Rho gtpase activating protein 21
Rho GTPase activating protein 21 is a protein that in humans is encoded by the ARHGAP21 gene. [1]
Function
ARHGAP21 functions preferentially as a GTPase-activating protein (GAP) for CDC42 (MIM 116952) and regulates the ARP2/3 complex (MIM 604221) and F-actin dynamics at the Golgi through control of CDC42 activity (Dubois et al., 2005 [PubMed 15793564]).
References
- ↑ “Entrez Gene: Rho GTPase activating protein 21”. Retrieved 2017-01-30.
Further reading
- Bassères DS, Tizzei EV, Duarte AA, Costa FF, Saad ST (2002). “ARHGAP10, a novel human gene coding for a potentially cytoskeletal Rho-GTPase activating protein”. Biochem. Biophys. Res. Commun. 294 (3): 579–85. doi:10.1016/S0006-291X(02)00514-4. PMID 12056806.
- Dubois T, Paléotti O, Mironov AA, Fraisier V, Stradal TE, De Matteis MA, Franco M, Chavrier P (2005). “Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics”. Nat. Cell Biol. 7 (4): 353–64. doi:10.1038/ncb1244. PMID 15793564.
- Grupe A, Li Y, Rowland C, Nowotny P, Hinrichs AL, Smemo S, Kauwe JS, Maxwell TJ, Cherny S, Doil L, Tacey K, van Luchene R, Myers A, Wavrant-De Vrièze F, Kaleem M, Hollingworth P, Jehu L, Foy C, Archer N, Hamilton G, Holmans P, Morris CM, Catanese J, Sninsky J, White TJ, Powell J, Hardy J, O’Donovan M, Lovestone S, Jones L, Morris JC, Thal L, Owen M, Williams J, Goate A (2006). “A scan of chromosome 10 identifies a novel locus showing strong association with late-onset Alzheimer disease”. Am. J. Hum. Genet. 78 (1): 78–88. doi:10.1086/498851. PMC 1380225. PMID 16385451.
- Ménétrey J, Perderiset M, Cicolari J, Dubois T, Elkhatib N, El Khadali F, Franco M, Chavrier P, Houdusse A (2007). “Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi membranes”. EMBO J. 26 (7): 1953–62. doi:10.1038/sj.emboj.7601634. PMC 1847662. PMID 17347647.
- Bigarella CL, Borges L, Costa FF, Saad ST (2009). “ARHGAP21 modulates FAK activity and impairs glioblastoma cell migration”. Biochim. Biophys. Acta. 1793 (5): 806–16. doi:10.1016/j.bbamcr.2009.02.010. PMID 19268501.
- Anthony DF, Sin YY, Vadrevu S, Advant N, Day JP, Byrne AM, Lynch MJ, Milligan G, Houslay MD, Baillie GS (2011). “β-Arrestin 1 inhibits the GTPase-activating protein function of ARHGAP21, promoting activation of RhoA following angiotensin II type 1A receptor stimulation”. Mol. Cell. Biol. 31 (5): 1066–75. doi:10.1128/MCB.00883-10. PMC 3067824. PMID 21173159.
- Wang S, Li H, Chen Y, Wei H, Gao GF, Liu H, Huang S, Chen JL (2012). “Transport of influenza virus neuraminidase (NA) to host cell surface is regulated by ARHGAP21 and Cdc42 proteins”. J. Biol. Chem. 287 (13): 9804–16. doi:10.1074/jbc.M111.312959. PMC 3323004. PMID 22318733.
- Bigarella CL, Ferro KP, Barcellos KS, Martins-de-Souza D, Traina F, Novello JC, Saad ST, Archangelo LF (2012). “Post-translational modification of the RhoGTPase activating protein 21, ARHGAP21, by SUMO2/3”. FEBS Lett. 586 (19): 3522–8. doi:10.1016/j.febslet.2012.08.012. PMID 22922005.
- Barcellos KS, Bigarella CL, Wagner MV, Vieira KP, Lazarini M, Langford PR, Machado-Neto JA, Call SG, Staley DM, Chung JY, Hansen MD, Saad ST (2013). “ARHGAP21 protein, a new partner of α-tubulin involved in cell-cell adhesion formation and essential for epithelial-mesenchymal transition”. J. Biol. Chem. 288 (4): 2179–89. doi:10.1074/jbc.M112.432716. PMC 3554890. PMID 23235160.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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