Villin: Difference between revisions
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<StructureSection load=' | <StructureSection load='' size='340' side='right' caption='Human supervillin headpiece, [[2k6n]]' scene='Villin/Cv/1' > | ||
== Function == | == Function == | ||
* [[Villin]] (VIL) is an actin-binding protein. It contains gelsolin-like domains in its N-terminal and a helical headpiece which binds actin<ref>PMID:10480879</ref>.<br /> | * [[Villin]] (VIL) is an actin-binding protein. It contains gelsolin-like domains in its N-terminal and a helical headpiece which binds actin<ref>PMID:10480879</ref>.<br /> | ||
* '''Supervillin (SVIL)''' contains numerous gelsolin-like domains in its C-terminal and interacts with actin.<br /> | * '''Supervillin (SVIL)''' contains numerous gelsolin-like domains in its C-terminal and interacts with actin<ref>PMID:20309963</ref>.<br /> | ||
* '''Advillin (AVIL)''' is another actin-binding protein in the [[gelsolin]] superfamily which is expressed in the peripheral sensory neurons.<br /> | * '''Advillin (AVIL)''' is another actin-binding protein in the [[gelsolin]] superfamily which is expressed in the peripheral sensory neurons.<br /> | ||
* '''Cytovillin (CVIL) or ezrin or villin-2''' serves as intermediate between plasma membrane and actin cytoskeleton. | * '''Cytovillin (CVIL) or ezrin or villin-2''' serves as intermediate between plasma membrane and actin cytoskeleton<ref>PMID:8089177</ref>. | ||
== Relevance == | == Relevance == | ||
| Line 20: | Line 20: | ||
* Villin | * Villin | ||
**[[3fg7]] – hVIL gelsolin domains 4-6<br /> | **[[3fg7]] – hVIL-1 gelsolin domains 4-6<br /> | ||
**[[ | **[[1unc]] – hVIL-1 headpiece<br /> | ||
**[[ | **[[3iur]] - hVIL headpiece H2H3 helices + prolyl endopeptidase <br /> | ||
**[[ | **[[1yu5]], [[1qqv]] - cVIL headpiece - chicken<br /> | ||
**[[2rjw]], [[2rjx]], [[2rjv]], [[2rjy]], [[1yu7]], [[1yu8 | **[[2rjw]], [[2rjx]], [[2rjv]], [[2rjy]], [[1yu7]], [[1yu8]], [[3myc]], [[3mye]], [[3nkj]], [[3mya]], [[3tjw]], [[3trv]], [[3trw]], [[3try]] - cVIL-1 headpiece (mutant)<br /> | ||
**[[2llf]] - cVIL-1 gelsolin-like domain 6 - NMR<br /> | |||
**[[5i1n]], [[5i1o]], [[5i1p]], [[5i1s]] – cVIL-1 + cVIL headpiece<br /> | **[[5i1n]], [[5i1o]], [[5i1p]], [[5i1s]] – cVIL-1 + cVIL headpiece<br /> | ||
**[[1vii]], [[2vik]], [[2vil]], [[4cz3]], [[4cz4]] - cVIL headpiece - NMR<br /> | **[[1vii]], [[2vik]], [[2vil]], [[4cz3]], [[4cz4]] - cVIL-14T headpiece - NMR<br /> | ||
**[[2ppz]], [[2jm0]] - VIL headpiece (mutant) – synthetic – NMR<br /> | **[[2ppz]], [[2jm0]] - VIL-1 headpiece (mutant) – synthetic – NMR<br /> | ||
**[[2f4k]], [[1wy3]], [[1wy4]], [[1yrf]], [[1yri]] - VIL fragment (mutant) – synthetic<br /> | **[[2f4k]], [[1wy3]], [[1wy4]], [[1yrf]], [[1yri]] - VIL-1 fragment (mutant) – synthetic<br /> | ||
**[[5vnt]] - VIL-4 C-terminal headpiece - ''Arabidopsis thaliana'' - NMR<br /> | **[[5vnt]] - VIL-4 C-terminal headpiece - ''Arabidopsis thaliana'' - NMR<br /> | ||
Latest revision as of 11:29, 11 January 2021
Function
RelevanceVIL immunohisochemistry is a reliable method for diagnosing microvillus inclusion disease (MVID)[4]. |
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3D Structures of Villin3D Structures of Villin
Updated on 11-January-2021
ReferencesReferences
- ↑ Friederich E, Vancompernolle K, Louvard D, Vandekerckhove J. Villin function in the organization of the actin cytoskeleton. Correlation of in vivo effects to its biochemical activities in vitro. J Biol Chem. 1999 Sep 17;274(38):26751-60. PMID:10480879
- ↑ Smith TC, Fang Z, Luna EJ. Novel interactors and a role for supervillin in early cytokinesis. Cytoskeleton (Hoboken). 2010 Jun;67(6):346-64. doi: 10.1002/cm.20449. PMID:20309963 doi:http://dx.doi.org/10.1002/cm.20449
- ↑ Turunen O, Wahlstrom T, Vaheri A. Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family. J Cell Biol. 1994 Sep;126(6):1445-53. PMID:8089177
- ↑ Shillingford NM, Calicchio ML, Teot LA, Boyd T, Kurek KC, Goldsmith JD, Bousvaros A, Perez-Atayde AR, Kozakewich HP. Villin immunohistochemistry is a reliable method for diagnosing microvillus inclusion disease. Am J Surg Pathol. 2015 Feb;39(2):245-50. doi: 10.1097/PAS.0000000000000355. PMID:25517957 doi:http://dx.doi.org/10.1097/PAS.0000000000000355