PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32656574-4 2020 The PH domain portion of the PH-CC bi-domain interacts with the Rho GTPases Cdc42 and Rho3 and both interactions are independent of the GTP/GDP-bound state of each GTPase. Guanosine Triphosphate 68-71 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 76-81 32656257-7 2020 Biphasic Cdc42 polarization is likely to ensure the proper timing of events including the assembly and recognition of spatial landmarks and stepwise assembly of a new ring of septins, cytoskeletal GTP-binding proteins, at the incipient bud site. Guanosine Triphosphate 197-200 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 9-14 28742002-4 2017 Cdc42 GTPase can be found in a GTP- or GDP-bound state, which determines the ability to bind downstream effector proteins and activate signalling pathways. Guanosine Triphosphate 6-9 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 0-5 30566437-5 2018 In yeast cells, Cdc42 polarization involves a positive feedback loop in which effectors called p21-activated kinases (PAKs) act to recruit a Cdc42-directed guanine nucleotide exchange factor (GEF), generating more GTP-Cdc42 in areas that already have GTP-Cdc42. Guanosine Triphosphate 214-217 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 16-21 30566437-5 2018 In yeast cells, Cdc42 polarization involves a positive feedback loop in which effectors called p21-activated kinases (PAKs) act to recruit a Cdc42-directed guanine nucleotide exchange factor (GEF), generating more GTP-Cdc42 in areas that already have GTP-Cdc42. Guanosine Triphosphate 214-217 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 141-146 30566437-5 2018 In yeast cells, Cdc42 polarization involves a positive feedback loop in which effectors called p21-activated kinases (PAKs) act to recruit a Cdc42-directed guanine nucleotide exchange factor (GEF), generating more GTP-Cdc42 in areas that already have GTP-Cdc42. Guanosine Triphosphate 214-217 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 141-146 30566437-5 2018 In yeast cells, Cdc42 polarization involves a positive feedback loop in which effectors called p21-activated kinases (PAKs) act to recruit a Cdc42-directed guanine nucleotide exchange factor (GEF), generating more GTP-Cdc42 in areas that already have GTP-Cdc42. Guanosine Triphosphate 214-217 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 141-146 30566437-5 2018 In yeast cells, Cdc42 polarization involves a positive feedback loop in which effectors called p21-activated kinases (PAKs) act to recruit a Cdc42-directed guanine nucleotide exchange factor (GEF), generating more GTP-Cdc42 in areas that already have GTP-Cdc42. Guanosine Triphosphate 251-254 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 16-21 30566437-5 2018 In yeast cells, Cdc42 polarization involves a positive feedback loop in which effectors called p21-activated kinases (PAKs) act to recruit a Cdc42-directed guanine nucleotide exchange factor (GEF), generating more GTP-Cdc42 in areas that already have GTP-Cdc42. Guanosine Triphosphate 251-254 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 141-146 30566437-5 2018 In yeast cells, Cdc42 polarization involves a positive feedback loop in which effectors called p21-activated kinases (PAKs) act to recruit a Cdc42-directed guanine nucleotide exchange factor (GEF), generating more GTP-Cdc42 in areas that already have GTP-Cdc42. Guanosine Triphosphate 251-254 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 141-146 30566437-5 2018 In yeast cells, Cdc42 polarization involves a positive feedback loop in which effectors called p21-activated kinases (PAKs) act to recruit a Cdc42-directed guanine nucleotide exchange factor (GEF), generating more GTP-Cdc42 in areas that already have GTP-Cdc42. Guanosine Triphosphate 251-254 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 141-146 28783960-3 2017 The core circuit involves positive feedback by local activation of Cdc42 to generate a cluster of concentrated GTP-Cdc42 at the membrane. Guanosine Triphosphate 111-114 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 67-72 28783960-3 2017 The core circuit involves positive feedback by local activation of Cdc42 to generate a cluster of concentrated GTP-Cdc42 at the membrane. Guanosine Triphosphate 111-114 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 115-120 