate (GDP) and then to discharge of the activated GTP-bound Cdc42. Guanosine Diphosphate 182-185 cell division cycle 42 Homo sapiens 236-241 19581296-5 2009 Despite having similar affinities for the signaling-inactive (GDP-bound) and signaling-active (GTP-bound) forms of Cdc42 in solution, we show that when RhoGDI interacts with Cdc42 along the membrane surface, it has a much higher affinity for GDP-bound Cdc42 compared with its GTP-bound counterpart. Guanosine Diphosphate 242-245 cell division cycle 42 Homo sapiens 115-120 19581296-5 2009 Despite having similar affinities for the signaling-inactive (GDP-bound) and signaling-active (GTP-bound) forms of Cdc42 in solution, we show that when RhoGDI interacts with Cdc42 along the membrane surface, it has a much higher affinity for GDP-bound Cdc42 compared with its GTP-bound counterpart. Guanosine Diphosphate 242-245 cell division cycle 42 Homo sapiens 174-179 19581296-5 2009 Despite having similar affinities for the signaling-inactive (GDP-bound) and signaling-active (GTP-bound) forms of Cdc42 in solution, we show that when RhoGDI interacts with Cdc42 along the membrane surface, it has a much higher affinity for GDP-bound Cdc42 compared with its GTP-bound counterpart. Guanosine Diphosphate 242-245 cell division cycle 42 Homo sapiens 174-179 19581296-8 2009 These findings lead us to propose a new model for how RhoGDI influences the ability of Cdc42 to move between membranes and the cytosol, which highlights the role of the membrane in helping RhoGDI to distinguish between the GDP- and GTP-bound forms of Cdc42 and holds important implications for how it functions as a key regulator of the cellular localization and signaling activities of this GTPase. Guanosine Diphosphate 223-226 cell division cycle 42 Homo sapiens 87-92 19581296-8 2009 These findings lead us to propose a new model for how RhoGDI influences the ability of Cdc42 to move between membranes and the cytosol, which highlights the role of the membrane in helping RhoGDI to distinguish between the GDP- and GTP-bound forms of Cdc42 and holds important implications for how it functions as a key regulator of the cellular localization and signaling activities of this GTPase. Guanosine Diphosphate 223-226 cell division cycle 42 Homo sapiens 251-256 19356586-5 2009 The selectivity in nucleotide exchange kinetics for GDP over GTP is even more pronounced when a Cdc42 mutant, F28L, is used, which is characterised by fast intrinsic dissociation of nucleotides. Guanosine Diphosphate 52-55 cell division cycle 42 Homo sapiens 96-101 19221465-3 2009 The cellular stress resulting from the GTP/GDP depletion leads to the activation of the small GTPase Cdc42 and the remodeling of actin, which are crucial events in the transmission of the MPA-mediated necrotic signal. Guanosine Diphosphate 43-46 cell division cycle 42 Homo sapiens 101-106 19356586-8 2009 The higher exchange activity of ITSN1L towards the GDP-bound conformation of Cdc42 could represent an evolutionary adaptation of this GEF that ensures nucleotide exchange towards the formation of the signalling-active GTP-bound form of Cdc42 and avoids dissociation of the active complex. Guanosine Diphosphate 51-54 cell division cycle 42 Homo sapiens 77-82 19356586-8 2009 The higher exchange activity of ITSN1L towards the GDP-bound conformation of Cdc42 could represent an evolutionary adaptation of this GEF that ensures nucleotide exchange towards the formation of the signalling-active GTP-bound form of Cdc42 and avoids dissociation of the active complex. Guanosine Diphosphate 51-54 cell division cycle 42 Homo sapiens 236-241 18728185-3 2008 We fused the Rho family GTPase Cdc42 