Signaling by Rho GTPases (Homo sapiens)

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The Rho family of small guanine nucleotide binding proteins is one of five generally recognized branches of the Ras superfamily. Like most Ras superfamily members, typical Rho proteins function as binary switches controlling a variety of biological processes. They perform this function by cycling between active GTP-bound and inactive GDP-bound conformations. Mammalian Rho GTPases include RhoA, RhoB and RhoC (Rho proteins), Rac1 3 (Rac proteins), Cdc42, TC10, TCL, Wrch1, Chp/Wrch2, RhoD and RhoG, to name some. The family also includes RhoH and Rnd1-3, which lack GTPase activity and are predicted to exist in a constitutively active state.

Members of the Rho family have been identified in all eukaryotes. Including the atypical RHOBTB1-3 and RHOT1-2 proteins, 24 Rho family members have been identified in mammals (Jaffe and Hall, 2005; Bernards, 2005; Ridley, 2006). Among Rho GTPases, RhoA, Rac1 and Cdc42 have been most extensively studied. These proteins are best known for their ability to induce dynamic rearrangements of the plasma membrane-associated actin cytoskeleton (Aspenstrom et al, 2004; Murphy et al, 1999; Govek et al, 2005). Beyond this function, Rho GTPases also regulate actomyosin contractility and microtubule dynamics. Rho mediated effects on transcription and membrane trafficking are believed to be secondary to these functions. At the more macroscopic level, Rho GTPases have been implicated in many important cell biological processes, including cell growth control, cytokinesis, cell motility, cell cell and cell extracellular matrix adhesion, cell transformation and invasion, and development (Govek et al., 2005). The illustration below lists Rho GTPase effectors implicated in actin and microtubule dynamics (courtesy: Govek et al., 2005, Genes and Development, CSHL Press). Detailed annotations of various biological processes regulated by Rho GTPases will be available in future releases. View original pathway at:Reactome.</div>