32079658-6 2020 The fMAPK pathway also stimulated GTP-Cdc42p levels, which is a critical determinant of polarity establishment. Guanosine Triphosphate 34-37 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 38-44 28742002-5 2017 Only GTP-bound Cdc42 is active. Guanosine Triphosphate 5-8 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 15-20 28336063-5 2017 Because it binds specifically to the GTP-bound Cdc42, this biosensor can be used to monitor Cdc42 activation in vivo. Guanosine Triphosphate 37-40 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 47-52 28336063-5 2017 Because it binds specifically to the GTP-bound Cdc42, this biosensor can be used to monitor Cdc42 activation in vivo. Guanosine Triphosphate 37-40 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 92-97 27476596-12 2016 We suggest that GAP activity cooperates with the GDI to counteract the dissipative effect of a previously unappreciated pathway whereby GTP-Cdc42 escapes from the polarity site through the cytoplasm. Guanosine Triphosphate 136-139 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 140-145 24062579-5 2013 Additional Cdc42 accumulates by positive feedback, creating a concentrated patch of GTP-Cdc42, which polarizes the cytoskeleton to promote bud emergence. Guanosine Triphosphate 84-87 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 11-16 25002677-3 2014 Bud3 catalyzes the release of guanosine diphosphate (GDP) from Cdc42 and elevates intracellular Cdc42-guanosine triphosphate (GTP) levels in cells with inactive Cdc24, which has as of yet been the sole GDP-GTP exchange factor for Cdc42. Guanosine Triphosphate 126-129 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 96-101 25002677-3 2014 Bud3 catalyzes the release of guanosine diphosphate (GDP) from Cdc42 and elevates intracellular Cdc42-guanosine triphosphate (GTP) levels in cells with inactive Cdc24, which has as of yet been the sole GDP-GTP exchange factor for Cdc42. Guanosine Triphosphate 126-129 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 96-101 26681517-8 2015 The Dbl homology domain (DBH) binds GTP-bound Cdc42p; binding is required for cell fusion, but not localization. Guanosine Triphosphate 36-39 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 46-52 24631237-8 2014 We further show that replacing the GEF with a phosphosite mutant GEF abolishes oscillations and leads to the accumulation of excess GTP-Cdc42 and other polarity factors at the front. Guanosine Triphosphate 132-135 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 136-141 24385582-6 2014 Expression of GTP-locked Cdc42 reversed the polarity of hypha emergence from cathodal to anodal, an effect augmented by Ca(2+). Guanosine Triphosphate 14-17 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 25-30 24062579-5 2013 Additional Cdc42 accumulates by positive feedback, creating a concentrated patch of GTP-Cdc42, which polarizes the cytoskeleton to promote bud emergence. Guanosine Triphosphate 84-87 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 88-93 19013066-9 2008 CONCLUSIONS: Yeast symmetry-breaking polarization involves a GEF-PAK complex that binds GTP-Cdc42p via the PAK and promotes local Cdc42p GTP-loading via the GEF. Guanosine Triphosphate 88-91 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 92-98 22117027-2 2012 Cdc24 is an upstream regulator of budding yeast Cdc42 that accelerates the exchange of GDP for GTP in Cdc42 via its Dbl homology (DH) domain. Guanosine Triphosphate 95-98 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 48-53 22117027-2 2012 Cdc24 is an upstream regulator of budding yeast Cdc42 that accelerates the exchange of GDP for GTP in Cdc42 via its Dbl homology (DH) domain. Guanosine Triphosphate 95-98 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 102-107 23437206-0 2013 Polarization of diploid daughter cells directed by spatial cues and GTP hydrolysis of Cdc42 budding yeast. Guanosine Triphosphate 68-71 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 86-91 23437206-8 2013 Unexpectedly, we also find that over 50% of daughter cells lacking Rga1 exhibit persistent Cdc42-GTP polarization at the bud tip and the distal pole, revealing an additional role of Rga1 in spatiotemporal regulation of Cdc42 and thus in the pattern of polarized growth. Guanosine Triphosphate 97-100 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 