in its GDP-bound form to the photosensory domain of phytochrome B (PhyB) and fused the Cdc42 effector, the Wiskott-Aldrich Syndrome Protein (WASP), to the light-dependent PhyB-binding domain of phytochrome interacting factor 3 (Pif3). Guanosine Diphosphate 44-47 cell division cycle 42 Homo sapiens 31-36 18558478-3 2008 The activation of Cdc42 in response to upstream signals is mediated by guanine nucleotide exchange factors (GEFs), which converse GDP-bound inactive form to the GTP-bound active form of Cdc42. Guanosine Diphosphate 130-133 cell division cycle 42 Homo sapiens 18-23 18558478-3 2008 The activation of Cdc42 in response to upstream signals is mediated by guanine nucleotide exchange factors (GEFs), which converse GDP-bound inactive form to the GTP-bound active form of Cdc42. Guanosine Diphosphate 130-133 cell division cycle 42 Homo sapiens 186-191 18348980-3 2008 Here we describe the high resolution x-ray crystal structure for Cdc42 bound to the GTP analog guanylyl beta,gamma-methylene-diphosphonate (GMP-PCP) (i.e. the presumed signaling-active state) and show that it is virtually identical to the structures for the signaling-inactive, GDP-bound form of the protein, contrary to what has been reported for Ras and other G-proteins. Guanosine Diphosphate 278-281 cell division cycle 42 Homo sapiens 65-70 18348980-4 2008 Especially surprising was that the GMP-PCP- and GDP-bound forms of Cdc42 did not show detectable differences in their Switch I and Switch II loops. Guanosine Diphosphate 48-51 cell division cycle 42 Homo sapiens 67-72 18348980-7 2008 An examination of the available structures for Cdc42 complexed to different effector proteins, versus the x-ray crystal structure for GMP-PCP-bound Cdc42, provides a possible explanation for how effectors can distinguish between the GTP- and GDP-bound forms of this G-protein and ensure that the necessary conformational changes for signal propagation occur. Guanosine Diphosphate 242-245 cell division cycle 42 Homo sapiens 47-52 18348980-7 2008 An examination of the available structures for Cdc42 complexed to different effector proteins, versus the x-ray crystal structure for GMP-PCP-bound Cdc42, provides a possible explanation for how effectors can distinguish between the GTP- and GDP-bound forms of this G-protein and ensure that the necessary conformational changes for signal propagation occur. Guanosine Diphosphate 242-245 cell division cycle 42 Homo sapiens 148-153 16101281-3 2005 This interaction is thought to affect the localization of PAK, as well as increased GTP/GDP exchange of Rac and Cdc42. Guanosine Diphosphate 88-91 cell division cycle 42 Homo sapiens 112-117 16190977-1 2005 Small GTP-binding proteins of the Rho/Rac/Cdc42 family combine their GDP/GTP cycle, regulated by guanine nucleotide-exchange factors and GTPase-activating proteins, to a cytosol/membrane cycle, regulated by guanine nucleotide dissociation inhibitors (rhoGDIs). Guanosine Diphosphate 69-72 cell division cycle 42 Homo sapiens 42-47 17145773-6 2007 Deletion of the C-terminal tail did not constitutively activate Asef2 as predicted; rather, a conserved C-terminal segment was required for augmented Cdc42 GDP/GTP exchange. Guanosine Diphosphate 156-159 cell division cycle 42 Homo sapiens 150-155 16998826-1 2006 The Rho GTPases-Rho, Rac and Cdc42-act as molecular switches, cycling between an active GTP-bound state and an inactive GDP-bound state, to regulate the actin cytoskeleton. Guanosine Diphosphate 120-123 cell division cycle 42 Homo sapiens 29-34 16337026-1 2006 Alpha and betaPIX belong to the group of guanine nucleotide exchange factors (GEFs) that mediate activation of members