Reactome | CDC42 GAPs stimulate CDC42 GTPase activity

CDC42 GAPs stimulate CDC42 GTPase activity

Stable Identifier

R-HSA-9013161

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane, cytosol

ReviewStatus

5/5

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CDC42 GAPs stimulate CDC42 GTPase activity

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The following GTPase activating proteins (GAPs) were shown to bind CDC42 and stimulate its GTPase activity, resulting in GTP to GDP hydrolysis and conversion of the active CDC42:GTP complex into the inactive CDC42:GDP complex (the high throughput screen by Bagci et al. 2020 is cited as supporting evidence since it examined binding of GAPs to constitutively active CDC42 mutant but did not test for activation of CDC42 GTPase activity):
ARAP1 (Miura et al. 2002; Müller et al. 2020)
ARHGAP1 (Nassar et al. 1998; Amin et al. 2016; Müller et al. 2020; supported by Bagci et al. 2020)
ARHGAP20 (Müller et al. 2020)
ARHGAP22 (Mori et al. 2014; Müller et al. 2020)
ARHGAP39 (Lundström et al. 2004; Müller et al. 2020; supported by Bagci et al. 2020)
ARHGAP40 (Müller et al. 2020)
FAM13B (Müller et al. 2020)
HMHA1 (de Kreuk et al. 2013)

The following GAPs were shown to bind CDC42 and stimulate its GTPase activity in some but not all studies and are annotated as candidate CDC42 GAPs:
ABR (Chuang et al. 1995, Amin et al. 2016: CDC42 directed GAP activity; Müller et al. 2020: no CDC42 directed GAP activity; Bagci et al. 2020: no binding to active CDC42 GAP)
ARAP2 (Müller et al. 2020: CDC42-directed GAP activity; Yoon et al. 2006: no CDC42-directed GAP activity; Bagci et al. 2020: no binding to active CDC42)
ARAP3 (Krugmann et al. 2002, Müller et al. 2020: CDC42 directed GAP activity; Bagci et al. 2020: no binding to active CDC42)
ARHGAP4 (Vogt et al. 2007: CDC42-directed GAP activity; Müller et al. 2020: no CDC42-directed GAP activity)
ARHGAP5 (Burbelo et al. 1995: CDC42-directed GAP activity; Bagci et al. 2020: binding to active CDC42; Müller et al. 2020: no CDC42-directed GAP activity)
ARHGAP9 (Furukawa et al. 2001: CDC42-directed GAP activity; Müller et al. 2020: no CDC42-directed GAP activity)
ARHGAP10 (also known as Graf2) (Shibata et al. 2001: CDC42-directed GAP activity; Müller et al. 2020: no CDC42-directed GAP activity)
ARHGAP11B (Müller et al. 2020: CDC42-directed GAP activity; Florio et al. 2015: no CDC42-directed GAP activity)
ARHGAP17 (Richnau and Aspenstrom 2001, Amin et al. 2016: CDC42-directed GAP activity; Bagci et al. 2020: binding to active CDC42; Müller et al. 2020: no CDC42-directed GAP activity)
ARHGAP21 (Sousa et al. 2005: CDC42 directed GAP activity; Bagci et al. 2020: binding to active CDC42; Lazarini et al. 2013, Müller et al. 2020: no CDC42 directed GAP activity)
ARHGAP24 (Lavelin and Geiger 2005, Ohta et al. 2006: CDC42 directed GAP activity; Su et al. 2004, Müller et al. 2020: no CDC42 directed GAP activity)
ARHGAP26 (Hildebrand 1996, Sheffield et al. 1999, Amin et al. 2016: CDC42-directed GAP activity; Müller et al. 2020: no CDC42-directed GAP activity)
