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Details on Person CDC42 GAPs stimulate CDC42 GTPase activity

Class:Id	Reaction:9013161
_displayName	CDC42 GAPs stimulate CDC42 GTPase activity
_doRelease	TRUE
_timestamp	2021-06-11 00:17:19
authored	[InstanceEdit:9695572] Orlic-Milacic, Marija, 2020-07-14 [InstanceEdit:9695561] Rothfels, Karen, 2020-07-14
catalystActivity	[CatalystActivity:9013235] GTPase activator activity of CDC42 GAPs [cytosol]
compartment	[Compartment:876] plasma membrane [Compartment:70101] cytosol
created	[InstanceEdit:9013160] Orlic-Milacic, Marija, 2017-07-24
edited	[InstanceEdit:9716798] Orlic-Milacic, Marija, 2021-02-25 [InstanceEdit:9733842] Orlic-Milacic, Marija, 2021-06-10
input	[Complex:182921] CDC42:GTP [plasma membrane] [Homo sapiens] [SimpleEntity:29356] H2O [cytosol]
isChimeric	FALSE
literatureReference	[LiteratureReference:9690676] A CDC42-centered signaling unit is a dominant positive regulator of endothelial integrity [LiteratureReference:9679669] A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1 [LiteratureReference:9679694] A novel Rho GTPase-activating-protein interacts with Gem, a member of the Ras superfamily of GTPases [LiteratureReference:8871052] A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway [LiteratureReference:9681326] A vascular cell-restricted RhoGAP, p73RhoGAP, is a key regulator of angiogenesis [LiteratureReference:9679623] ARAP1: a point of convergence for Arf and Rho signaling [LiteratureReference:9681442] ARAP2 effects on the actin cytoskeleton are dependent on Arf6-specific GTPase-activating-protein activity and binding to RhoA-GTP [LiteratureReference:9679624] ARHGAP10 is necessary for alpha-catenin recruitment at adherens junctions and for Listeria invasion [LiteratureReference:9679588] ARHGAP18, a GTPase-activating protein for RhoA, controls cell shape, spreading, and motility [LiteratureReference:9679620] ARHGAP21 is a RhoGAP for RhoA and RhoC with a role in proliferation and migration of prostate adenocarcinoma cells [LiteratureReference:9681450] ARHGAP22 localizes at endosomes and regulates actin cytoskeleton [LiteratureReference:9681454] ARHGAP25, a novel Rac GTPase-activating protein, regulates phagocytosis in human neutrophilic granulocytes [LiteratureReference:9679659] ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics and cell adhesion [LiteratureReference:9679660] ARHGAP4 is a novel RhoGAP that mediates inhibition of cell motility and axon outgrowth [LiteratureReference:8980785] Abr and Bcr are multifunctional regulators of the Rho GTP-binding protein family [LiteratureReference:9679626] An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase [LiteratureReference:9681439] ArhGAP15, a novel human RacGAP protein with GTPase binding property [LiteratureReference:9679653] Arhgap28 is a RhoGAP that inactivates RhoA and downregulates stress fibers [LiteratureReference:9690846] Arhgap36-dependent activation of Gli transcription factors [LiteratureReference:9679707] BPGAP1 interacts with cortactin and facilitates its translocation to cell periphery for enhanced cell migration [LiteratureReference:5665805] Bi-modal regulation of a formin by srGAP2 [LiteratureReference:9681471] Breakpoint cluster region gene product-related domain of n-chimaerin. Discrimination between Rac-binding and GTPase-activating residues by mutational analysis [LiteratureReference:9681480] Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity [LiteratureReference:9681320] Characterization of a novel GTPase-activating protein associated with focal adhesions and the actin cytoskeleton [LiteratureReference:9681473] Characterization of the Rac-GAP (Rac-GTPase-activating protein) activity of beta2-chimaerin, a 'non-protein kinase C' phorbol ester