of the Rho GTPase family, in particular Rac1 and Cdc42, by stimulating the exchange of GDP for GTP. Guanosine Diphosphate 206-209 cell division cycle 42 Homo sapiens 168-173 16489751-1 2006 Cdc42Hs(F28L) is a single-point mutant of Cdc42Hs, a member of the Ras superfamily of GTP-binding proteins, that facilitates cellular transformation brought about by an increased rate of cycling between GTP and GDP [Lin, R., et al. Guanosine Diphosphate 211-214 cell division cycle 42 Homo sapiens 0-5 16489751-1 2006 Cdc42Hs(F28L) is a single-point mutant of Cdc42Hs, a member of the Ras superfamily of GTP-binding proteins, that facilitates cellular transformation brought about by an increased rate of cycling between GTP and GDP [Lin, R., et al. Guanosine Diphosphate 211-214 cell division cycle 42 Homo sapiens 0-7 16489751-5 2006 Dynamics studies of Cdc42Hs(F28L)-GDP have shown increased flexibility for several residues at the nucleotide-binding site [Adams, P. D., et al. Guanosine Diphosphate 34-37 cell division cycle 42 Homo sapiens 20-27 16489751-7 2006 The solution structure of Cdc42Hs-GDP (wild type) has previously been determined by NMR spectroscopy [Feltham, J. L., et al. Guanosine Diphosphate 34-37 cell division cycle 42 Homo sapiens 26-33 16489751-9 2006 Here, we describe the solution structure of Cdc42Hs(F28L)-GDP, which provides insight into the structural basis for the change in affinity for GDP. Guanosine Diphosphate 58-61 cell division cycle 42 Homo sapiens 44-51 16489751-9 2006 Here, we describe the solution structure of Cdc42Hs(F28L)-GDP, which provides insight into the structural basis for the change in affinity for GDP. Guanosine Diphosphate 143-146 cell division cycle 42 Homo sapiens 44-51 16489751-11 2006 The overall structure of Cdc42Hs(F28L)-GDP is very similar to that of wild-type Cdc42Hs, consisting of a centrally located six-stranded beta-sheet structure surrounding the C-terminal alpha-helix [Feltham, J. L., et al. Guanosine Diphosphate 39-42 cell division cycle 42 Homo sapiens 25-32 16489751-11 2006 The overall structure of Cdc42Hs(F28L)-GDP is very similar to that of wild-type Cdc42Hs, consisting of a centrally located six-stranded beta-sheet structure surrounding the C-terminal alpha-helix [Feltham, J. L., et al. Guanosine Diphosphate 39-42 cell division cycle 42 Homo sapiens 80-87 16489751-14 2006 Although the structure of Cdc42Hs(F28L)-GDP is very similar to that of the wild type, interactions with the nucleotide and hydrogen bonding within the nucleotide binding site are altered, and the region surrounding L28 is substantially more disordered. Guanosine Diphosphate 40-43 cell division cycle 42 Homo sapiens 26-33 16201754-2 2005 Guanine nucleotide exchange factors of the Dbl family activate Cdc42 and other Rho GTPases by catalyzing the removal of bound GDP, allowing for GTP loading, and subsequent effector recognition ultimately leading to downstream signaling events. Guanosine Diphosphate 126-129 cell division cycle 42 Homo sapiens 63-68 11883956-0 2002 Probing the binding states of GDP to Cdc42 using urea interaction. Guanosine Diphosphate 30-33 cell division cycle 42 Homo sapiens 37-42 15649357-5 2005 RESULTS: We show that the binding of activated Cdc42 to the Cool-2 dimer markedly enhances its ability to associate with GDP bound Rac1, resulting in a significant activation of Rac-GEF activity. Guanosine Diphosphate 121-124 cell division cycle 42 Homo sapiens 47-52 14973186-2 2004 We show that three guanosine 5"-triphosphate analogs with BODIPY fluorophores coupled via the gamma phosphate bind to the GTPases Cdc42, Rac1, RhoA, and Ras and displace guanosine 5"-diphosphate with high intrinsic