91-96 20007700-5 2010 Stimulation of multiple rounds of fusion enhanced vacuole fragmentation, suggesting that cycles of Cdc42p activation, involving rounds of GTP binding and hydrolysis, are required to propagate Cdc42p signaling. Guanosine Triphosphate 138-141 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 99-105 20007700-5 2010 Stimulation of multiple rounds of fusion enhanced vacuole fragmentation, suggesting that cycles of Cdc42p activation, involving rounds of GTP binding and hydrolysis, are required to propagate Cdc42p signaling. Guanosine Triphosphate 138-141 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 99-104 19013066-9 2008 CONCLUSIONS: Yeast symmetry-breaking polarization involves a GEF-PAK complex that binds GTP-Cdc42p via the PAK and promotes local Cdc42p GTP-loading via the GEF. Guanosine Triphosphate 88-91 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 130-136 19013066-9 2008 CONCLUSIONS: Yeast symmetry-breaking polarization involves a GEF-PAK complex that binds GTP-Cdc42p via the PAK and promotes local Cdc42p GTP-loading via the GEF. Guanosine Triphosphate 137-140 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 92-98 19013066-9 2008 CONCLUSIONS: Yeast symmetry-breaking polarization involves a GEF-PAK complex that binds GTP-Cdc42p via the PAK and promotes local Cdc42p GTP-loading via the GEF. Guanosine Triphosphate 137-140 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 130-136 16400178-1 2006 Cdc42 is a highly conserved small GTP-binding protein that is involved in regulating morphogenesis in eukaryotes. Guanosine Triphosphate 34-37 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 0-5 17220465-2 2007 Regulatory proteins control its GTP binding and hydrolysis and its subcellular localization, ensuring that Cdc42p is appropriately activated and localized at sites of polarized growth during the cell cycle. Guanosine Triphosphate 32-35 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 107-113 18387956-4 2008 The GTP-bound Cdc42 interacts with Gic2 through the Cdc42/Rac interactive binding domain located at the N terminus of Gic2 and activates Gic2 during bud emergence. Guanosine Triphosphate 4-7 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 14-19 18387956-4 2008 The GTP-bound Cdc42 interacts with Gic2 through the Cdc42/Rac interactive binding domain located at the N terminus of Gic2 and activates Gic2 during bud emergence. Guanosine Triphosphate 4-7 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 52-57 18195105-4 2008 In addition, we have identified key residues in Sec3 that are critical for its binding to the guanosine triphosphate-bound form of Cdc42. Guanosine Triphosphate 94-116 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 131-136 15020407-8 2004 The Fus1p cytoplasmic domain also interacts with the activated GTP-bound form of Cdc42p and the Fus1p-SH3 domain interacts with Bni1p, a yeast formin that participates in cell fusion and controls the assembly of actin cables to polarize secretion in response to Cdc42p signaling. Guanosine Triphosphate 63-66 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 81-87 16325503-0 2005 Cdc42-dependent localization of polarisome component Spa2 to the incipient bud site is independent of the GDP/GTP exchange factor Cdc24. Guanosine Triphosphate 110-113 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 0-5 16103227-6 2005 Consistent with this model, we find that the ability of Rho3 and Cdc42 to hydrolyze GTP is not required for their role in secretion. Guanosine Triphosphate 84-87 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 65-70 14872283-1 2004 The Saccharomyces cerevisiae Cdc24p guanine nucleotide exchange factor (GEF) activates the Cdc42p GTPase to a GTP-bound state. Guanosine Triphosphate 98-101 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 91-96 15164359-2 2004 In Saccharomyces cerevisiae Ste20 is involved in pheromone signalling, invasive growth, the hypertonic stress response, cell wall integrity and binds Cdc42, a Rho-like small GTP-binding protein required for polarized morphogenesis. Guanosine Triphosphate 174-177 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 150-155 15190213-3 2004 Current models of Cdc42p action generally follow the signaling paradigm established for Ras, in which receptors responding to an initiating stimulus cause guanine