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  22. Miki H, Yamaguchi H, Suetsugu S, Takenawa T.; ''IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling.''; PubMed Europe PMC Scholia
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  24. Miyano K, Ueno N, Takeya R, Sumimoto H.; ''Direct involvement of the small GTPase Rac in activation of the superoxide-producing NADPH oxidase Nox1.''; PubMed Europe PMC Scholia
  25. Sudo K, Ito H, Iwamoto I, Morishita R, Asano T, Nagata K.; ''Identification of a cell polarity-related protein, Lin-7B, as a binding partner for a Rho effector, Rhotekin, and their possible interaction in neurons.''; PubMed Europe PMC Scholia
  26. Metzger E, Müller JM, Ferrari S, Buettner R, Schüle R.; ''A novel inducible transactivation domain in the androgen receptor: implications for PRK in prostate cancer.''; PubMed Europe PMC Scholia
  27. Manser E, Leung T, Salihuddin H, Zhao ZS, Lim L.; ''A brain serine/threonine protein kinase activated by Cdc42 and Rac1.''; PubMed Europe PMC Scholia
  28. Fujita A, Nakamura K, Kato T, Watanabe N, Ishizaki T, Kimura K, Mizoguchi A, Narumiya S.; ''Ropporin, a sperm-specific binding protein of rhophilin, that is localized in the fibrous sheath of sperm flagella.''; PubMed Europe PMC Scholia
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  31. Leung T, Chen XQ, Manser E, Lim L.; ''The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton.''; PubMed Europe PMC Scholia
  32. Sun J, Barbieri JT.; ''ExoS Rho GTPase-activating protein activity stimulates reorganization of the actin cytoskeleton through Rho GTPase guanine nucleotide disassociation inhibitor.''; PubMed Europe PMC Scholia
  33. Hoffman GR, Nassar N, Cerione RA.; ''Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI.''; PubMed Europe PMC Scholia
  34. Gosser YQ, Nomanbhoy TK, Aghazadeh B, Manor D, Combs C, Cerione RA, Rosen MK.; ''C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases.''; PubMed Europe PMC Scholia
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  36. Madaule P, Furuyashiki T, Reid T, Ishizaki T, Watanabe G, Morii N, Narumiya S.; ''A novel partner for the GTP-bound forms of rho and rac.''; PubMed Europe PMC Scholia
  37. Zhou H, Kramer RH.; ''Integrin engagement differentially modulates epithelial cell motility by RhoA/ROCK and PAK1.''; PubMed Europe PMC Scholia
  38. Hage B, Meinel K, Baum I, Giehl K, Menke A.; ''Rac1 activation inhibits E-cadherin-mediated adherens junctions via binding to IQGAP1 in pancreatic carcinoma cells.''; PubMed Europe PMC Scholia
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  40. Soltau M, Richter D, Kreienkamp HJ.; ''The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42.''; PubMed Europe PMC Scholia
  41. Watanabe T, Hosoya H, Yonemura S.; ''Regulation of myosin II dynamics by phosphorylation and dephosphorylation of its light chain in epithelial cells.''; PubMed Europe PMC Scholia
  42. Hart MJ, Sharma S, elMasry N, Qiu RG, McCabe P, Polakis P, Bollag G.; ''Identification of a novel guanine nucleotide exchange factor for the Rho GTPase.''; PubMed Europe PMC Scholia
  43. Amano M, Ito M, Kimura K, Fukata Y, Chihara K, Nakano T, Matsuura Y, Kaibuchi K.; ''Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase).''; PubMed Europe PMC Scholia
  44. Maesaki R, Ihara K, Shimizu T, Kuroda S, Kaibuchi K, Hakoshima T.; ''The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1.''; PubMed Europe PMC Scholia
  45. Hutchinson CL, Lowe PN, McLaughlin SH, Mott HR, Owen D.; ''Differential binding of RhoA, RhoB, and RhoC to protein kinase C-related kinase (PRK) isoforms PRK1, PRK2, and PRK3: PRKs have the highest affinity for RhoB.''; PubMed Europe PMC Scholia
  46. Lane J, Martin T, Weeks HP, Jiang WG.; ''Structure and role of WASP and WAVE in Rho GTPase signalling in cancer.''; PubMed Europe PMC Scholia
  47. Govek EE, Newey SE, Van Aelst L.; ''The role of the Rho GTPases in neuronal development.''; PubMed Europe PMC Scholia
  48. Hart MJ, Maru Y, Leonard D, Witte ON, Evans T, Cerione RA.; ''A GDP dissociation inhibitor that serves as a GTPase inhibitor for the Ras-like protein CDC42Hs.''; PubMed Europe PMC Scholia
  49. Tan YC, Wu H, Wang WN, Zheng Y, Wang ZX.; ''Characterization of the interactions between the small GTPase RhoA and its guanine nucleotide exchange factors.''; PubMed Europe PMC Scholia
  50. Scheffzek K, Stephan I, Jensen ON, Illenberger D, Gierschik P.; ''The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI.''; PubMed Europe PMC Scholia
  51. Suzuki K, Takahashi K.; ''Regulation of lamellipodia formation and cell invasion by CLIP-170 in invasive human breast cancer cells.''; PubMed Europe PMC Scholia