ARHGAP27 (Sakakibara et al. 2004: CDC42-directed GAP activity; Müller et al. 2020: no CDC42-directed GAP activity)
ARHGAP29 (Saras et al. 1997: CDC42 directed GAP activity; Müller et al. 2020: no CDC42 directed GAP activity; Bagci et al. 2020: no binding to active CDC42)
ARHGAP30 (Müller et al. 2020: CDC42-directed GAP activity; Naji et al. 2011: no CDC42-directed GAP activity)
ARHGAP31 (Tcherkezian et al. 2006, Müller et al. 2020: CDC42 directed GAP activity; Bagci et al. 2020: no binding to active CDC42)
ARHGAP32 (Nakazawa et al. 2003: CDC42-directed GAP activity; Bagci et al. 2020: binding to active CDC42; Müller et al. 2020: no CDC42-directed GAP activity)
ARHGAP33 (Chiang et al. 2003, Liu et al. 2006: CDC42-directed GAP activity; Müller et al. 2020: no CDC42-directed GAP activity)
ARHGAP35 (Zhang et al. 1997, Amin et al. 2016: CDC42 directed GAP activity; Müller et al. 2020: no CDC42 directed GAP activity; Bagci et al. 2020: no binding to active CDC42)
ARHGAP42 (Bai et al. 2013: CDC42 directed GAP activity; Bagci et al. 2020: no binding to active CDC42)
ARHGAP44 (also known as RICH2) (Raynaud et al. 2014: CDC42-directed GAP activity; Müller et al. 2020: no CDC42-directed GAP activity)
BCR (Chuang et al. 1995: CDC42 directed GAP activity; Müller et al. 2020: no CDC42 directed GAP activity; Bagci et al. 2020: no binding to active CDC42)
CHN1 (also known as ARHGAP2) (Ahmed et al. 1994: CDC42-directed GAP activity; Müller et al. 2020: no CDC42-directed GAP activity)
DEPDC1B (Bagci et al. 2020: binding to active CDC42; Wu et al. 2015, Müller et al. 2020: no CDC42 directed GAP activity)
DLC1 (Healy et al. 2008, Kim et al. 2008, Amin et al. 2016: CDC42-directed GAP activity; Müller et al. 2020: no CDC42-directed GAP activity)
GMIP (Müller et al. 2020: CDC42-directed GAP activity; Aresta et al. 2002: no CDC42-directed GAP activity)
MYO9B (Müller et al. 2020: CDC42-directed GAP activity; Post et al. 1998, Kong et al. 2015: no CDC42-directed GAP activity; Bagci et al. 2020: no binding to active CDC42)
OPHN1 (Elvers et al. 2012, Amin et al. 2016: CDC42-directed GAP activity; Bagci et al. 2020: binding to active CDC42; Müller et al. 2020: no CDC42-directed GAP activity)
PIK3R1 (Bagci et al. 2020: binding to active CDC42; Müller et al. 2020: no CDC42-directed GAP activity)
PIK3R2 (Bagci et al. 2020: binding to active CDC42; Müller et al. 2020: no CDC42-directed GAP activity)
RACGAP1 (Touré et al. 1998, Amin et al. 2016: CDC42 directed GAP activity; Müller et al. 2020: no CDC42 directed GAP activity; Bagci et al. 2020: no binding to active CDC42)
RALBP1 (Jullien Flores et al. 1995: CDC42-directed GAP activity; Müller et al. 2020: no CDC42-directed GAP activity)
SRGAP1 (Wong et al. 2001: CDC42-directed GAP activity; Müller et al. 2020: no CDC42-directed GAP activity)
SRGAP2 (Mason et al. 2011, Müller et al. 2020: CDC42 directed GAP activity; Bagci et al. 2020: no binding to active CDC42)
SRGAP3 (Endris et al. 2002: CDC42-directed GAP activity; Müller et al. 2020: no CDC42-directed GAP activity)
STARD8 (Kawai et al. 2007, Müller et al. 2020: CDC42 directed GAP activity; Amin et al. 2016: no CDC42 directed GAP activity)