receptor [LiteratureReference:9679693] DLC-1 suppresses non-small cell lung cancer growth and invasion by RhoGAP-dependent and independent mechanisms [LiteratureReference:9679631] Deciphering the Molecular and Functional Basis of RHOGAP Family Proteins: A SYSTEMATIC APPROACH TOWARD SELECTIVE INACTIVATION OF RHO FAMILY PROTEINS [LiteratureReference:9681420] Deleted in liver cancer (DLC) 2 encodes a RhoGAP protein with growth suppressor function and is underexpressed in hepatocellular carcinoma [LiteratureReference:9681430] Deleted in liver cancer 2 (DLC2) suppresses cell transformation by means of inhibition of RhoA activity [LiteratureReference:9679627] Expression, purification and crystallization of a BH domain from the GTPase regulatory protein associated with focal adhesion kinase [LiteratureReference:9681319] FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control actin remodelling [LiteratureReference:9679713] Functional analysis of ARHGAP6, a novel GTPase-activating protein for RhoA [LiteratureReference:8985683] Human myosin-IXb is a mechanochemically active motor and a GAP for rho [LiteratureReference:9690812] Human-specific gene ARHGAP11B promotes basal progenitor amplification and neocortex expansion [LiteratureReference:9681455] Identification and characterization of a novel Rho GTPase activating protein implicated in receptor-mediated endocytosis [LiteratureReference:196684] Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices [LiteratureReference:9681403] Identification of the GTPase-activating protein DEP domain containing 1B (DEPDC1B) as a transcriptional target of Pitx2 [LiteratureReference:9679717] Isolation of a novel human gene, ARHGAP9, encoding a rho-GTPase activating protein [LiteratureReference:9679344] Mapping the proximity interaction network of the Rho-family GTPases reveals signalling pathways and regulatory mechanisms [LiteratureReference:9681428] MgcRacGAP, a new human GTPase-activating protein for Rac and Cdc42 similar to Drosophila rotundRacGAP gene product, is expressed in male germ cells [LiteratureReference:8985599] Myo9b is a key player in SLIT/ROBO-mediated lung tumor suppression [LiteratureReference:9679615] PKNbeta interacts with the SH3 domains of Graf and a novel Graf related protein, Graf2, which are GTPase activating proteins for Rho family [LiteratureReference:9681458] Physical and functional interaction of Fyn tyrosine kinase with a brain-enriched Rho GTPase-activating protein TCGAP [LiteratureReference:9679597] Rho GTPase Transcriptome Analysis Reveals Oncogenic Roles for Rho GTPase-Activating Proteins in Basal-like Breast Cancers [LiteratureReference:9679662] Rho-GTPase-activating protein interacting with Cdc-42-interacting protein 4 homolog 2 (Rich2): a new Ras-related C3 botulinum toxin substrate 1 (Rac1) GTPase-activating protein that controls dendritic spine morphogenesis [LiteratureReference:196680] Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1 [LiteratureReference:9681421] START-GAP3/DLC3 is a GAP for RhoA and Cdc42 and is localized in focal adhesions regulating cell morphology [LiteratureReference:375968] Signal transduction in neuronal migration: roles of GTPase activating proteins and the small GTPase Cdc42 in the Slit-Robo pathway [LiteratureReference:9681396] The GRAF family member oligophrenin1 is a RhoGAP with BAR domain and regulates Rho GTPases in platelets [LiteratureReference:9679603] The RhoGAP ARHGAP19 controls cytokinesis and chromosome segregation in T lymphocytes [LiteratureReference:9681483] The effect of missense mutations in the RhoGAP-homology domain on ocrl1 function [LiteratureReference:9679699] The human minor histocompatibility antigen 1 is a RhoGAP [LiteratureReference:9681452] The human orthologue of CdGAP