  52. Torbett NE, Casamassima A, Parker PJ.; ''Hyperosmotic-induced protein kinase N 1 activation in a vesicular compartment is dependent upon Rac1 and 3-phosphoinositide-dependent kinase 1.''; PubMed Europe PMC Scholia
  53. Bächner D, Sedlacek Z, Korn B, Hameister H, Poustka A.; ''Expression patterns of two human genes coding for different rab GDP-dissociation inhibitors (GDIs), extremely conserved proteins involved in cellular transport.''; PubMed Europe PMC Scholia
  54. Pasteris NG, Cadle A, Logie LJ, Porteous ME, Schwartz CE, Stevenson RE, Glover TW, Wilroy RS, Gorski JL.; ''Isolation and characterization of the faciogenital dysplasia (Aarskog-Scott syndrome) gene: a putative Rho/Rac guanine nucleotide exchange factor.''; PubMed Europe PMC Scholia
  55. Robbe K, Otto-Bruc A, Chardin P, Antonny B.; ''Dissociation of GDP dissociation inhibitor and membrane translocation are required for efficient activation of Rac by the Dbl homology-pleckstrin homology region of Tiam.''; PubMed Europe PMC Scholia
  56. DerMardirossian C, Bokoch GM.; ''GDIs: central regulatory molecules in Rho GTPase activation.''; PubMed Europe PMC Scholia
  57. Metzger E, Yin N, Wissmann M, Kunowska N, Fischer K, Friedrichs N, Patnaik D, Higgins JM, Potier N, Scheidtmann KH, Buettner R, Schüle R.; ''Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation.''; PubMed Europe PMC Scholia
  58. Parrini MC, Lei M, Harrison SC, Mayer BJ.; ''Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.''; PubMed Europe PMC Scholia
  59. Lancaster CA, Taylor-Harris PM, Self AJ, Brill S, van Erp HE, Hall A.; ''Characterization of rhoGAP. A GTPase-activating protein for rho-related small GTPases.''; PubMed Europe PMC Scholia
  60. Bashour AM, Fullerton AT, Hart MJ, Bloom GS.; ''IQGAP1, a Rac- and Cdc42-binding protein, directly binds and cross-links microfilaments.''; PubMed Europe PMC Scholia
  61. Ueyama T, Geiszt M, Leto TL.; ''Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-based NADPH oxidases.''; PubMed Europe PMC Scholia
  62. Swart-Mataraza JM, Li Z, Sacks DB.; ''IQGAP1 is a component of Cdc42 signaling to the cytoskeleton.''; PubMed Europe PMC Scholia
  63. Hamaguchi T, Ito M, Feng J, Seko T, Koyama M, Machida H, Takase K, Amano M, Kaibuchi K, Hartshorne DJ, Nakano T.; ''Phosphorylation of CPI-17, an inhibitor of myosin phosphatase, by protein kinase N.''; PubMed Europe PMC Scholia
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  65. Watanabe G, Saito Y, Madaule P, Ishizaki T, Fujisawa K, Morii N, Mukai H, Ono Y, Kakizuka A, Narumiya S.; ''Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho.''; PubMed Europe PMC Scholia
  66. Schmidt A, Hall A.; ''Guanine nucleotide exchange factors for Rho GTPases: turning on the switch.''; PubMed Europe PMC Scholia
  67. Govind S, Kozma R, Monfries C, Lim L, Ahmed S.; ''Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin.''; PubMed Europe PMC Scholia
  68. Camera P, da Silva JS, Griffiths G, Giuffrida MG, Ferrara L, Schubert V, Imarisio S, Silengo L, Dotti CG, Di Cunto F.; ''Citron-N is a neuronal Rho-associated protein involved in Golgi organization through actin cytoskeleton regulation.''; PubMed Europe PMC Scholia
  69. Cheng G, Diebold BA, Hughes Y, Lambeth JD.; ''Nox1-dependent reactive oxygen generation is regulated by Rac1.''; PubMed Europe PMC Scholia
  70. Flynn P, Mellor H, Casamassima A, Parker PJ.; ''Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase.''; PubMed Europe PMC Scholia
  71. Reynaud C, Fabre S, Jalinot P.; ''The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element.''; PubMed Europe PMC Scholia
  72. Sahai E, Marshall CJ.; ''RHO-GTPases and cancer.''; PubMed Europe PMC Scholia
  73. Ishizaki T, Maekawa M, Fujisawa K, Okawa K, Iwamatsu A, Fujita A, Watanabe N, Saito Y, Kakizuka A, Morii N, Narumiya S.; ''The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase.''; PubMed Europe PMC Scholia
  74. Edwards DC, Sanders LC, Bokoch GM, Gill GN.; ''Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics.''; PubMed Europe PMC Scholia
  75. Fainstein E, Marcelle C, Rosner A, Canaani E, Gale RP, Dreazen O, Smith SD, Croce CM.; ''A new fused transcript in Philadelphia chromosome positive acute lymphocytic leukaemia.''; PubMed Europe PMC Scholia
  76. Modha R, Campbell LJ, Nietlispach D, Buhecha HR, Owen D, Mott HR.; ''The Rac1 polybasic region is required for interaction with its effector PRK1.''; PubMed Europe PMC Scholia
  77. Neudauer CL, Joberty G, Macara IG.; ''PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10.''; PubMed Europe PMC Scholia
  78. Tcherkezian J, Lamarche-Vane N.; ''Current knowledge of the large RhoGAP family of proteins.''; PubMed Europe PMC Scholia