STARD13 (Leung et al. 2005, Ching et al. 2003: CDC42 directed GAP activity; Amin et al. 2016, Müller et al. 2020: no CDC42 directed GAP activity)
SYDE1 (Amado Azevedo et al. 2017: CDC42-directed GAP activity; Bagci et al. 2020: binding to active CDC42; Müller et al. 2020: no CDC42-directed GAP activity)
TAGAP (Bauer et al. 2005: CDC42-directed GAP activity; Müller et al. 2020: no CDC42-directed GAP activity)

The following GAPs do not act on CDC42 or were shown in the high throughput screen by Bagci et al. 2020 to not bind to constitutively active CDC42 mutant:
ARHGAP6 (Prakash et al. 2000; Müller et al. 2020)
ARHGAP8 (Lua and Low 2004; Müller et al. 2020)
ARHGAP11A (Lawson et al. 2016; Müller et al. 2020)
ARHGAP12 (Bagci et al. 2020; Müller et al. 2020)
ARHGAP15 (Seoh et al. 2003; Müller et al. 2020)
ARHGAP18 (Maeda et al. 2011; Müller et al. 2020)
ARHGAP19 (David et al. 2014; Müller et al. 2020)
ARHGAP23 (Müller et al. 2020)
ARHGAP25 (Csépányi Kömi et al. 2012; Müller et al. 2020)
ARHGAP28 (Yeung et al. 2014; Müller et al. 2020)
ARHGAP36 (Rack et al. 2014; Müller et al. 2020; ARHGAP36 was shown by Jelen et al. 2009 to lack motifs needed for the GAP activity and likely does not act like a GAP)
ARHGAP45 (Müller et al. 2020)
CHN2 (Caloca et al. 2003; Müller et al. 2020)
DEPDC1 (Müller et al. 2020)
FAM13A (Müller et al. 2020)
INPP5B (Müller et al. 2020)
MYO9A (Müller et al. 2020; Bagci et al. 2020)
OCRL (Erdmann et al. 2007; Lichter Konecki et al. 2006; Müller et al. 2020; Bagci et al. 2020)
SH3BP1 (Müller et al. 2020)
SYDE2 (Müller et al. 2020)

Literature References

PubMed ID	Title	Journal	Year
27216196	Rho GTPase Transcriptome Analysis Reveals Oncogenic Roles for Rho GTPase-Activating Proteins in Basal-like Breast Cancers Burridge, K, Rossman, KL, Graham, DM, Mitin, N, George, SD, Perou, CM, Lawson, CD, Baker, NM, Fan, C, Der, CJ	Cancer Res.	2016
15342493	Vilse, a conserved Rac/Cdc42 GAP mediating Robo repulsion in tracheal cells and axons Lundström, A, Hemphälä, J, Keleman, K, Steneberg, P, Gallio, M, Aspenström, P, Falileeva, L, Samakovlis, C, Englund, C, Dickson, BJ	Genes Dev	2004
21865595	ARHGAP18, a GTPase-activating protein for RhoA, controls cell shape, spreading, and motility Asano, E, Hyodo, T, Funasaka, K, Ito, S, Hamaguchi, M, Hasegawa, Y, Hasegawa, H, Maeda, M, Yuang, H, Senga, T, Shimokata, K	Mol. Biol. Cell	2011
26529257	Myo9b is a key player in SLIT/ROBO-mediated lung tumor suppression Nie, Y, Li, X, Zhu, L, Fan, D, Wen, P, Liu, J, Yi, F, Kong, R, Wu, JY, Wu, K, Chen, X, Shang, Y, Feng, W, Ren, J	J. Clin. Invest.	2015
11396949	Isolation of a novel human gene, ARHGAP9, encoding a rho-GTPase activating protein Kawasoe, T, Takahashi, M, Ishiguro, H, Furukawa, Y, Nakamura, Y, Kitayama, J, Nishiwaki, T, Daigo, Y	Biochem. Biophys. Res. Commun.	2001
10699171	Functional analysis of ARHGAP6, a novel GTPase-activating protein for RhoA Paylor, R, Xu, B, Armstrong, DL, Zoghbi, HY, Lamarche-Vane, N, Prakash, SK, Jenna, S, Mancini, MA	Hum. Mol. Genet.	2000
