{{Short description|Protein-coding gene in the species Homo sapiens}} {{Infobox_gene}} '''Supervillin''' is a protein that in humans is encoded by the ''SVIL'' gene.<ref name="pmid9382871">{{cite journal | vauthors = Pestonjamasp KN, Pope RK, Wulfkuhle JD, Luna EJ | title = Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily | journal = The Journal of Cell Biology | volume = 139 | issue = 5 | pages = 1255–69 | date = Dec 1997 | pmid = 9382871 | pmc = 2140202 | doi = 10.1083/jcb.139.5.1255 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SVIL supervillin| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=6840}}</ref>
== Function ==
This gene encodes a bipartite protein with distinct amino- and carboxy-terminal domains. The amino-terminus contains nuclear localization signals and the carboxy-terminus contains numerous consecutive sequences with extensive similarity to proteins in the gelsolin family of actin-binding proteins, which cap, nucleate, and/or sever actin filaments.<ref>{{cite journal | vauthors = Ghoshdastider U, Popp D, Burtnick LD, Robinson RC | title = The expanding superfamily of gelsolin homology domain proteins | journal = Cytoskeleton | volume = 70 | issue = 11 | pages = 775–95 | date = Nov 2013 | pmid = 24155256 | doi = 10.1002/cm.21149 | s2cid = 205643538 }}</ref> The gene product is tightly associated with both actin filaments and plasma membranes, suggesting a role as a high-affinity link between the actin cytoskeleton and the membrane. Its function may include recruitment of actin and other cytoskeletal proteins into specialized structures at the plasma membrane and in the nuclei of growing cells. Two transcript variants encoding different isoforms of supervillin have been described.<ref name="entrez" />
== Interactions ==
SVIL has been shown to interact with Androgen receptor.<ref name=pmid11792840>{{cite journal | vauthors = Ting HJ, Yeh S, Nishimura K, Chang C | title = Supervillin associates with androgen receptor and modulates its transcriptional activity | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 2 | pages = 661–6 | date = Jan 2002 | pmid = 11792840 | pmc = 117362 | doi = 10.1073/pnas.022469899 | bibcode = 2002PNAS...99..661T | doi-access = free }}</ref>
== References == {{reflist}}
== Further reading == {{refbegin|2}} * {{cite journal|vauthors=Pope RK, Pestonjamasp KN, Smith KP, Wulfkuhle JD, Strassel CP, Lawrence JB, Luna EJ|title=Cloning, characterization, and chromosomal localization of human supervillin (SVIL)|journal=Genomics|volume=52|issue=3|pages=342–51|date=Sep 1998|pmid=9867483|doi=10.1006/geno.1998.5466}} * {{cite journal|vauthors=Wulfkuhle JD, Donina IE, Stark NH, Pope RK, Pestonjamasp KN, Niswonger ML, Luna EJ|title=Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals|journal=Journal of Cell Science|volume=112 ( Pt 13)|issue=13|pages=2125–36|date=Jul 1999|doi=10.1242/jcs.112.13.2125|pmid=10362542|url=https://escholarship.umassmed.edu/wfc_pp/300}} * {{cite journal|vauthors=Kim M, Jiang LH, Wilson HL, North RA, Surprenant A|title=Proteomic and functional evidence for a P2X7 receptor signalling complex|journal=The EMBO Journal|volume=20|issue=22|pages=6347–58|date=Nov 2001|pmid=11707406|pmc=125721|doi=10.1093/emboj/20.22.6347}} * {{cite journal|vauthors=Ting HJ, Yeh S, Nishimura K, Chang C|title=Supervillin associates with androgen receptor and modulates its transcriptional activity|journal=Proceedings of the National Academy of Sciences of the United States of America|volume=99|issue=2|pages=661–6|date=Jan 2002|pmid=11792840|pmc=117362|doi=10.1073/pnas.022469899|bibcode=2002PNAS...99..661T|doi-access=free}} * {{cite journal|vauthors=Oh SW, Pope RK, Smith KP, Crowley JL, Nebl T, Lawrence JB, Luna EJ|title=Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton|journal=Journal of Cell Science|volume=116|issue=Pt 11|pages=2261–75|date=Jun 2003|pmid=12711699|doi=10.1242/jcs.00422|doi-access=free|hdl=2022/26449|hdl-access=free}} * {{cite journal|vauthors=Chen Y, Takizawa N, Crowley JL, Oh SW, Gatto CL, Kambara T, Sato O, Li XD, Ikebe M, Luna EJ|title=F-actin and myosin II binding domains in supervillin|journal=The Journal of Biological Chemistry|volume=278|issue=46|pages=46094–106|date=Nov 2003|pmid=12917436|doi=10.1074/jbc.M305311200|doi-access=free}} * {{cite journal|vauthors=Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP|title=Large-scale characterization of HeLa cell nuclear phosphoproteins|journal=Proceedings of the National Academy of Sciences of the United States of America|volume=101|issue=33|pages=12130–5|date=Aug 2004|pmid=15302935|pmc=514446|doi=10.1073/pnas.0404720101|bibcode=2004PNAS..10112130B|doi-access=free}} * {{cite journal|vauthors=Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T|title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization|journal=Current Biology|volume=14|issue=16|pages=1436–50|date=Aug 2004|pmid=15324660|doi=10.1016/j.cub.2004.07.051|s2cid=2371325|doi-access=free}} * {{cite journal|vauthors=Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M|title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks|journal=Cell|volume=127|issue=3|pages=635–48|date=Nov 2006|pmid=17081983|doi=10.1016/j.cell.2006.09.026|s2cid=7827573|doi-access=free}} {{refend}}
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