SVIL explained
Supervillin is a protein that in humans is encoded by the SVIL gene.[1] [2]
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.[3] 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.
Interactions
SVIL has been shown to interact with Androgen receptor.[4]
Further reading
- Pope RK, Pestonjamasp KN, Smith KP, Wulfkuhle JD, Strassel CP, Lawrence JB, Luna EJ. Cloning, characterization, and chromosomal localization of human supervillin (SVIL). Genomics. 52. 3. 342–51. Sep 1998. 9867483. 10.1006/geno.1998.5466.
- Wulfkuhle JD, Donina IE, Stark NH, Pope RK, Pestonjamasp KN, Niswonger ML, Luna EJ. Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals. Journal of Cell Science. 112 (Pt 13). 13. 2125–36. Jul 1999. 10.1242/jcs.112.13.2125. 10362542.
- Kim M, Jiang LH, Wilson HL, North RA, Surprenant A. Proteomic and functional evidence for a P2X7 receptor signalling complex. The EMBO Journal. 20. 22. 6347–58. Nov 2001. 11707406. 125721. 10.1093/emboj/20.22.6347.
- Ting HJ, Yeh S, Nishimura K, Chang C. Supervillin associates with androgen receptor and modulates its transcriptional activity. Proceedings of the National Academy of Sciences of the United States of America. 99. 2. 661–6. Jan 2002. 11792840. 117362. 10.1073/pnas.022469899. 2002PNAS...99..661T. free.
- Oh SW, Pope RK, Smith KP, Crowley JL, Nebl T, Lawrence JB, Luna EJ. Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton. Journal of Cell Science. 116. Pt 11. 2261–75. Jun 2003. 12711699. 10.1242/jcs.00422. free. 2022/26449. free.
- Chen Y, Takizawa N, Crowley JL, Oh SW, Gatto CL, Kambara T, Sato O, Li XD, Ikebe M, Luna EJ. F-actin and myosin II binding domains in supervillin. The Journal of Biological Chemistry. 278. 46. 46094–106. Nov 2003. 12917436. 10.1074/jbc.M305311200. free.
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP. Large-scale characterization of HeLa cell nuclear phosphoproteins. Proceedings of the National Academy of Sciences of the United States of America. 101. 33. 12130–5. Aug 2004. 15302935. 514446. 10.1073/pnas.0404720101. 2004PNAS..10112130B. free.
- 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. Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. Current Biology. 14. 16. 1436–50. Aug 2004. 15324660. 10.1016/j.cub.2004.07.051. 2371325. free.
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 127. 3. 635–48. Nov 2006. 17081983. 10.1016/j.cell.2006.09.026. 7827573. free.
Notes and References
- Pestonjamasp KN, Pope RK, Wulfkuhle JD, Luna EJ . Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily . The Journal of Cell Biology . 139 . 5 . 1255–69 . Dec 1997 . 9382871 . 2140202 . 10.1083/jcb.139.5.1255 .
- Web site: Entrez Gene: SVIL supervillin.
- Ghoshdastider U, Popp D, Burtnick LD, Robinson RC . The expanding superfamily of gelsolin homology domain proteins . Cytoskeleton . 70 . 11 . 775–95 . Nov 2013 . 24155256 . 10.1002/cm.21149 . 205643538 .
- Ting HJ, Yeh S, Nishimura K, Chang C . Supervillin associates with androgen receptor and modulates its transcriptional activity . Proceedings of the National Academy of Sciences of the United States of America . 99 . 2 . 661–6 . Jan 2002 . 11792840 . 117362 . 10.1073/pnas.022469899 . 2002PNAS...99..661T . free .