11432776	PKNbeta interacts with the SH3 domains of Graf and a novel Graf related protein, Graf2, which are GTPase activating proteins for Rho family Shibata, H, Oishi, K, Mukai, H, Matsumoto, M, Yamagiwa, A, Ono, Y	J. Biochem.	2001
25704760	Identification of the GTPase-activating protein DEP domain containing 1B (DEPDC1B) as a transcriptional target of Pitx2 Lombana, N, Wu, D, Sollecito, CC, Mold, AJ, Wei, Q, Zhu, X, Jiao, M, Jimenez-Cowell, K	Exp. Cell Res.	2015
22298643	The GRAF family member oligophrenin1 is a RhoGAP with BAR domain and regulates Rho GTPases in platelets Beck, S, Ziegler, M, Fotinos, A, Elvers, M, Gawaz, M	Cardiovasc. Res.	2012
16116428	The t complex-encoded GTPase-activating protein Tagap1 acts as a transmission ratio distorter in mice Koschorz, B, Willert, J, Bauer, H, Herrmann, BG	Nat. Genet.	2005
31871319	Mapping the proximity interaction network of the Rho-family GTPases reveals signalling pathways and regulatory mechanisms Tran, V, Gingras, AC, Elkholi, IE, Robert, A, Boulais, J, Faubert, D, Dubé, N, Hipfner, DR, Cote, JF, Lin, ZY, Bagci, H, Sriskandarajah, N, Thibault, MP	Nat. Cell Biol.	2020
24259668	The RhoGAP ARHGAP19 controls cytokinesis and chromosome segregation in T lymphocytes Bertoglio, J, David, MD, Petit, D	J. Cell. Sci.	2014
17932950	DLC-1 suppresses non-small cell lung cancer growth and invasion by RhoGAP-dependent and independent mechanisms Kim, TY, Shutes, A, Healy, KD, Juliano, RL, Hodgson, L, Harden, TK, Bang, YJ, Der, CJ, Maddileti, S, Hahn, KM	Mol. Carcinog.	2008
12093360	A novel Rho GTPase-activating-protein interacts with Gem, a member of the Ras superfamily of GTPases Aresta, S, de Gunzburg, J, Béranger, F, de Tand-Heim, MF	Biochem. J.	2002
18929667	Dissecting the thermodynamics of GAP-RhoA interactions Jelen, F, Apostoluk, W, Derewenda, ZS, Lachowicz, P, Otlewski, J, Mateja, A	J Struct Biol	2009
7673236	Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity Berger, R, Saragosti, S, Gacon, G, Romero, F, Letourneur, F, Camonis, JH, Dorseuil, O, Jullien-Flores, V, Tavitian, A	J. Biol. Chem.	1995
21148482	Bi-modal regulation of a formin by srGAP2 Higgs, HN, Heimsath, EG, Mason, FM, Soderling, SH	J. Biol. Chem.	2011
9490638	Human myosin-IXb is a mechanochemically active motor and a GAP for rho Post, PL, Bokoch, GM, Mooseker, MS	J. Cell. Sci.	1998
16777452	The effect of missense mutations in the RhoGAP-homology domain on ocrl1 function Nussbaum, RL, Lichter-Konecki, U, Suchy, SF, Farber, LW, Cronin, JS	Mol. Genet. Metab.	2006
24335996	The smooth muscle-selective RhoGAP GRAF3 is a critical regulator of vascular tone and hypertension Bai, X, Mack, CP, Suen, AA, Li, F, Kakoki, M, Taylor, JM, Lenhart, KC, Smithies, O, Bird, KE, Rojas, M	Nat Commun	2013
12877655	Characterization of the Rac-GAP (Rac-GTPase-activating protein) activity of beta2-chimaerin, a 'non-protein kinase C' phorbol ester receptor Caloca, MJ, Wang, H, Kazanietz, MG	Biochem. J.	2003
11804589	Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices Painter, G, Nazarian, A, Michell, RH, Risso, N, Cooper, MA, Dove, SK, Davidson, K, Lim, ZY, Ridley, SH, Ellson, CD, Holmes, AB, Grewal, A, Lipp, P, Tempst, P, Erdjument-Bromage, H, Anderson, KE, Hawkins, PT, Eguinoa, A, Manifava, M, McGregor, A, Thuring, JW, Coadwell, J, Krugmann, S, Stephens, LR, Ktistakis, N	Mol Cell	2002