  79. Vignal E, Blangy A, Martin M, Gauthier-Rouvière C, Fort P.; ''Kinectin is a key effector of RhoG microtubule-dependent cellular activity.''; PubMed Europe PMC Scholia
  80. Zong H, Raman N, Mickelson-Young LA, Atkinson SJ, Quilliam LA.; ''Loop 6 of RhoA confers specificity for effector binding, stress fiber formation, and cellular transformation.''; PubMed Europe PMC Scholia
  81. Peck JW, Oberst M, Bouker KB, Bowden E, Burbelo PD.; ''The RhoA-binding protein, rhophilin-2, regulates actin cytoskeleton organization.''; PubMed Europe PMC Scholia
  82. Bassi ZI, Audusseau M, Riparbelli MG, Callaini G, D'Avino PP.; ''Citron kinase controls a molecular network required for midbody formation in cytokinesis.''; PubMed Europe PMC Scholia
  83. Jyoti A, Singh AK, Dubey M, Kumar S, Saluja R, Keshari RS, Verma A, Chandra T, Kumar A, Bajpai VK, Barthwal MK, Dikshit M.; ''Interaction of inducible nitric oxide synthase with rac2 regulates reactive oxygen and nitrogen species generation in the human neutrophil phagosomes: implication in microbial killing.''; PubMed Europe PMC Scholia
  84. Mircescu H, Steuve S, Savonet V, Degraef C, Mellor H, Dumont JE, Maenhaut C, Pirson I.; ''Identification and characterization of a novel activated RhoB binding protein containing a PDZ domain whose expression is specifically modulated in thyroid cells by cAMP.''; PubMed Europe PMC Scholia
  85. Metzger E, Wissmann M, Yin N, Müller JM, Schneider R, Peters AH, Günther T, Buettner R, Schüle R.; ''LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription.''; PubMed Europe PMC Scholia
  86. Adra CN, Manor D, Ko JL, Zhu S, Horiuchi T, Van Aelst L, Cerione RA, Lim B.; ''RhoGDIgamma: a GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas.''; PubMed Europe PMC Scholia
  87. Kuroda S, Fukata M, Nakagawa M, Fujii K, Nakamura T, Ookubo T, Izawa I, Nagase T, Nomura N, Tani H, Shoji I, Matsuura Y, Yonehara S, Kaibuchi K.; ''Role of IQGAP1, a target of the small GTPases Cdc42 and Rac1, in regulation of E-cadherin- mediated cell-cell adhesion.''; PubMed Europe PMC Scholia
  88. Van Aelst L, D'Souza-Schorey C.; ''Rho GTPases and signaling networks.''; PubMed Europe PMC Scholia
  89. Kühn S, Geyer M.; ''Formins as effector proteins of Rho GTPases.''; PubMed Europe PMC Scholia
  90. Hotta K, Tanaka K, Mino A, Kohno H, Takai Y.; ''Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor.''; PubMed Europe PMC Scholia
  91. Krugmann S, Anderson KE, Ridley SH, Risso N, McGregor A, Coadwell J, Davidson K, Eguinoa A, Ellson CD, Lipp P, Manifava M, Ktistakis N, Painter G, Thuring JW, Cooper MA, Lim ZY, Holmes AB, Dove SK, Michell RH, Grewal A, Nazarian A, Erdjument-Bromage H, Tempst P, Stephens LR, Hawkins PT.; ''Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices.''; PubMed Europe PMC Scholia
  92. Kim C, Dinauer MC.; ''Rac2 is an essential regulator of neutrophil nicotinamide adenine dinucleotide phosphate oxidase activation in response to specific signaling pathways.''; PubMed Europe PMC Scholia
  93. Fukata M, Watanabe T, Noritake J, Nakagawa M, Yamaga M, Kuroda S, Matsuura Y, Iwamatsu A, Perez F, Kaibuchi K.; ''Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170.''; PubMed Europe PMC Scholia
  94. Wang S, Watanabe T, Noritake J, Fukata M, Yoshimura T, Itoh N, Harada T, Nakagawa M, Matsuura Y, Arimura N, Kaibuchi K.; ''IQGAP3, a novel effector of Rac1 and Cdc42, regulates neurite outgrowth.''; PubMed Europe PMC Scholia
  95. Ren Y, Li R, Zheng Y, Busch H.; ''Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases.''; PubMed Europe PMC Scholia
  96. Hutchinson CL, Lowe PN, McLaughlin SH, Mott HR, Owen D.; ''Mutational analysis reveals a single binding interface between RhoA and its effector, PRK1.''; PubMed Europe PMC Scholia
  97. Fukata M, Kuroda S, Fujii K, Nakamura T, Shoji I, Matsuura Y, Okawa K, Iwamatsu A, Kikuchi A, Kaibuchi K.; ''Regulation of cross-linking of actin filament by IQGAP1, a target for Cdc42.''; PubMed Europe PMC Scholia
  98. Miralles F, Posern G, Zaromytidou AI, Treisman R.; ''Actin dynamics control SRF activity by regulation of its coactivator MAL.''; PubMed Europe PMC Scholia
  99. Leung DW, Rosen MK.; ''The nucleotide switch in Cdc42 modulates coupling between the GTPase-binding and allosteric equilibria of Wiskott-Aldrich syndrome protein.''; PubMed Europe PMC Scholia
  100. Richnau N, Aspenström P.; ''Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1.''; PubMed Europe PMC Scholia
  101. Brill S, Li S, Lyman CW, Church DM, Wasmuth JJ, Weissbach L, Bernards A, Snijders AJ.; ''The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases.''; PubMed Europe PMC Scholia