nucleotide exchange factors (GEFs) to trigger GTP-loading of Ras, leading to engagement of downstream effectors and ensuing cell proliferation. Guanosine Triphosphate 209-212 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 18-24 15190213-6 2004 (3-6) Here, we discuss the available information on this issue and conclude that unlike Ras signaling, Cdc42p directed polarity establishment additionally requires cycling between GTP- and GDP-bound forms. Guanosine Triphosphate 180-183 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 103-109 15020407-8 2004 The Fus1p cytoplasmic domain also interacts with the activated GTP-bound form of Cdc42p and the Fus1p-SH3 domain interacts with Bni1p, a yeast formin that participates in cell fusion and controls the assembly of actin cables to polarize secretion in response to Cdc42p signaling. Guanosine Triphosphate 63-66 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 262-268 11595741-6 2001 Biochemical experiments indicated that Sec3p directly interacts with Cdc42 in its GTP-bound form. Guanosine Triphosphate 82-85 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 69-74 11940652-4 2002 We also found that Ste20 kinase activity is stimulated by GTP-bound Cdc42 in vivo and this effect is blocked by the CRIB point mutations. Guanosine Triphosphate 58-61 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 68-73 11807094-2 2002 Here, we present an analysis of cdc42 mutants that display specific defects in septin organization, which identifies an important role for GTP hydrolysis by Cdc42p in the assembly of the septin ring. Guanosine Triphosphate 139-142 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 32-37 11807094-2 2002 Here, we present an analysis of cdc42 mutants that display specific defects in septin organization, which identifies an important role for GTP hydrolysis by Cdc42p in the assembly of the septin ring. Guanosine Triphosphate 139-142 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 157-163 11807094-4 2002 Other mutants known to affect GTP hydrolysis by Cdc42p also caused septin misorganization, as did deletion of Cdc42p GAPs. Guanosine Triphosphate 30-33 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 48-54 11807094-4 2002 Other mutants known to affect GTP hydrolysis by Cdc42p also caused septin misorganization, as did deletion of Cdc42p GAPs. Guanosine Triphosphate 30-33 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 48-53 11807094-6 2002 Excess accumulation of GTP-Cdc42p due to a defect in GTP hydrolysis by the septin-specific alleles might cause unphysiological activation of effectors, interfering with septin assembly. Guanosine Triphosphate 23-26 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 27-33 11807094-6 2002 Excess accumulation of GTP-Cdc42p due to a defect in GTP hydrolysis by the septin-specific alleles might cause unphysiological activation of effectors, interfering with septin assembly. Guanosine Triphosphate 53-56 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 27-33 11807094-8 2002 Instead, we suggest that assembly of the septin ring involves repeated cycles of GTP loading and GTP hydrolysis by Cdc42p. Guanosine Triphosphate 97-100 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 115-121 11807094-9 2002 These results suggest that a single GTPase, Cdc42p, can act either as a ras-like GTP-dependent "switch" to turn on effectors or as an EF-Tu-like "assembly factor" using the GTPase cycle to assemble a macromolecular structure. Guanosine Triphosphate 36-39 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 44-50 14625559-6 2003 Moreover, polarization was dependent on GTP hydrolysis by Cdc42p, suggesting that assembly of a polarization site involves cycling of Cdc42p between GTP- and GDP-bound forms, rather than functioning as a simple on/off switch. Guanosine Triphosphate 40-43 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 58-64 14625559-6 2003 Moreover, polarization was dependent on GTP hydrolysis by Cdc42p, suggesting that assembly of a polarization site involves cycling of Cdc42p between GTP- and GDP-bound forms, rather than functioning as a simple on/off switch. Guanosine Triphosphate 40-43 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 134-140 14625559-6 2003 Moreover, polarization was dependent on GTP hydrolysis by Cdc42p, suggesting that assembly of a polarization site