Rho GTPase-activating protein 21
| ARHGAP21 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | ARHGAP21, ARHGAP10, Rho GTPase activating protein 21 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 609870; MGI: 1918685; HomoloGene: 10822; GeneCards: ARHGAP21; OMA:ARHGAP21 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Rho GTPase activating protein 21 is a protein that in humans is encoded by the ARHGAP21 gene.[5]
Function
[edit]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.[6] There is little scientific literature on ARHGAP21, but recent reviews highlighted that it plays an important role in cytoskeletal processes in cancer, substance transport within the cell, and insulin secretion [7]
References
[edit]- 1 2 3 GRCh38: Ensembl release 89: ENSG00000107863 – Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000036591 – Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Entrez Gene: Rho GTPase activating protein 21". Retrieved 2017-01-30.
- ↑ Dubois T, Paléotti O, Mironov AA, Fraisier V, Stradal TE, De Matteis MA, et al. (2005). "Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics". Nature Cell Biology. 7 (4): 353–364. doi:10.1038/ncb1244. PMID 15793564. S2CID 37000096.
- ↑ Rosa LR, Soares GM, Silveira LR, Boschero AC, Barbosa-Sampaio HC (November 2018). "ARHGAP21 as a master regulator of multiple cellular processes". Journal of Cellular Physiology. 233 (11): 8477–8481. doi:10.1002/jcp.26829. PMID 29856495. S2CID 46919924.
Further reading
[edit]- 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". Biochemical and Biophysical Research Communications. 294 (3): 579–585. doi:10.1016/S0006-291X(02)00514-4. PMID 12056806.
- Grupe A, Li Y, Rowland C, Nowotny P, Hinrichs AL, Smemo S, et al. (2006). "A scan of chromosome 10 identifies a novel locus showing strong association with late-onset Alzheimer disease". American Journal of Human Genetics. 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, et al. (2007). "Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi membranes". The EMBO Journal. 26 (7): 1953–1962. 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". Biochimica et Biophysica Acta. 1793 (5): 806–816. doi:10.1016/j.bbamcr.2009.02.010. PMID 19268501.
- Anthony DF, Sin YY, Vadrevu S, Advant N, Day JP, Byrne AM, et al. (2011). "β-Arrestin 1 inhibits the GTPase-activating protein function of ARHGAP21, promoting activation of RhoA following angiotensin II type 1A receptor stimulation". Molecular and Cellular Biology. 31 (5): 1066–1075. doi:10.1128/MCB.00883-10. PMC 3067824. PMID 21173159.
- Wang S, Li H, Chen Y, Wei H, Gao GF, Liu H, et al. (2012). "Transport of influenza virus neuraminidase (NA) to host cell surface is regulated by ARHGAP21 and Cdc42 proteins". The Journal of Biological Chemistry. 287 (13): 9804–9816. doi:10.1074/jbc.M111.312959. PMC 3323004. PMID 22318733.
- Bigarella CL, Ferro KP, Barcellos KS, Martins-de-Souza D, Traina F, Novello JC, et al. (2012). "Post-translational modification of the RhoGTPase activating protein 21, ARHGAP21, by SUMO2/3". FEBS Letters. 586 (19): 3522–3528. doi:10.1016/j.febslet.2012.08.012. PMID 22922005. S2CID 35663132.
- Barcellos KS, Bigarella CL, Wagner MV, Vieira KP, Lazarini M, Langford PR, et al. (2013). "ARHGAP21 protein, a new partner of α-tubulin involved in cell-cell adhesion formation and essential for epithelial-mesenchymal transition". The Journal of Biological Chemistry. 288 (4): 2179–2189. 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.