exchange rates in the presence of Mg(2+) ions, thereby acting as synthetic, low molecular weight guanine nucleotide exchange factors. Guanosine Diphosphate 170-194 cell division cycle 42 Homo sapiens 130-135 12760905-6 2003 Moreover, expression of the constitutively active form of Cdc42 (Q61L) inhibited glucose-stimulated insulin secretion, whereas the dominant negative form (T17N) was without effect, suggesting that glucose-stimulated insulin secretion requires Cdc42 cycling to the GDP-bound state. Guanosine Diphosphate 264-267 cell division cycle 42 Homo sapiens 58-63 12432077-5 2002 Importantly, we have identified several novel homologues of DOCK180 that possess this domain and found that many of them directly bind to and exchange GDP for GTP both in vitro and in vivo on either Rac or another Rho-family member, Cdc42. Guanosine Diphosphate 151-154 cell division cycle 42 Homo sapiens 233-238 11952837-1 2002 BACKGROUND: Frabin is an actin filament (F-actin)-binding protein with GDP/GTP exchange activity specific for Cdc42 small G protein. Guanosine Diphosphate 71-74 cell division cycle 42 Homo sapiens 110-115 15530857-0 2004 An activating mutant of Cdc42 that fails to interact with Rho GDP-dissociation inhibitor localizes to the plasma membrane and mediates actin reorganization. Guanosine Diphosphate 62-65 cell division cycle 42 Homo sapiens 24-29 15287724-5 2004 The F28L mutation of Cdc42Hs is characterized by an increased rate of cycling between the GTP and GDP-bound forms leading to cell transformation (Lin et al. Guanosine Diphosphate 98-101 cell division cycle 42 Homo sapiens 21-28 15287724-9 2004 Here, we describe the backbone dynamics of Cdc42Hs(F28L)-GDP using 1H-15N NMR measurements of T1, T1rho, and steady-state NOE at two magnetic field strengths. Guanosine Diphosphate 57-60 cell division cycle 42 Homo sapiens 43-50 12501193-2 2002 The cycling of Cdc42 between its on (GTP-bound) and off (GDP-bound) states is essential for its stimulation of cell growth and transformation, with an important aspect of this cycle being the regulation of the GTP hydrolytic activity of Cdc42 by its GTPase-activating protein (Cdc42GAP). Guanosine Diphosphate 57-60 cell division cycle 42 Homo sapiens 15-20 12501193-2 2002 The cycling of Cdc42 between its on (GTP-bound) and off (GDP-bound) states is essential for its stimulation of cell growth and transformation, with an important aspect of this cycle being the regulation of the GTP hydrolytic activity of Cdc42 by its GTPase-activating protein (Cdc42GAP). Guanosine Diphosphate 57-60 cell division cycle 42 Homo sapiens 237-242 12369824-2 2002 While GTPase-defective forms of Cdc42 inhibit cell growth, a mutation [Cdc42(F28L)] that allows the constitutive exchange of GDP for GTP and is GTPase-competent induces cellular transformation. Guanosine Diphosphate 125-128 cell division cycle 42 Homo sapiens 71-76 12369824-3 2002 These results suggest that Cdc42 must cycle between its GTP- and GDP-bound states to stimulate cell growth. Guanosine Diphosphate 65-68 cell division cycle 42 Homo sapiens 27-32 12369824-6 2002 The Cdc42(D118N) protein exchanges GDP for GTP more rapidly than wild-type Cdc42, but significantly more slowly than the Cdc42(F28L) mutant. Guanosine Diphosphate 35-38 cell division cycle 42 Homo sapiens 4-9 12369824-10 2002 Thus, mutations that combine some capacity for cycling between the GTP- and GDP-bound states with increased survival against apoptotic signals yield Cdc42 molecules with the maximum capability for inducing cellular transformation. Guanosine Diphosphate 76-79 cell division cycle 42 Homo sapiens 149-154 11948177-8 2002 Some insight into the mechanism