25024229	Arhgap36-dependent activation of Gli transcription factors Crapster, JA, Pfister, SM, Cho, YJ, Nguyen, V, Ni, J, Mich, JK, Hovestadt, V, Rack, PG, Firestone, AJ, Jones, DT, Kool, M, Chen, JK, Payumo, AY	Proc. Natl. Acad. Sci. U.S.A.	2014
11431473	Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1 Aspenstrom, P, Richnau, N	J Biol Chem	2001
9846874	Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP Nassar, N, Cerione, RA, Manor, D, Clardy, JC, Hoffman, GR	Nat. Struct. Biol.	1998
15064355	BPGAP1 interacts with cortactin and facilitates its translocation to cell periphery for enhanced cell migration Lua, BL, Low, BC	Mol. Biol. Cell	2004
9268338	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 Zhang, B, Wang, ZX, Zheng, Y	J. Biol. Chem.	1997
16217026	Deleted in liver cancer 2 (DLC2) suppresses cell transformation by means of inhibition of RhoA activity Wong, CM, Ching, YP, Ng, IO, Jin, DY, Leung, TH, Yau, TO, Yam, JW	Proc. Natl. Acad. Sci. U.S.A.	2005
9497316	MgcRacGAP, a new human GTPase-activating protein for Rac and Cdc42 similar to Drosophila rotundRacGAP gene product, is expressed in male germ cells Reibel, L, Gacon, G, Morin, L, Jégou, B, Dorseuil, O, Touré, A, Timmons, P	J. Biol. Chem.	1998
17765681	A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway Paradise, S, Zoncu, R, Lee, S, Mao, Y, Biemesderfer, D, McCrea, HJ, Toomre, D, De Camilli, P, Erdmann, KS, Modregger, J	Dev. Cell	2007
12650940	ArhGAP15, a novel human RacGAP protein with GTPase binding property Leung, T, Seoh, ML, Lim, L, Ng, CH, Yong, J	FEBS Lett.	2003
11804590	ARAP1: a point of convergence for Arf and Rho signaling Hirsch, DS, Zhu, K, Jacques, KM, Stauffer, S, Randazzo, PA, Resau, J, Zheng, Y, Miura, K, Kubosaki, A	Mol. Cell	2002
23200924	ARHGAP21 is a RhoGAP for RhoA and RhoC with a role in proliferation and migration of prostate adenocarcinoma cells Ridley, AJ, Machado-Neto, JA, Saad, ST, Verjovski-Almeida, S, Barcellos, KS, Lazarini, M, Traina, F, Brandão, MM, Moreira, YB	Biochim. Biophys. Acta	2013
10232922	Expression, purification and crystallization of a BH domain from the GTPase regulatory protein associated with focal adhesion kinase Derewenda, U, Derewenda, ZS, Parsons, TJ, Sheffield, PJ, Taylor, J	Acta Crystallogr. D Biol. Crystallogr.	1999
8649427	An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase Parsons, JT, Taylor, JM, Hildebrand, JD	Mol. Cell. Biol.	1996
16184169	ARHGAP10 is necessary for alpha-catenin recruitment at adherens junctions and for Listeria invasion Boisson-Dupuis, S, Legrain, P, Gouin, E, Lecuit, M, Lemichez, E, Colland, F, Cabanes, D, Cossart, P, Archambaud, C, Popoff, M, Sousa, S	Nat. Cell Biol.	2005
27481945	Deciphering the Molecular and Functional Basis of RHOGAP Family Proteins: A SYSTEMATIC APPROACH TOWARD SELECTIVE INACTIVATION OF RHO FAMILY PROTEINS Ahmadian, MR, Somlyo, AV, Amin, E, Koessmeier, KT, Jaiswal, M, Dvorsky, R, Reis, K, Derewenda, U, Nouri, K, Aspenström, P	J. Biol. Chem.	2016
