Villin

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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].

Human supervillin headpiece, 2k6n

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3D Structures of Villin

Updated on 11-January-2021

References

  1. 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
  2. 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
  3. 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
  4. 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
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