was provided by in vitro analysis, which revealed that IQGAP1deltaGRD increased the intrinsic GTPase activity of Cdc42, thereby increasing the amount of inactive, GDP-bound Cdc42. Guanosine Diphosphate 195-198 cell division cycle 42 Homo sapiens 145-150 11948177-8 2002 Some insight into the mechanism was provided by in vitro analysis, which revealed that IQGAP1deltaGRD increased the intrinsic GTPase activity of Cdc42, thereby increasing the amount of inactive, GDP-bound Cdc42. Guanosine Diphosphate 195-198 cell division cycle 42 Homo sapiens 205-210 11883956-1 2002 The inactive state of the small G protein Cdc42, the Cdc42.GDP.Mg(2+) ternary complex, was investigated using fluorescence, Mn(2+) substituted electron paramagnetic resonance, and (31)P nuclear magnetic resonance spectroscopy at various urea concentrations. Guanosine Diphosphate 59-62 cell division cycle 42 Homo sapiens 42-47 11883956-1 2002 The inactive state of the small G protein Cdc42, the Cdc42.GDP.Mg(2+) ternary complex, was investigated using fluorescence, Mn(2+) substituted electron paramagnetic resonance, and (31)P nuclear magnetic resonance spectroscopy at various urea concentrations. Guanosine Diphosphate 59-62 cell division cycle 42 Homo sapiens 53-58 11883956-2 2002 The urea interaction with the protein was used to probe the binding state of GDP.Mg(2+) to Cdc42. Guanosine Diphosphate 77-80 cell division cycle 42 Homo sapiens 91-96 11883956-3 2002 Two binding states of the Cdc42.GDP.Mg(2+) ternary complex with different binding stability were observed. Guanosine Diphosphate 32-35 cell division cycle 42 Homo sapiens 26-31 10676816-3 2000 First, the amino-terminal regulatory arm of the GDI binds to the switch I and II domains of Cdc42 leading to the inhibition of both GDP dissociation and GTP hydrolysis. Guanosine Diphosphate 132-135 cell division cycle 42 Homo sapiens 92-97 10871857-1 2000 Frabin is an actin filament-binding protein which shows GDP/GTP exchange activity specific for Cdc42 small G protein and induces filopodium-like microspike formation and c-Jun N-terminal kinase (JNK) activation presumably through the activation of Cdc42. Guanosine Diphosphate 56-59 cell division cycle 42 Homo sapiens 95-100 11583574-1 2001 We have identified a mutant of the human G-protein Cdc42Hs, R66E, that fails to form a detectable complex with the GDP-dissociation inhibitor RhoGDI in cell-free systems or in intact cells. Guanosine Diphosphate 115-118 cell division cycle 42 Homo sapiens 51-58 11285260-0 2001 Maintenance of CDC42 GDP-bound state by Rho-GDI inhibits MAP kinase activation by the exchange factor Ras-GRF. Guanosine Diphosphate 21-24 cell division cycle 42 Homo sapiens 15-20 11285260-4 2001 Here, we report that retaining Cdc42 in its GDP-bound state by overexpressing Rho-GDI inhibits Ras-GRF-mediated MAPK activation. Guanosine Diphosphate 44-47 cell division cycle 42 Homo sapiens 31-36 11285260-7 2001 In contrast, promoting GDP release from Cdc42 with the Rho family GEF Dbl or with ionomycin suppressed the restraint exerted by Cdc42 on Ras-GRF activity. Guanosine Diphosphate 23-26 cell division cycle 42 Homo sapiens 40-45 11285260-7 2001 In contrast, promoting GDP release from Cdc42 with the Rho family GEF Dbl or with ionomycin suppressed the restraint exerted by Cdc42 on Ras-GRF activity. Guanosine Diphosphate 23-26 cell division cycle 42 Homo sapiens 128-133 11285260-9 2001 Interestingly, the loss of the GDP-bound state by Cdc42 abolishes its inhibitory effects on Ras-GRF function. Guanosine Diphosphate 31-34 cell division cycle 42 Homo sapiens 50-55 11294626-2 2001 We describe here the methyl side chain dynamics of three forms of (2)H,(13)C,(15)N-Cdc42Hs [GDP-bound (inactive), GMPPCP-bound (active), and GMPPCP/PBD46-bound (effector-bound)] from (13)C-(1)H NMR measurements of deuterium T(1) and T(1 rho) relaxation times. Guanosine Diphosphate 92-95 cell division cycle 42 Homo sapiens 83-90 11040036-1 2000 The functional activity of Cdc42 is known to be regulated by proteins that control its GDP/GTP-bound state. Guanosine Diphosphate 87-90 cell division cycle 42 Homo sapiens 27-32 11040036-12 2000 Instead, the proteins that modulate the GDP/GTP-bound state of Cdc42 may be the primary targets of PKA phosphorylation. Guanosine Diphosphate 40-43 cell division cycle 42 Homo sapiens 63-68 10840034-5 2000 We also demonstrate that catalyzing GDP/GTP exchange on Cdc42 facilitates Ras-GRF-induced MAPK activation. Guanosine Diphosphate 36-39 cell division cycle 42 Homo sapiens 56-61 10504223-9 1999 The Insert region of Cdc42Hs-GDP exhibits high-order, nanosecond motions; the time scale of motion in the Insert is reduced in Cdc42Hs-GMPPCP and Cdc42Hs-PBD46. Guanosine Diphosphate 29-32 cell division cycle 42 Homo sapiens 21-28 10504223-6 1999 Here we describe the backbone dynamics of three constructs of [(15)N]Cdc42Hs (GDP-, GMPPCP-, and GMPPCP- and PBD46-bound) using (15)N-(1)H NMR measurements of T(1), T(1)(rho), and the steady-state NOE at three magnetic field strengths. Guanosine Diphosphate 78-81 cell division cycle 42 Homo sapiens 69-76 10504223-9 1999 The Insert region of Cdc42Hs-GDP exhibits high-order, nanosecond motions; the time scale of motion in the Insert is reduced in Cdc42Hs-GMPPCP and Cdc42Hs-PBD46. Guanosine Diphosphate 29-32 cell division cycle 42 Homo sapiens 127-134 10504223-9 1999 The Insert region of Cdc42Hs-GDP exhibits high-order, nanosecond motions; the time scale of motion in the Insert is reduced in Cdc42Hs-GMPPCP and Cdc42Hs-PBD46. Guanosine Diphosphate 29-32 cell division cycle 42 Homo sapiens 127-134 10211824-1 1999 The 2.5 A crystal structure of the full length human placental isoform of the Gly12 to Val mutant Cdc42 protein (Cdc42(G12V)) bound to both GDP/Mg2+ and GDPNH2 (guanosine-5"-diphospho-beta-amidate) is reported. Guanosine Diphosphate 140-143 cell division cycle 42 Homo sapiens 98-103 10360579-4 1999 The effector loop of Cdc42 and Rac (comprising residues 30-40, also called switch I), is one of two regions which change conformation on exchange of GDP for GTP. Guanosine Diphosphate 149-152 cell division cycle 42 Homo sapiens 21-26 10211824-1 1999 The 2.5 A crystal structure of the full length human placental isoform of the Gly12 to Val mutant Cdc42 protein (Cdc42(G12V)) bound to both GDP/Mg2+ and GDPNH2 (guanosine-5"-diphospho-beta-amidate) is reported. Guanosine Diphosphate 140-143 cell division cycle 42 Homo sapiens 113-118 10211824-5 1999 The amino group of GDPNH2 drastically reduces the affinity to Cdc42 in comparison with that of GDP, causes the loss of the Mg2+ ion, and apparently also increases the conformational flexibility of the protein as seen in the crystal. Guanosine Diphosphate 19-22 cell division cycle 42 Homo sapiens 62-67 9642217-3 1998 In this report, we show that deletion of residues 120-139 from Cdc42(F28L), which comprise an insert region unique to Rho subfamily proteins but is missing in other GTP-binding proteins, yields a Cdc42 molecule that still undergoes spontaneous GTP-GDP exchange and stimulates both actin cytoskeletal changes and the activation of the cellular targets p21-activated kinase and the c-Jun kinase (JNK1). Guanosine Diphosphate 248-251 cell division cycle 42 Homo sapiens 63-68 9748241-2 1998 Here the Rho family members Cdc42, Rac2, and RhoA were found to form reversible