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101394view11:28, 1 November 2018ReactomeTeamreactome version 66
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99569view14:54, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
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93909view13:44, 16 August 2017ReactomeTeamreactome version 61
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83049view09:47, 18 November 2015ReactomeTeamVersion54
81350view12:52, 21 August 2015ReactomeTeamVersion53
76820view08:04, 17 July 2014ReactomeTeamFixed remaining interactions
76524view11:45, 16 July 2014ReactomeTeamFixed remaining interactions
75857view09:50, 11 June 2014ReactomeTeamRe-fixing comment source
75557view10:35, 10 June 2014ReactomeTeamReactome 48 Update
74912view13:44, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74556view08:35, 30 April 2014ReactomeTeamReactome46
68961view17:39, 8 July 2013MaintBotUpdated to 2013 gpml schema
45211view17:23, 7 October 2011KhanspersOntology Term : 'signaling pathway' added !
42133view21:59, 4 March 2011MaintBotAutomatic update
39943view05:57, 21 January 2011MaintBotNew pathway

External references


View all...
NameTypeDatabase referenceComment
A2M ProteinP01023 (Uniprot-TrEMBL)
ABR ProteinQ12979 (Uniprot-TrEMBL)
AKAP13 ProteinQ12802 (Uniprot-TrEMBL)
ARAP1 ProteinQ96P48 (Uniprot-TrEMBL)
ARAP2 ProteinQ8WZ64 (Uniprot-TrEMBL)
ARAP3 ProteinQ8WWN8 (Uniprot-TrEMBL)
ARHGAP1 ProteinQ07960 (Uniprot-TrEMBL)
ARHGAP10 ProteinA1A4S6 (Uniprot-TrEMBL)
ARHGAP11A ProteinQ6P4F7 (Uniprot-TrEMBL)
ARHGAP11B ProteinQ3KRB8 (Uniprot-TrEMBL)
ARHGAP12 ProteinQ8IWW6 (Uniprot-TrEMBL)
ARHGAP15 ProteinQ53QZ3 (Uniprot-TrEMBL)
ARHGAP17 ProteinQ68EM7 (Uniprot-TrEMBL)
ARHGAP18 ProteinQ8N392 (Uniprot-TrEMBL)
ARHGAP19 ProteinQ14CB8 (Uniprot-TrEMBL)
ARHGAP20 ProteinQ9P2F6 (Uniprot-TrEMBL)
ARHGAP22 ProteinQ7Z5H3 (Uniprot-TrEMBL)
ARHGAP23 ProteinQ9P227 (Uniprot-TrEMBL)
ARHGAP24 ProteinQ8N264 (Uniprot-TrEMBL)
ARHGAP25 ProteinP42331 (Uniprot-TrEMBL)
ARHGAP26 ProteinQ9UNA1 (Uniprot-TrEMBL)
ARHGAP28 ProteinQ9P2N2 (Uniprot-TrEMBL)
ARHGAP29 ProteinQ52LW3 (Uniprot-TrEMBL)
ARHGAP30 ProteinQ7Z6I6 (Uniprot-TrEMBL)
ARHGAP31 ProteinQ2M1Z3 (Uniprot-TrEMBL)
ARHGAP32 ProteinA7KAX9 (Uniprot-TrEMBL)
ARHGAP33 ProteinO14559 (Uniprot-TrEMBL)
ARHGAP36 ProteinQ6ZRI8 (Uniprot-TrEMBL)
ARHGAP39 ProteinQ9C0H5 (Uniprot-TrEMBL)
ARHGAP4 ProteinP98171 (Uniprot-TrEMBL)
ARHGAP40 ProteinQ5TG30 (Uniprot-TrEMBL)
ARHGAP44 ProteinQ17R89 (Uniprot-TrEMBL)
ARHGAP6 ProteinO43182 (Uniprot-TrEMBL)
ARHGAP8 ProteinP85298 (Uniprot-TrEMBL)
ARHGAP9 ProteinQ9BRR9 (Uniprot-TrEMBL)
ARHGDIA ProteinP52565 (Uniprot-TrEMBL)
ARHGDIB ProteinP52566 (Uniprot-TrEMBL)
ARHGDIG ProteinQ99819 (Uniprot-TrEMBL)
ARHGEF11 ProteinO15085 (Uniprot-TrEMBL)
ARHGEF12 ProteinQ9NZN5 (Uniprot-TrEMBL)
ARHGEF16 ProteinQ5VV41 (Uniprot-TrEMBL)
ARHGEF17 ProteinQ96PE2 (Uniprot-TrEMBL)
ARHGEF18 ProteinQ6ZSZ5 (Uniprot-TrEMBL)
ARHGEF2 ProteinQ92974 (Uniprot-TrEMBL)
ARHGEF3 ProteinQ9NR81 (Uniprot-TrEMBL)
ARHGEF4 ProteinQ9NR80 (Uniprot-TrEMBL)
ARHGEF6 ProteinQ15052 (Uniprot-TrEMBL)
ARHGEF7 ProteinQ14155 (Uniprot-TrEMBL)
ARHGEF9 ProteinO43307 (Uniprot-TrEMBL)
BCR ProteinP11274 (Uniprot-TrEMBL)
BPGAP1(1-?) ProteinQ8IZM6 (Uniprot-TrEMBL)
CDC42 ProteinP60953 (Uniprot-TrEMBL)
CHN1 ProteinP15882 (Uniprot-TrEMBL)
CHN2 ProteinP52757 (Uniprot-TrEMBL)
DEPDC1B ProteinQ8WUY9 (Uniprot-TrEMBL)
DEPDC7 ProteinQ96QD5 (Uniprot-TrEMBL)
DLC1 ProteinQ96QB1 (Uniprot-TrEMBL)
ECT2 ProteinQ9H8V3 (Uniprot-TrEMBL)
FAM13A ProteinO94988 (Uniprot-TrEMBL)
FAM13B ProteinQ9NYF5 (Uniprot-TrEMBL)
FGD1 ProteinP98174 (Uniprot-TrEMBL)
FGD2 ProteinQ7Z6J4 (Uniprot-TrEMBL)
FGD3 ProteinQ5JSP0 (Uniprot-TrEMBL)
FGD4 ProteinQ96M96 (Uniprot-TrEMBL)
GAP proteinsComplexR-HSA-194904 (Reactome)
GDI proteinsComplexR-HSA-194862 (Reactome)
GDI1 ProteinP31150 (Uniprot-TrEMBL)
GDI2 ProteinP50395 (Uniprot-TrEMBL)
GDP MetaboliteCHEBI:17552 (ChEBI)
GDPMetaboliteCHEBI:17552 (ChEBI)
GEFComplexR-HSA-194849 (Reactome)
GMIP ProteinQ9P107 (Uniprot-TrEMBL)
GTP MetaboliteCHEBI:15996 (ChEBI)
GTPMetaboliteCHEBI:15996 (ChEBI)
HMHA1 ProteinQ92619 (Uniprot-TrEMBL)
INPP5B(321-993) ProteinP32019 (Uniprot-TrEMBL)
ITSN1 ProteinQ15811 (Uniprot-TrEMBL)