involves cycling of Cdc42p between GTP- and GDP-bound forms, rather than functioning as a simple on/off switch. Guanosine Triphosphate 149-152 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 58-64 14625559-6 2003 Moreover, polarization was dependent on GTP hydrolysis by Cdc42p, suggesting that assembly of a polarization site involves cycling of Cdc42p between GTP- and GDP-bound forms, rather than functioning as a simple on/off switch. Guanosine Triphosphate 149-152 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 134-140 12622721-4 2003 Previous observations suggested that Rsr1p-GTP recruits Cdc24p, a GDP/GTP exchange factor for Cdc42p, at the incipient bud site. Guanosine Triphosphate 43-46 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 94-100 12622721-4 2003 Previous observations suggested that Rsr1p-GTP recruits Cdc24p, a GDP/GTP exchange factor for Cdc42p, at the incipient bud site. Guanosine Triphosphate 70-73 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 94-100 12455995-2 2002 A group of proteins called GTPase-activating proteins (GAPs) catalyze the hydrolysis of GTP to GDP, thereby inactivating Cdc42. Guanosine Triphosphate 27-30 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 121-126 11113154-5 2001 Expression of GTP-Cdc42p, the product of Cdc24p-mediated GDP/GTP exchange, stimulated Cdc24p phosphorylation independent of cell cycle cues, raising the possibility that the phosphorylation is part of a feedback regulatory pathway. Guanosine Triphosphate 61-64 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 18-24 11113154-6 2001 Bem1p binds directly to Cdc24p, to Cla4p, and to GTP-bound Cdc42p and can mediate complex formation between these proteins in vitro. Guanosine Triphosphate 49-52 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 59-65 10866202-1 2000 The Ras-related GTP-binding protein Cdc42 is implicated in a variety of biological activities including the establishment of cell polarity in yeast, the regulation of cell morphology, motility and cell-cycle progression in mammalian cells and the induction of malignant transformation. Guanosine Triphosphate 16-19 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 36-41 11113154-5 2001 Expression of GTP-Cdc42p, the product of Cdc24p-mediated GDP/GTP exchange, stimulated Cdc24p phosphorylation independent of cell cycle cues, raising the possibility that the phosphorylation is part of a feedback regulatory pathway. Guanosine Triphosphate 14-17 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 18-24 9367979-4 1997 Each protein contains a CRIB (Cdc42/Rac-interactive binding) motif and each interacts in the two-hybrid assay with the GTP-bound form of the Rho-type Cdc42 GTPase, a key regulator of polarized growth in yeast. Guanosine Triphosphate 119-122 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 30-35 10066541-2 1998 Recent evidence suggests that such cytoskeletal organization arises through the action of large protein complexes that form in response to signals from small GTP-binding proteins, such as Cdc42, Rho, and Ras. Guanosine Triphosphate 158-161 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 188-193 9535835-3 1998 ROCK-I, Kinectin, and mDia2 can bind the wild type forms of both RhoA and Cdc42 in a GTP-dependent manner in vitro. Guanosine Triphosphate 85-88 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 74-79 9395447-2 1997 In the GTP-bound state, Ral proteins bind to RalBP1, a GTPase-activating protein for CDC42 and Rac GTPases. Guanosine Triphosphate 7-10 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 85-90 9989831-2 1999 Paks can be activated in vivo and in vitro by binding to GTP-bound Cdc42 and Rac1, members of the Rho family of small GTPases implicated in regulating the organization of the actin cytoskeleton. Guanosine Triphosphate 57-60 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 67-72 9736614-1 1998 Cdc42p, a Rho-related GTP-binding protein, regulates cytoskeletal polarization and rearrangements in eukaryotic cells. Guanosine Triphosphate 22-25 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 0-6 9740799-8 1998 Furthermore, Cla4 undergoes a dramatic hyperphosphorylation in response to the combined activity of Nap1, the Clb2-Cdc28 kinase complex, and the GTP-bound form of Cdc42. Guanosine Triphosphate 145-148 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 