17976533	START-GAP3/DLC3 is a GAP for RhoA and Cdc42 and is localized in focal adhesions regulating cell morphology Kiyota, M, Seike, J, Deki, Y, Yagisawa, H, Kawai, K	Biochem. Biophys. Res. Commun.	2007
12531887	Deleted in liver cancer (DLC) 2 encodes a RhoGAP protein with growth suppressor function and is underexpressed in hepatocellular carcinoma Wong, CM, Ching, YP, Ng, IO, Jin, DY, Ng, DC, Leung, TH, Chan, SF	J. Biol. Chem.	2003
16777849	Physical and functional interaction of Fyn tyrosine kinase with a brain-enriched Rho GTPase-activating protein TCGAP Liu, H, Nakazawa, T, Yamamoto, T, Tezuka, T	J. Biol. Chem.	2006
11672528	Signal transduction in neuronal migration: roles of GTPase activating proteins and the small GTPase Cdc42 in the Slit-Robo pathway Brady-Kalnay, SM, Tang, H, Xie, Y, Wen, L, Mei, L, Wu, JY, Ren, XR, Rao, Y, Saito, H, Wong, K, Xiong, WC, Liu, G, Huang, YZ	Cell	2001
9305890	A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1 Franzén, P, Hellman, U, Aspenström, P, Gonez, LJ, Saras, J, Heldin, CH	J. Biol. Chem.	1997
28860633	A CDC42-centered signaling unit is a dominant positive regulator of endothelial integrity van Nieuw Amerongen, GP, van Beusechem, VW, Amado-Azevedo, J, Hordijk, PL, van Bezu, J, van Hinsbergh, VWM, Reinhard, NR, de Menezes, RX	Sci Rep	2017
32203420	Systems analysis of RhoGEF and RhoGAP regulatory proteins reveals spatially organized RAC1 signalling from integrin adhesions Pawson, T, Freitag, K, Zhang, S, Bakal, C, Popp, O, Petsalaki, E, Giudice, G, Mertins, P, Bagshaw, RD, Larsen, B, Rrustemi, T, Brandenburg, L, Nguyen, V, Roth, FP, Sanchez-Castro, M, Barth, C, Eccles, RL, Czajkowski, MT, Rademacher, J, Colwill, K, Pascual-Vargas, P, Wortmann, C, Pertz, O, Tucholska, M, Alp, KM, Rocks, O, Trnka, P, Mbamalu, G, van Unen, J, Spatt, L, Müller, PM, Heinrich, LE, Welke, RW, Gingras, AC	Nat Cell Biol	2020
8021274	Breakpoint cluster region gene product-related domain of n-chimaerin. Discrimination between Rac-binding and GTPase-activating residues by mutational analysis Best, A, Wen, LP, Lim, L, Zhao, Z, Kozma, R, Ho, J, Lee, J, Ahmed, S	J. Biol. Chem.	1994
8537347	p190-B, a new member of the Rho GAP family, and Rho are induced to cluster after integrin cross-linking Miyamoto, S, Burbelo, PD, Utani, A, Yamada, KM, Yamada, Y, Hall, A, Brill, S	J. Biol. Chem.	1995
25721503	Human-specific gene ARHGAP11B promotes basal progenitor amplification and neocortex expansion Haffner, C, Florio, M, Huttner, WB, Klemroth, S, Lewitus, E, Lachmann, R, Guhr, E, Kelso, J, Wong, FK, Albert, M, Taverna, E, Naumann, R, Sykes, A, Nüsslein, I, Dahl, A, Prüfer, K, Brandl, H, Namba, T, Peters, J, Paabo, S	Science	2015
17077126	ARAP2 effects on the actin cytoskeleton are dependent on Arf6-specific GTPase-activating-protein activity and binding to RhoA-GTP Casanova, JE, Randazzo, PA, Cuthbert, EJ, Davis, KK, Miura, K, Yoon, HY, Ahvazi, B	J. Cell. Sci.	2006
12857875	p250GAP, a novel brain-enriched GTPase-activating protein for Rho family GTPases, is involved in the N-methyl-d-aspartate receptor signaling Yokoyama, K, Nakazawa, T, Manabe, T, Umemori, H, Yoshida, Y, Inoue, A, Yamamoto, T, Watabe, AM, Okabe, S, Tezuka, T	Mol. Biol. Cell	2003