ComplexR-HSA-194912 (Reactome)
KALRN ProteinO60229 (Uniprot-TrEMBL)
MCF2(1-925) ProteinP10911 (Uniprot-TrEMBL)
MCF2L ProteinO15068 (Uniprot-TrEMBL)
MYO9A ProteinB2RTY4 (Uniprot-TrEMBL)
MYO9B ProteinQ13459 (Uniprot-TrEMBL)
NET1 ProteinQ7Z628 (Uniprot-TrEMBL)
NGEF ProteinQ8N5V2 (Uniprot-TrEMBL)
OBSCN ProteinQ5VST9 (Uniprot-TrEMBL)
OCRL ProteinQ01968 (Uniprot-TrEMBL)
OPHN1 ProteinO60890 (Uniprot-TrEMBL)
PIK3R2 ProteinO00459 (Uniprot-TrEMBL)
PLEKHG2 ProteinQ9H7P9 (Uniprot-TrEMBL)
PLEKHG5 ProteinO94827 (Uniprot-TrEMBL)
PiMetaboliteCHEBI:18367 (ChEBI)
RAC1 ProteinP63000 (Uniprot-TrEMBL)
RAC2 ProteinP15153 (Uniprot-TrEMBL)
RAC3 ProteinP60763 (Uniprot-TrEMBL)
RACGAP1 ProteinQ9H0H5 (Uniprot-TrEMBL)
RALBP1 ProteinQ15311 (Uniprot-TrEMBL)
RASGRF2 ProteinO14827 (Uniprot-TrEMBL)
RHO GTPase EffectorsPathwayR-HSA-195258 (Reactome) RHO GTPases regulate cell behaviour by activating a number of downstream effectors that regulate cytoskeletal organization, intracellular trafficking and transcription (reviewed by Sahai and Marshall 2002).

One of the best studied RHO GTPase effectors are protein kinases ROCK1 and ROCK2, which are activated by binding RHOA, RHOB or RHOC. ROCK1 and ROCK2 phosphorylate many proteins involved in the stabilization of actin filaments and generation of actin-myosin contractile force, such as LIM kinases and myosin regulatory light chains (MRLC) (Amano et al. 1996, Ishizaki et al. 1996, Leung et al. 1996, Ohashi et al. 2000, Sumi et al. 2001, Riento and Ridley 2003, Watanabe et al. 2007).

PAK1, PAK2 and PAK3, members of the p21-activated kinase family, are activated by binding to RHO GTPases RAC1 and CDC42 and subsequent autophosphorylation and are involved in cytoskeleton regulation (Manser et al. 1994, Manser et al. 1995, Zhang et al. 1998, Edwards et al. 1999, Lei et al. 2000, Parrini et al. 2002; reviewed by Daniels and Bokoch 1999, Szczepanowska 2009).

RHOA, RHOB, RHOC and RAC1 activate protein kinase C related kinases (PKNs) PKN1, PKN2 and PKN3 (Maesaki et al. 1999, Zong et al. 1999, Owen et al. 2003, Modha et al. 2008, Hutchinson et al. 2011, Hutchinson et al. 2013), bringing them in proximity to the PIP3-activated PDPK1 (PDK1) and thus enabling PDPK1-mediated phosphorylation of PKN1, PKN2 and PKN3 (Flynn et al. 2000, Torbett et al. 2003). PKNs play important roles in cytoskeleton organization (Hamaguchi et al. 2000), regulation of cell cycle (Misaki et al. 2001), receptor trafficking (Metzger et al. 2003) and apoptosis (Takahashi et al. 1998). PKN1 is also involved in the ligand-dependent transcriptional activation by the androgen receptor (Metzger et al. 2003, Metzger et al. 2005, Metzger et al. 2008).

Citron kinase (CIT) binds RHO GTPases RHOA, RHOB, RHOC and RAC1 (Madaule et al. 1995), but the mechanism of CIT activation by GTP-bound RHO GTPases has not been elucidated. CIT and RHOA are implicated to act together in Golgi apparatus organization through regulation of the actin cytoskeleton (Camera et al. 2003). CIT is also involved in the regulation of cytokinesis through its interaction with KIF14 (Gruneberg et al. 2006, Bassi et al. 2013, Watanabe et al. 2013).

RHOA, RHOG, RAC1 and CDC42 bind kinectin (KTN1), a kinesin anchor protein involved in kinesin-mediated vesicle motility (Vignal et al. 2001, Hotta et al. 1996). The effect of RHOG activity on cellular morphology, exhibited in the formation of microtubule-dependent cellular protrusions, depends both on RHOG interaction with KTN1, as well as on the kinesin activity (Vignal et al. 2001). RHOG and KTN1 also cooperate in microtubule-dependent lysosomal transport (Vignal et al. 2001).

IQGAP proteins IQGAP1, IQGAP2 and IQGAP3, bind RAC1 and CDC42 and stabilize them in their GTP-bound state (Kuroda et al. 1996, Swart-Mataraza et al. 2002, Wang et al. 2007). IQGAPs bind F-actin filaments and modulate cell shape and motility through regulation of G-actin/F-actin equilibrium (Brill et al. 1996, Fukata et al. 1997, Bashour et al. 1997, Wang et al. 2007, Pelikan-Conchaudron et al. 2011). Binding of IQGAPs to F-actin is inhibited by calmodulin (Bashour et al. 1997, Pelikan-Conchaudron et al. 2011). IQGAP1 is involved in the regulation of adherens junctions through its interaction with E-cadherin (CDH1) and catenins (CTTNB1 and CTTNA1) (Kuroda et al. 1998, Hage et al. 2009). IQGAP1 contributes to cell polarity and lamellipodia formation through its interaction with microtubules (Fukata et al. 2002, Suzuki and Takahashi 2008).

