Transforming protein RhoA

NameTransforming protein RhoA
Synonyms
  • ARH12
  • ARHA
  • h12
  • Rho cDNA clone 12
  • RHO12
Gene NameRHOA
OrganismHuman
Amino acid sequence
>lcl|BSEQ0021661|Transforming protein RhoA
MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDT
AGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKD
LRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQ
ARRGKKKSGCLVL
Number of residues193
Molecular Weight21767.94
Theoretical pI5.89
GO Classification
Functions
  • myosin binding
  • GDP binding
  • GTP binding
  • GTPase activity
Processes
  • cerebral cortex cell migration
  • positive regulation of neuron differentiation
  • regulation of actin cytoskeleton organization
  • regulation of axonogenesis
  • blood coagulation
  • androgen receptor signaling pathway
  • response to mechanical stimulus
  • positive regulation of cell migration
  • apical junction assembly
  • positive regulation of NF-kappaB import into nucleus
  • response to amino acid
  • neurotrophin TRK receptor signaling pathway
  • positive regulation of lipase activity
  • positive regulation of cytokinesis
  • positive regulation of translation
  • response to drug
  • transforming growth factor beta receptor signaling pathway
  • response to hypoxia
  • skeletal muscle satellite cell migration
  • regulation of neural precursor cell proliferation
  • wound healing, spreading of cells
  • positive regulation of alpha-beta T cell differentiation
  • vascular endothelial growth factor receptor signaling pathway
  • regulation of microtubule cytoskeleton organization
  • cell-matrix adhesion
  • positive regulation of stress fiber assembly
  • response to ethanol
  • positive regulation of smooth muscle contraction
  • positive regulation of axonogenesis
  • beta selection
  • positive regulation of cell growth
  • skeletal muscle tissue development
  • Rho protein signal transduction
  • small GTPase mediated signal transduction
  • negative regulation of neuron apoptotic process
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process
  • response to glucocorticoid
  • regulation of dendrite development
  • platelet activation
  • positive regulation of podosome assembly
  • positive regulation of actin filament polymerization
  • positive regulation of I-kappaB kinase/NF-kappaB signaling
  • alpha-beta T cell lineage commitment
  • regulation of cell migration
  • negative regulation of axonogenesis
  • regulation of transcription from RNA polymerase II promoter
  • regulation of osteoblast proliferation
  • regulation of calcium ion transport
  • forebrain radial glial cell differentiation
  • mitotic spindle assembly
  • response to glucose
  • negative regulation of I-kappaB kinase/NF-kappaB signaling
  • negative regulation of reactive oxygen species biosynthetic process
  • negative regulation of oxidative phosphorylation
  • ephrin receptor signaling pathway
  • positive regulation of neuron apoptotic process
  • apolipoprotein A-I-mediated signaling pathway
  • ossification involved in bone maturation
  • regulation of small GTPase mediated signal transduction
  • positive regulation of vasoconstriction
  • trabecula morphogenesis
  • negative chemotaxis
  • negative regulation of intracellular steroid hormone receptor signaling pathway
  • actin cytoskeleton organization
  • stress-activated protein kinase signaling cascade
  • substantia nigra development
  • stress fiber assembly
  • phosphatidylinositol-mediated signaling
  • axon guidance
  • cleavage furrow formation
  • viral process
Components