is a phosphoprotein and a GTPase-activating protein for Cdc42 and Rac1 but not RhoA [LiteratureReference:9681495] The novel Rho-GTPase activating gene MEGAP/ srGAP3 has a putative role in severe mental retardation [LiteratureReference:9681345] The smooth muscle-selective RhoGAP GRAF3 is a critical regulator of vascular tone and hypertension [LiteratureReference:9679728] The t complex-encoded GTPase-activating protein Tagap1 acts as a transmission ratio distorter in mice [LiteratureReference:428411] Vilse, a conserved Rac/Cdc42 GAP mediating Robo repulsion in tracheal cells and axons [LiteratureReference:9679678] p190-B, a new member of the Rho GAP family, and Rho are induced to cluster after integrin cross-linking [LiteratureReference:9679648] p250GAP, a novel brain-enriched GTPase-activating protein for Rho family GTPases, is involved in the N-methyl-d-aspartate receptor signaling [LiteratureReference:9692761] Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP [LiteratureReference:9692752] TCGAP, a multidomain Rho GTPase-activating protein involved in insulin-stimulated glucose transport [LiteratureReference:9692753] Effects of structure of Rho GTPase-activating protein DLC-1 on cell morphology and migration [LiteratureReference:9692758] Characterization of the interactions between the small GTPase Cdc42 and its GTPase-activating proteins and putative effectors. Comparison of kinetic properties of Cdc42 binding to the Cdc42-interactive domains [LiteratureReference:9714239] Systems analysis of RhoGEF and RhoGAP regulatory proteins reveals spatially organized RAC1 signalling from integrin adhesions [LiteratureReference:9733576] Dissecting the thermodynamics of GAP-RhoA interactions
modified	[InstanceEdit:9013167] Orlic-Milacic, Marija, 2017-07-24 [InstanceEdit:9013238] Orlic-Milacic, Marija, 2017-07-24 [InstanceEdit:9026093] Orlic-Milacic, Marija, 2017-10-17 [InstanceEdit:9028492] Orlic-Milacic, Marija, 2017-11-08 [InstanceEdit:9692640] Orlic-Milacic, Marija, 2020-06-24 [InstanceEdit:9692763] Orlic-Milacic, Marija, 2020-06-25 [InstanceEdit:9696553] Orlic-Milacic, Marija, 2020-07-22 [InstanceEdit:9697611] Orlic-Milacic, Marija, 2020-08-18 [InstanceEdit:9698215] Orlic-Milacic, Marija, 2020-08-24 [InstanceEdit:9714844] Orlic-Milacic, Marija, 2021-02-15 [InstanceEdit:9715101] Orlic-Milacic, Marija, 2021-02-16 [InstanceEdit:9715390] Orlic-Milacic, Marija, 2021-02-17 [InstanceEdit:9716668] Orlic-Milacic, Marija, 2021-02-23 [InstanceEdit:9716799] Orlic-Milacic, Marija, 2021-02-25 [InstanceEdit:9733577] Orlic-Milacic, Marija, 2021-06-07 [InstanceEdit:9733841] Orlic-Milacic, Marija, 2021-06-10 [InstanceEdit:9733843] Orlic-Milacic, Marija, 2021-06-11 [InstanceEdit:9830342] Matthews, Lisa, 2023-03-08
name	CDC42 GAPs stimulate CDC42 GTPase activity
output	[Complex:9013230] CDC42:GDP [plasma membrane] [Homo sapiens] [SimpleEntity:29372] Pi [cytosol]
precedingEvent	[Reaction:9013159] CDC42 GEFs activate CDC42 [Homo sapiens]
releaseDate	2021-03-23
reviewed	[InstanceEdit:9714226] Fort, Philippe, 2021-02-05 [InstanceEdit:9733837] Das, Maitreyi, 2021-05-17
reviewStatus	[ReviewStatus:9821382] five stars
species	[Species:48887] Homo sapiens
stableIdentifier	[StableIdentifier:9013164] R-HSA-9013161.3
summation	[Summation:9692639] The following GTPase activating proteins (GAPs) were shown t...
(hasEvent)	[Pathway:9013148] CDC42 GTPase cycle [Homo sapiens] [Pathway:9025112] (NEW)ROCK signaling regulates MRLC phosphorylation [Homo sapiens]
(replacementInstances)	[_Deleted:9768323] Deletion of instance: 194922
(updatedInstance)	[_UpdateTracker:9775890] Update Tracker - [Reaction:9013161] CDC42 GAPs stimulate CDC42 GTPase activity - v78:[addLiteratureReference, modifyText]
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