RHOQ (TC10) regulates the trafficking of CFTR (cystic fibrosis transmembrane conductance regulator) by binding to the Golgi-associated protein GOPC (also known as PIST, FIG and CAL). In the absence of RHOQ, GOPC bound to CFTR directs CFTR for lysosomal degradation, while GTP-bound RHOQ directs GOPC:CFTR complex to the plasma membrane, thereby rescuing CFTR (Neudauer et al. 2001, Cheng et al. 2005).

RAC1 and CDC42 activate WASP and WAVE proteins, members of the Wiskott-Aldrich Syndrome protein family. WASPs and WAVEs simultaneously interact with G-actin and the actin-related ARP2/3 complex, acting as nucleation promoting factors in actin polymerization (reviewed by Lane et al. 2014).

RHOA, RHOB, RHOC, RAC1 and CDC42 activate a subset of formin family members. Once activated, formins bind G-actin and the actin-bound profilins and accelerate actin polymerization, while some formins also interact with microtubules. Formin-mediated cytoskeletal reorganization plays important roles in cell motility, organelle trafficking and mitosis (reviewed by Kuhn and Geyer 2014).

Rhotekin (RTKN) and rhophilins (RHPN1 and RHPN2) are effectors of RHOA, RHOB and RHOC and have not been studied in detail. They regulate the organization of the actin cytoskeleton and are implicated in the establishment of cell polarity, cell motility and possibly endosome trafficking (Sudo et al. 2006, Watanabe et al. 1996, Fujita et al. 2000, Peck et al. 2002, Mircescu et al. 2002). Similar to formins (Miralles et al. 2003), cytoskeletal changes triggered by RTKN activation may lead to stimulation of SRF-mediated transcription (Reynaud et al. 2000).

RHO GTPases RAC1 and RAC2 are needed for activation of NADPH oxidase complexes 1, 2 and 3 (NOX1, NOX2 and NOX3), membrane associated enzymatic complexes that use NADPH as an electron donor to reduce oxygen and produce superoxide (O2-). Superoxide serves as a secondary messenger and also directly contributes to the microbicidal activity of neutrophils (Knaus et al. 1991, Roberts et al. 1999, Kim and Dinauer 2001, Jyoti et al. 2014, Cheng et al. 2006, Miyano et al. 2006, Ueyama et al. 2006).

RHOA ProteinP61586 (Uniprot-TrEMBL)
RHOB ProteinP62745 (Uniprot-TrEMBL)
RHOC ProteinP08134 (Uniprot-TrEMBL)
RHOD ProteinO00212 (Uniprot-TrEMBL)
RHOF ProteinQ9HBH0 (Uniprot-TrEMBL)
RHOG ProteinP84095 (Uniprot-TrEMBL)
RHOH ProteinQ15669 (Uniprot-TrEMBL)
RHOJ ProteinQ9H4E5 (Uniprot-TrEMBL)
RHOQ ProteinP17081 (Uniprot-TrEMBL)
RHOT1 ProteinQ8IXI2 (Uniprot-TrEMBL)
RHOT2 ProteinQ8IXI1 (Uniprot-TrEMBL)
RHOU ProteinQ7L0Q8 (Uniprot-TrEMBL)
RHOV ProteinQ96L33 (Uniprot-TrEMBL)
Rac R-HSA-195337 (Reactome)
RhoBTB R-HSA-194873 (Reactome)
RhoBTB R-HSA-194916 (Reactome)
RhoGTPase:GDPComplexR-HSA-194900 (Reactome)
RhoGTPase:GDPComplexR-HSA-194915 (Reactome)
RhoGTPase:GTP:Effectors complexComplexR-HSA-194875 (Reactome)
RhoGTPase:GTPComplexR-HSA-194890 (Reactome)
SOS1 ProteinQ07889 (Uniprot-TrEMBL)
SOS2 ProteinQ07890 (Uniprot-TrEMBL)
SRGAP1 ProteinQ7Z6B7 (Uniprot-TrEMBL)
SRGAP2 ProteinO75044 (Uniprot-TrEMBL)
SRGAP3 ProteinO43295 (Uniprot-TrEMBL)
STARD13 ProteinQ9Y3M8 (Uniprot-TrEMBL)
STARD8 ProteinQ92502 (Uniprot-TrEMBL)
SYDE1 ProteinQ6ZW31 (Uniprot-TrEMBL)
SYDE2 ProteinQ5VT97 (Uniprot-TrEMBL)
TAGAP ProteinQ8N103 (Uniprot-TrEMBL)
TIAM1 ProteinQ13009 (Uniprot-TrEMBL)
TIAM2 ProteinQ8IVF5 (Uniprot-TrEMBL)
TRIO ProteinO75962 (Uniprot-TrEMBL)
TRIP10 ProteinQ15642 (Uniprot-TrEMBL)
VAV1 ProteinP15498 (Uniprot-TrEMBL)
VAV2 ProteinP52735 (Uniprot-TrEMBL)
VAV3 ProteinQ9UKW4 (Uniprot-TrEMBL)
effector proteins R-HSA-194872 (Reactome)
effector proteinsR-HSA-194872 (Reactome)
p190 R-HSA-195116 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
GAP proteinsmim-catalysisR-HSA-194922 (Reactome)
GDI proteinsArrowR-HSA-195146 (Reactome)
GDI proteinsR-HSA-194854 (Reactome)
GDPArrowR-HSA-194913 (Reactome)
GEFmim-catalysisR-HSA-194913 (Reactome)
GTPR-HSA-194913 (Reactome)