  • cytoskeleton
  • cell cortex
  • nucleus
  • midbody
  • plasma membrane
  • endoplasmic reticulum membrane
  • ruffle membrane
  • apical junction complex
  • cleavage furrow
  • endosome
  • vesicle
  • cell junction
  • cytosol
  • axon
  • mitochondrion
  • lamellipodium
  • extracellular exosome
  • cell periphery
  • focal adhesion
General FunctionMyosin binding
Specific FunctionRegulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis (PubMed:9635436, PubMed:19403695).(Microbial infection) Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID36030
UniProtKB IDP61586
UniProtKB Entry NameRHOA_HUMAN
Cellular LocationCell membrane
Gene sequence
>lcl|BSEQ0021662|Transforming protein RhoA (RHOA)
ATGGCTGCCATCCGGAAGAAACTGGTGATTGTTGGTGATGGAGCCTGTGGAAAGACATGC
TTGCTCATAGTCTTCAGCAAGGACCAGTTCCCAGAGGTGTATGTGCCCACAGTGTTTGAG
AACTATGTGGCAGATATCGAGGTGGATGGAAAGCAGGTAGAGTTGGCTTTGTGGGACACA
GCTGGGCAGGAAGATTATGATCGCCTGAGGCCCCTCTCCTACCCAGATACCGATGTTATA
CTGATGTGTTTTTCCATCGACAGCCCTGATAGTTTAGAAAACATCCCAGAAAAGTGGACC
CCAGAAGTCAAGCATTTCTGTCCCAACGTGCCCATCATCCTGGTTGGGAATAAGAAGGAT
CTTCGGAATGATGAGCACACAAGGCGGGAGCTAGCCAAGATGAAGCAGGAGCCGGTGAAA
CCTGAAGAAGGCAGAGATATGGCAAACAGGATTGGCGCTTTTGGGTACATGGAGTGTTCA
GCAAAGACCAAAGATGGAGTGAGAGAGGTTTTTGAAATGGCTACGAGAGCTGCTCTGCAA
GCTAGACGTGGGAAGAAAAAATCTGGGTGCCTTGTCTTGTGA
GenBank Gene IDX05026
GeneCard IDNot Available
GenAtlas IDRHOA
HGNC IDHGNC:667
Chromosome Location3
Locus3p21.3
References
  1. Yeramian P, Chardin P, Madaule P, Tavitian A: Nucleotide sequence of human rho cDNA clone 12. Nucleic Acids Res. 1987 Feb 25;15(4):1869. 3822842
  2. Fagan KP, Oliveira L, Pittler SJ: Sequence of rho small GTP-binding protein cDNAs from human retina and identification of novel 5' end cloning artifacts. Exp Eye Res. 1994 Aug;59(2):235-7. 7835413
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. 17974005
  4. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. 16641997
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334
  6. Moscow JA, He R, Gudas JM, Cowan KH: Utilization of multiple polyadenylation signals in the human RHOA protooncogene. Gene. 1994 Jul 8;144(2):229-36. 8039707
  7. Nemoto Y, Namba T, Teru-uchi T, Ushikubi F, Morii N, Narumiya S: A rho gene product in human blood platelets. I. Identification of the platelet substrate for botulinum C3 ADP-ribosyltransferase as rhoA protein. J Biol Chem. 1992 Oct 15;267(29):20916-20. 1328215
  8. Moscow JA, Morrow CS, He R, Mullenbach GT, Cowan KH: Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1). J Biol Chem. 1992 Mar 25;267(9):5949-58. 1556108
  9. 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. EMBO J. 1996 Apr 15;15(8):1885-93. 8617235
  10. Matsui T, Amano M, Yamamoto T, Chihara K, Nakafuku M, Ito M, Nakano T, Okawa K, Iwamatsu A, Kaibuchi K: Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho. EMBO J. 1996 May 1;15(9):2208-16. 8641286
  11. Quilliam LA, Lambert QT, Mickelson-Young LA, Westwick JK, Sparks AB, Kay BK, Jenkins NA, Gilbert DJ, Copeland NG, Der CJ: Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling. J Biol Chem. 1996 Nov 15;271(46):28772-6. 8910519
  12. Vincent S, Settleman J: The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization. Mol Cell Biol. 1997 Apr;17(4):2247-56. 9121475
  13. Cachero TG, Morielli AD, Peralta EG: The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel. Cell. 1998 Jun 12;93(6):1077-85. 9635436
  14. 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. J Biol Chem. 1998 Dec 25;273(52):34954-60. 9857026