163-168 9367979-4 1997 Each protein contains a CRIB (Cdc42/Rac-interactive binding) motif and each interacts in the two-hybrid assay with the GTP-bound form of the Rho-type Cdc42 GTPase, a key regulator of polarized growth in yeast. Guanosine Triphosphate 119-122 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 150-155 9367980-1 1997 Cdc42p, a Rho-related GTP-binding protein, regulates cytoskeletal polarization and rearrangements in eukaryotic cells, but the effectors mediating this control remain unknown. Guanosine Triphosphate 22-25 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 0-6 7565673-2 1995 A possible target for the subunits is Ste20p, whose structural homolog, the serine/threonine kinase PAK, is activated by GTP-binding p21s Cdc42 and Rac1. Guanosine Triphosphate 121-124 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 138-143 9055077-2 1997 Filamentous growth is regulated by an evolutionarily conserved signaling pathway that includes the small GTP-binding proteins Ras2p and Cdc42p, the protein kinases Ste20p, Ste11p and Ste7p, and the transcription factor Ste12p. Guanosine Triphosphate 105-108 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 136-142 9271384-7 1997 Cla4p kinase was activated in vivo by the GTP-bound form of Cdc42p. Guanosine Triphosphate 42-45 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 60-66 9242378-1 1997 The small GTP-binding proteins of the Rho family, consisting of the Rho, Rac, and Cdc42 subfamilies, are implicated in various cell functions, such as cell shape change, cell motility and cytokinesis, through reorganization of actin cytoskeleton. Guanosine Triphosphate 10-13 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 82-87 9009270-2 1997 Ste20p fulfills multiple roles in pheromone signaling, morphological switching and vegetative growth and binds Cdc42p, a Rho-like small GTP binding protein required for polarized morphogenesis. Guanosine Triphosphate 136-139 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 111-117 9003780-0 1996 Functional analysis of the interaction between the small GTP binding protein Cdc42 and the Ste20 protein kinase in yeast. Guanosine Triphosphate 57-60 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 77-82 9003780-3 1996 It is not clear how the activity of Ste20 is regulated in response to these different signals in vivo, but it has been demonstrated recently that binding of the small GTP binding protein Cdc42 is able to activate Ste20 in vitro. Guanosine Triphosphate 167-170 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 187-192 9003780-4 1996 Here we show that Ste20 functionally interacts with Cdc42 in a GTP-dependent manner in vivo: Ste20 mutants that can no longer bind Cdc42 were unable to restore growth of ste20 cla4 mutant cells. Guanosine Triphosphate 63-66 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 52-57 8914522-8 1996 The mating defect of cells deleted for STE20 is partially suppressed by multiple copies of BEM1 and CDC42, which encodes a small GTP-binding protein that binds to Ste20p and is necessary for the development of cell polarity. Guanosine Triphosphate 129-132 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 100-105 7565673-3 1995 The putative Cdc42p-binding domain of Ste20p, expressed as a fusion protein, binds human and yeast GTP-binding Cdc42p. Guanosine Triphosphate 99-102 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 13-19 7565673-3 1995 The putative Cdc42p-binding domain of Ste20p, expressed as a fusion protein, binds human and yeast GTP-binding Cdc42p. Guanosine Triphosphate 99-102 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 111-117 7565673-4 1995 Cdc42p is required for alpha-factor-induced activation of FUS1.cdc24ts strains defective for Cdc42p GDP/GTP exchange show no pheromone induction at restrictive temperatures but are partially rescued by overexpression of Cdc42p, which is potentiated by Cdc42p12V mutants. Guanosine Triphosphate 104-107 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 0-6 7565673-4 1995 Cdc42p is required for alpha-factor-induced activation of FUS1.cdc24ts strains defective for Cdc42p GDP/GTP exchange show no pheromone induction at restrictive temperatures but are partially rescued by overexpression of Cdc42p, which is potentiated by Cdc42p12V mutants. Guanosine Triphosphate 104-107 