ArrowR-HSA-194854 (Reactome)


R-HSA-195146 (Reactome)
PiArrowR-HSA-194922 (Reactome)
R-HSA-194854 (Reactome) GDP dissociation inhibitors or GDIs confer an additional but important layer of Rho GTPase regulation along with GEFs and GAPs. GDIs mainly inhibit the dissociation of bound guanine nucleotide (usually GDP) from their partner GTPases. So far, three human GDIs with proven biological functions have been found: RhoGDI/GDIalpha/GDI1, hematopoietic cell selective Ly/D4GDI/GDIbeta/GDI2, and Rho GDIgamma/GDI3 (DerMardirossian and Bokoch, 2005). Three specific biochemical functions of GDIs have been established: inhibiting the dissociation of GDP from Rho proteins, maintaining the GTPases in an inactive form, and preventing GTPase activation by GEFs (Olofsson, 1999). Detailed annotations of GDIs will be available in future releases.
R-HSA-194894 (Reactome) To transduce signals, the activated, GTP-bound Rho GTPases interact with specific effector molecules. It has been observed that GEFs contribute to the signaling specificity of their downstream target GTPase via association with scaffolding molecules that link them and the GTPase to specific GTPase effectors (Govek et al., 2005). Some of the effector molecules implicated in actin and microtubule dynamics include diaphanous-related formins, Toca 1, WIP, WASP, Pak, p35/Cdk5, Wave, Nap125, MLCK, MLC, IRSp53. Detailed annotations of the downstream events stimulated by activated, GTP bound Rho GTPases will be available in future releases.
R-HSA-194913 (Reactome) Guanine nucleotide exchange factors (GEFs) activate GTPases by enhancing the exchange of bound GDP for GTP. Much evidence points to GEFs being critical mediators of Rho GTPase activation (Schmidt and Hall, 2002). Many GEFs are known to be highly specific for a particular GTPase, e.g. Fgd1/Cdc42 and p115RhoGEF/Rho (Hart et al., 1996, Zheng et al., 1996). Others have a broader spectrum and activate several GTPases, e.g. Vav1 for Rac, Rho, and Cdc42 (Hart et al, 1994).
R-HSA-194922 (Reactome) The human genome includes approximately 70 genes that are predicted to encode Rho-specific GTPase Activating Proteins (RhoGAPs). As in the case of GEFs, some RhoGAPs are believed to be highly specific, whereas others are more promiscuous with respect to their target GTPases. Increasing evidence suggests that GAPs are also regulated by external cues in addition to being signal terminators leading to Rho GTPase inactivation. These proteins play important role in many Rho mediated signaling pathways.

Some known GAPs include p190 A, cdGAP, ARAP3, MgcRacGAP, Chimaerin, Nadrin, TCGAP, DLC 1, 2, ArhGAP6, Myosin IXA. These and other GAPs have been implicated in many processes, such as exocytosis, endocytosis, cytokinesis, cell differentiation, migration, neuronal morphogenesis, angiogenesis and tumor suppression. Detailed annotations of the biological role of GAPs in Rho mediated signaling will be available in future releases.

R-HSA-195146 (Reactome) GDIs sequester the inactive GTPases, preventing the dissociation of GDP and interactions with regulatory and effector molecules. They maintain Rho GTPases as soluble cytosolic proteins by forming high affinity complexes. In these complexes, the geranylgeranyl membrane targeting moiety present at the C terminus of the Rho GTPases is shielded from the solvent by its insertion into the hydrophobic pocket formed by the immunoglobulin like beta sandwich of the GDI (DerMardirossian and Bokoch, 2005).

Rho proteins, when released from the sequestering cytosolic GDIs, insert into the lipid bilayer of the plasma membrane with their isoprenylated C termini. The membrane bound GEFs activate these free RhoGTPases and thereby trigger the downstream signaling events via respective effector proteins on the membrane (Robbe et al., 2003). Detailed annotation of the activities of farnesyltransferase / geranylgeranyltransferases on prenylation of Rho GTPases thereby enabling their subsequent localization to plasma membrane will be available in future releases.

RhoGTPase:GDPArrowR-HSA-194922 (Reactome)
RhoGTPase:GDPArrowR-HSA-195146 (Reactome)
RhoGTPase:GDPR-HSA-194854 (Reactome)
RhoGTPase:GDPR-HSA-194913 (Reactome)
RhoGTPase:GTP:Effectors complexArrowR-HSA-194894 (Reactome)
RhoGTPase:GTPArrowR-HSA-194913 (Reactome)
RhoGTPase:GTPR-HSA-194894 (Reactome)
RhoGTPase:GTPR-HSA-194922 (Reactome)
effector proteinsR-HSA-194894 (Reactome)

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