  15. Houssa B, de Widt J, Kranenburg O, Moolenaar WH, van Blitterswijk WJ: Diacylglycerol kinase theta binds to and is negatively regulated by active RhoA. J Biol Chem. 1999 Mar 12;274(11):6820-2. 10066731
  16. Pastey MK, Crowe JE Jr, Graham BS: RhoA interacts with the fusion glycoprotein of respiratory syncytial virus and facilitates virus-induced syncytium formation. J Virol. 1999 Sep;73(9):7262-70. 10438814
  17. 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. J Biol Chem. 2000 Oct 27;275(43):33962-8. 10940294
  18. Sawada N, Itoh H, Yamashita J, Doi K, Inoue M, Masatsugu K, Fukunaga Y, Sakaguchi S, Sone M, Yamahara K, Yurugi T, Nakao K: cGMP-dependent protein kinase phosphorylates and inactivates RhoA. Biochem Biophys Res Commun. 2001 Jan 26;280(3):798-805. 11162591
  19. Klussmann E, Edemir B, Pepperle B, Tamma G, Henn V, Klauschenz E, Hundsrucker C, Maric K, Rosenthal W: Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling. FEBS Lett. 2001 Nov 2;507(3):264-8. 11696353
  20. Arthur WT, Ellerbroek SM, Der CJ, Burridge K, Wennerberg K: XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC. J Biol Chem. 2002 Nov 8;277(45):42964-72. Epub 2002 Sep 6. 12221096
  21. Shao F, Merritt PM, Bao Z, Innes RW, Dixon JE: A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis. Cell. 2002 May 31;109(5):575-88. 12062101
  22. Wing MR, Snyder JT, Sondek J, Harden TK: Direct activation of phospholipase C-epsilon by Rho. J Biol Chem. 2003 Oct 17;278(42):41253-8. Epub 2003 Aug 4. 12900402
  23. Shao F, Vacratsis PO, Bao Z, Bowers KE, Fierke CA, Dixon JE: Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases. Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):904-9. Epub 2003 Jan 21. 12538863
  24. Yuce O, Piekny A, Glotzer M: An ECT2-centralspindlin complex regulates the localization and function of RhoA. J Cell Biol. 2005 Aug 15;170(4):571-82. 16103226
  25. Kamijo K, Ohara N, Abe M, Uchimura T, Hosoya H, Lee JS, Miki T: Dissecting the role of Rho-mediated signaling in contractile ring formation. Mol Biol Cell. 2006 Jan;17(1):43-55. Epub 2005 Oct 19. 16236794
  26. Wolf A, Keil R, Gotzl O, Mun A, Schwarze K, Lederer M, Huttelmaier S, Hatzfeld M: The armadillo protein p0071 regulates Rho signalling during cytokinesis. Nat Cell Biol. 2006 Dec;8(12):1432-40. Epub 2006 Nov 19. 17115030
  27. Bristow JM, Sellers MH, Majumdar D, Anderson B, Hu L, Webb DJ: The Rho-family GEF Asef2 activates Rac to modulate adhesion and actin dynamics and thereby regulate cell migration. J Cell Sci. 2009 Dec 15;122(Pt 24):4535-46. doi: 10.1242/jcs.053728. Epub 2009 Nov 24. 19934221
  28. Stirling L, Williams MR, Morielli AD: Dual roles for RHOA/RHO-kinase in the regulated trafficking of a voltage-sensitive potassium channel. Mol Biol Cell. 2009 Jun;20(12):2991-3002. doi: 10.1091/mbc.E08-10-1074. Epub 2009 Apr 29. 19403695
  29. Worby CA, Mattoo S, Kruger RP, Corbeil LB, Koller A, Mendez JC, Zekarias B, Lazar C, Dixon JE: The fic domain: regulation of cell signaling by adenylylation. Mol Cell. 2009 Apr 10;34(1):93-103. doi: 10.1016/j.molcel.2009.03.008. 19362538
  30. Chen Y, Yang Z, Meng M, Zhao Y, Dong N, Yan H, Liu L, Ding M, Peng HB, Shao F: Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement. Mol Cell. 2009 Sep 24;35(6):841-55. doi: 10.1016/j.molcel.2009.09.004. 19782033
  31. Yarbrough ML, Li Y, Kinch LN, Grishin NV, Ball HL, Orth K: AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science. 2009 Jan 9;323(5911):269-72. doi: 10.1126/science.1166382. Epub 2008 Nov 27. 19039103