homodimers in both the GTP- and the GDP-bound states. Guanosine Diphosphate 116-119 cell division cycle 42 Homo sapiens 28-33 9748241-5 1998 Moreover, similar to the case of Cdc42 and Cdc42GAP interaction, Cdc42-GDP interacted with tetrafluoroaluminate and Cdc42-GTPgammaS (guanosine 5"-3-O-(thio)triphosphate) to form a transition state complex of the GTPase-activating reaction in which the carboxyl-terminal determinant(s) of the GTPgammaS-bound Cdc42 plays a critical role. Guanosine Diphosphate 71-74 cell division cycle 42 Homo sapiens 33-38 10872457-1 1999 Members of the Rho family of small Ras-like GTPases--including RhoA, -B, and -C, Rac1 and -2, and Cdc42--exhibit guanine nucleotide-binding activity and function as molecular switches, cycling between an inactive GDP-bound state and an active GTP-bound state. Guanosine Diphosphate 213-216 cell division cycle 42 Homo sapiens 98-103 9642217-3 1998 In this report, we show that deletion of residues 120-139 from Cdc42(F28L), which comprise an insert region unique to Rho subfamily proteins but is missing in other GTP-binding proteins, yields a Cdc42 molecule that still undergoes spontaneous GTP-GDP exchange and stimulates both actin cytoskeletal changes and the activation of the cellular targets p21-activated kinase and the c-Jun kinase (JNK1). Guanosine Diphosphate 248-251 cell division cycle 42 Homo sapiens 196-201 9468490-3 1998 We have characterized the AlF4--induced complex formation between the GDP-bound form of the Rho subfamily G-protein Cdc42Hs and a limit functional domain of the Cdc42-GAP using a variety of biochemical techniques. Guanosine Diphosphate 70-73 cell division cycle 42 Homo sapiens 116-123 9468490-6 1998 Unlike Ras, we find that AlF4- and BeF3- mediate complex formation between Cdc42Hs.GDP and downstream target/effector molecules, indicating that there are important differences in the mechanism of effector binding between the Ras and Rho subfamily G-proteins. Guanosine Diphosphate 83-86 cell division cycle 42 Homo sapiens 75-82 9334181-4 1997 However, the regulation of GDP dissociation and GTP hydrolysis on Cdc42Hs by the Rho GDP-dissociation inhibitor (GDI) is extremely sensitive to changes in the insert region, such that a Cdc42Hs/Ha-Ras chimera that lacks this insert is no longer susceptible to a GDI-induced inhibition of GDP dissociation and GTP hydrolysis. Guanosine Diphosphate 27-30 cell division cycle 42 Homo sapiens 66-73 9334181-4 1997 However, the regulation of GDP dissociation and GTP hydrolysis on Cdc42Hs by the Rho GDP-dissociation inhibitor (GDI) is extremely sensitive to changes in the insert region, such that a Cdc42Hs/Ha-Ras chimera that lacks this insert is no longer susceptible to a GDI-induced inhibition of GDP dissociation and GTP hydrolysis. Guanosine Diphosphate 27-30 cell division cycle 42 Homo sapiens 186-193 9334181-4 1997 However, the regulation of GDP dissociation and GTP hydrolysis on Cdc42Hs by the Rho GDP-dissociation inhibitor (GDI) is extremely sensitive to changes in the insert region, such that a Cdc42Hs/Ha-Ras chimera that lacks this insert is no longer susceptible to a GDI-induced inhibition of GDP dissociation and GTP hydrolysis. Guanosine Diphosphate 85-88 cell division cycle 42 Homo sapiens 66-73 9334181-4 1997 However, the regulation of GDP dissociation and GTP hydrolysis on Cdc42Hs by the Rho GDP-dissociation inhibitor (GDI) is extremely sensitive to changes in the insert region, such that a Cdc42Hs/Ha-Ras chimera that lacks this insert is no longer susceptible to a GDI-induced inhibition of GDP dissociation and GTP hydrolysis. Guanosine Diphosphate 85-88 cell division cycle 42 Homo sapiens 186-193