16862148	FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control actin remodelling Stossel, TP, Hartwig, JH, Ohta, Y	Nat. Cell Biol.	2006
25211221	Arhgap28 is a RhoGAP that inactivates RhoA and downregulates stress fibers Taylor, SH, Zeef, LA, Yeung, CY, Garva, R, Soininen, R, Holmes, DF, Boot-Handford, RP, Kadler, KE	PLoS ONE	2014
21565175	ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics and cell adhesion Pacholsky, D, Naji, L, Aspenström, P	Biochem. Biophys. Res. Commun.	2011
7479768	Abr and Bcr are multifunctional regulators of the Rho GTP-binding protein family Heisterkamp, N, Xu, X, Bokoch, GM, Groffen, J, Kaartinen, V, Chuang, TH	Proc. Natl. Acad. Sci. U.S.A.	1995
24933155	ARHGAP22 localizes at endosomes and regulates actin cytoskeleton Saito, K, Mori, M, Ohta, Y	PLoS ONE	2014
15611138	Characterization of a novel GTPase-activating protein associated with focal adhesions and the actin cytoskeleton Geiger, B, Lavelin, I	J. Biol. Chem.	2005
15147912	Identification and characterization of a novel Rho GTPase activating protein implicated in receptor-mediated endocytosis Nukiwa, T, Nemoto, Y, Takeshima, H, Sakakibara, T	FEBS Lett.	2004
15302923	A vascular cell-restricted RhoGAP, p73RhoGAP, is a key regulator of angiogenesis Goodall, GJ, Gamble, JR, Reck, NM, Leske, AF, Kremmidiotis, G, Su, ZJ, Vadas, MA, Hahn, CN, Davy, A	Proc. Natl. Acad. Sci. U.S.A.	2004
22096251	ARHGAP25, a novel Rac GTPase-activating protein, regulates phagocytosis in human neutrophilic granulocytes Ligeti, E, Geiszt, M, Sirokmány, G, Csépányi-Kömi, R	Blood	2012
24352656	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 Raynaud, F, Dahl, J, Boeckers, TM, Schmidt, S, Bertaso, F, Homburger, V, Fagni, L, Moutin, E	J. Biol. Chem.	2014
17804252	ARHGAP4 is a novel RhoGAP that mediates inhibition of cell motility and axon outgrowth Malouf, AT, Vogt, DL, Orellana, SA, Gray, CD, Young, WS	Mol. Cell. Neurosci.	2007
16519628	The human orthologue of CdGAP is a phosphoprotein and a GTPase-activating protein for Cdc42 and Rac1 but not RhoA Stenne, R, Triki, I, Danek, EI, Tcherkezian, J, Lamarche-Vane, N	Biol. Cell	2006
24086303	The human minor histocompatibility antigen 1 is a RhoGAP Anthony, EC, Schaefer, A, de Kreuk, BJ, Fernandez-Borja, M, Goulmy, E, Hordijk, PL, Geerts, D, Tol, S, Pool, J, Hambach, L	PLoS ONE	2013
18786931	Effects of structure of Rho GTPase-activating protein DLC-1 on cell morphology and migration Healy, KD, Juliano, RL, Sciaky, N, Bang, YJ, Kim, TY, Der, CJ	J. Biol. Chem.	2008
12773384	TCGAP, a multidomain Rho GTPase-activating protein involved in insulin-stimulated glucose transport Hwang, J, Legendre, M, Zhang, M, Saltiel, AR, Kimura, A, Chiang, SH	EMBO J.	2003
12195014	The novel Rho-GTPase activating gene MEGAP/ srGAP3 has a putative role in severe mental retardation Kirsch, S, Latif, F, Karch, D, Leimer, U, Rappold, GA, Zatyka, M, Endris, V, Tariverdian, G, Wogatzky, B, Maher, ER, Bartsch, D	Proc. Natl. Acad. Sci. U.S.A.	2002