  32. Chatterjee A, Wang L, Armstrong DL, Rossie S: Activated Rac1 GTPase translocates protein phosphatase 5 to the cell membrane and stimulates phosphatase activity in vitro. J Biol Chem. 2010 Feb 5;285(6):3872-82. doi: 10.1074/jbc.M109.088427. Epub 2009 Nov 30. 19948726
  33. Boulter E, Garcia-Mata R, Guilluy C, Dubash A, Rossi G, Brennwald PJ, Burridge K: Regulation of Rho GTPase crosstalk, degradation and activity by RhoGDI1. Nat Cell Biol. 2010 May;12(5):477-83. doi: 10.1038/ncb2049. Epub 2010 Apr 18. 20400958
  34. Zaoui K, Benseddik K, Daou P, Salaun D, Badache A: ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells. Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18517-22. doi: 10.1073/pnas.1000975107. Epub 2010 Oct 11. 20937854
  35. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. 21269460
  36. Naji L, Pacholsky D, Aspenstrom P: ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics and cell adhesion. Biochem Biophys Res Commun. 2011 May 27;409(1):96-102. doi: 10.1016/j.bbrc.2011.04.116. Epub 2011 May 1. 21565175
  37. Cao XX, Xu JD, Xu JW, Liu XL, Cheng YY, Li QQ, Xu ZD, Liu XP: RACK1 promotes breast carcinoma migration/metastasis via activation of the RhoA/Rho kinase pathway. Breast Cancer Res Treat. 2011 Apr;126(3):555-63. doi: 10.1007/s10549-010-0955-3. Epub 2010 May 25. 20499158
  38. Wallace SW, Magalhaes A, Hall A: The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells. Mol Cell Biol. 2011 Jan;31(1):81-91. doi: 10.1128/MCB.01001-10. Epub 2010 Oct 25. 20974804
  39. Li D, Dammer EB, Lucki NC, Sewer MB: cAMP-stimulated phosphorylation of diaphanous 1 regulates protein stability and interaction with binding partners in adrenocortical cells. Mol Biol Cell. 2013 Mar;24(6):848-57. doi: 10.1091/mbc.E12-08-0597. Epub 2013 Jan 16. 23325789
  40. Jank T, Bogdanovic X, Wirth C, Haaf E, Spoerner M, Bohmer KE, Steinemann M, Orth JH, Kalbitzer HR, Warscheid B, Hunte C, Aktories K: A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins. Nat Struct Mol Biol. 2013 Nov;20(11):1273-80. doi: 10.1038/nsmb.2688. Epub 2013 Oct 20. 24141704
  41. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. 25944712
  42. Wei Y, Zhang Y, Derewenda U, Liu X, Minor W, Nakamoto RK, Somlyo AV, Somlyo AP, Derewenda ZS: Crystal structure of RhoA-GDP and its functional implications. Nat Struct Biol. 1997 Sep;4(9):699-703. 9302995
  43. Ihara K, Muraguchi S, Kato M, Shimizu T, Shirakawa M, Kuroda S, Kaibuchi K, Hakoshima T: Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue. J Biol Chem. 1998 Apr 17;273(16):9656-66. 9545299
  44. Maesaki R, Shimizu T, Ihara K, Kuroda S, Kaibuchi K, Hakoshima T: Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA. J Struct Biol. 1999 Jun 15;126(2):166-70. 10388627
  45. Shimizu T, Ihara K, Maesaki R, Kuroda S, Kaibuchi K, Hakoshima T: An open conformation of switch I revealed by the crystal structure of a Mg2+-free form of RHOA complexed with GDP. Implications for the GDP/GTP exchange mechanism. J Biol Chem. 2000 Jun 16;275(24):18311-7. 10748207
  46. Graham DL, Lowe PN, Grime GW, Marsh M, Rittinger K, Smerdon SJ, Gamblin SJ, Eccleston JF: MgF(3)(-) as a transition state analog of phosphoryl transfer. Chem Biol. 2002 Mar;9(3):375-81. 11927263
  47. Snyder JT, Worthylake DK, Rossman KL, Betts L, Pruitt WM, Siderovski DP, Der CJ, Sondek J: Structural basis for the selective activation of Rho GTPases by Dbl exchange factors. Nat Struct Biol. 2002 Jun;9(6):468-75. 12006984
  48. Longenecker K, Read P, Lin SK, Somlyo AP, Nakamoto RK, Derewenda ZS: Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A resolution. Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):876-80. Epub 2003 Apr 25. 12777804