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 93-99 7565673-4 1995 Cdc42p is required for alpha-factor-induced activation of FUS1.cdc24ts strains defective for Cdc42p GDP/GTP exchange show no pheromone induction at restrictive temperatures but are partially rescued by overexpression of Cdc42p, which is potentiated by Cdc42p12V mutants. Guanosine Triphosphate 104-107 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 93-99 8300560-3 1994 As a first step toward understanding how these cytoskeletal rearrangements are controlled, we have sought to identify those proteins that regulate the binding and hydrolysis of GTP by Cdc42. Guanosine Triphosphate 177-180 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 184-189 8289788-7 1994 In addition, we have generated three site-specific mutations, G12V, Q61L, and D118A, in the Cdc42p GTP-binding domains that correspond to dominant-lethal mutations in S. cerevisiae CDC42. Guanosine Triphosphate 99-102 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 181-186 7860633-6 1995 Actin incorporation in the bud can be stimulated by treating the permeabilized cells with GTP-gamma S, and, significantly, the stimulatory effect is eliminated by a mutation in CDC42, a gene that encodes a Rho-like GTP-binding protein required for bud formation. Guanosine Triphosphate 90-93 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 177-182 7860633-6 1995 Actin incorporation in the bud can be stimulated by treating the permeabilized cells with GTP-gamma S, and, significantly, the stimulatory effect is eliminated by a mutation in CDC42, a gene that encodes a Rho-like GTP-binding protein required for bud formation. Guanosine Triphosphate 215-218 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 177-182 8300560-4 1994 Here we report that the product of the CDC24 gene, which is required for proper bud-site selection and bud emergence, can stimulate the exchange of GTP for GDP on Cdc42. Guanosine Triphosphate 148-151 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 163-168 1904541-1 1991 The Saccharomyces cerevisiae CDC42 gene product, a member of the ras superfamily of low-molecular-weight GTP-binding proteins, is involved in the control of cell polarity. Guanosine Triphosphate 105-108 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 29-34 8167411-1 1993 The Saccharomyces cerevisiae Cdc42 protein, a member of the Ras superfamily of low-molecular-weight GTP-binding proteins, is involved in the control of cell polarity during the yeast cell cycle. Guanosine Triphosphate 100-103 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 29-34 2124704-0 1990 Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42. Guanosine Triphosphate 54-57 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 190-195 2124704-0 1990 Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42. Guanosine Triphosphate 108-111 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 190-195 2164028-16 1990 The similarities to ras proteins (approximately 40% identical or related amino acids overall) were most pronounced in the regions that have been implicated in GTP binding and hydrolysis and in the COOH-terminal modifications leading to membrane association, suggesting that CDC42 function also involves these biochemical properties. Guanosine Triphosphate 159-162 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 274-279 34680163-8 2021 Because induction of mating pathway output via crosstalk from the HOG pathway takes significantly longer than induction of HOG pathway output, our findings suggest that, under normal conditions, Rga1 contributes to signal insulation by limiting availability of the GTP-bound Cdc42 pool generated by hypertonic stress. Guanosine Triphosphate 265-268 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 275-280 34908215-7 2022 This leads to decreased interactions between Exo70p and Sec3p, with Cdc42p, Rho1p and Rho3p, due to disruption of the GTP/GDP ratio of at least Rho1p and Rho3p GTPases, thereby preventing activation of the exocyst. Guanosine Triphosphate 118-121 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 68-74 2690082-7 1989 Although both CDC42 and RSR1 can suppress cdc24 and both appear to encode GTP-binding proteins, these genes do not themselves appear to be functionally interchangeable. Guanosine Triphosphate 74-77 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 14-19