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| == 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>. |
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| == Relevance == | | == Relevance == |
Revision as of 21:30, 5 October 2018
| Function
- Villin (VIL) is an actin-binding protein. It contains gelsolin-like domains in its N-terminal and a helical headpiece which binds actin[1].
- Supervillin (SVIL) contains numerous gelsolin-like domains in its C-terminal and interacts with actin[2].
- Advillin (AVIL) is another actin-binding protein in the gelsolin superfamily which is expressed in the peripheral sensory neurons.
- Cytovillin (CVIL) or ezrin or villin-2 serves as intermediate between plasma membrane and actin cytoskeleton[3].
Relevance
VIL immunohisochemistry is a reliable method for diagnosing microvillus inclusion disease (MVID)[4].
- ↑ 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:https://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:https://dx.doi.org/10.1097/PAS.0000000000000355
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3D Structures of Villin
Updated on 05-October-2018
{"openlevels":0}
- Supervillin
- Villin
- 3fg7 – hVIL gelsolin domains 4-6
- 2llf - hVIL gelsolin-like domain 6 - NMR
- 1unc – hVIL headpiece
- 3iur - hVIL headpiece H2H3 helices+prolyl endopeptidase – Aeromonas punctata
- 2rjw, 2rjx, 2rjv, 2rjy, 1yu7, 1yu8 – cVIL headpiece (mutant) – chicken
- 1yu5, 1qqv - cVIL headpiece
- 3myc, 3mye, 3nkj, 3mya, 3tjw, 3trv, 3trw, 3try - cVIL headpiece (mutant)
- 5i1n, 5i1o, 5i1p, 5i1s – cVIL-1 + cVIL headpiece
- 1vii, 2vik, 2vil, 4cz3, 4cz4 - cVIL headpiece - NMR
- 2ppz, 2jm0 - VIL headpiece (mutant) – synthetic – NMR
- 2f4k, 1wy3, 1wy4, 1yrf, 1yri - VIL fragment (mutant) – synthetic
- 5vnt - VIL-4 C-terminal headpiece - Arabidopsis thaliana - NMR
- Advillin
- Cytovillin or ezrin
References
