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Article
An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sites
Luna Lab
  • Stanislav O. Fedechkin, Western Washington University
  • Jacob Brockerman, Western Washington University
  • Elizabeth J. Luna, University of Massachusetts Medical School
  • Michail Yu. Lobanov, Russian Academy of Sciences
  • Oxana V. Galzitskaya, Russian Academy of Sciences
  • Serge L. Smirnov, Western Washington University
UMMS Affiliation
Department of Cell and Developmental Biology
Date
10-17-2012
Document Type
Article
Medical Subject Headings
Membrane Proteins; Microfilament Proteins
Abstract
Supervillin, the largest member of the villin/gelsolin family, is a cytoskeleton regulating, peripheral membrane protein. Supervillin increases cell motility and promotes invasive activity in tumors. Major cytoskeletal interactors, including filamentous actin and myosin II, bind within the unique supervillin amino terminus, amino acids 1-830. The structural features of this key region of the supervillin polypeptide are unknown. Here, we utilize circular dichroism and bioinformatics sequence analysis to demonstrate that the N-terminal part of supervillin forms an extended intrinsically disordered region (IDR). Our combined data indicate that the N-terminus of human and bovine supervillin sequences (positions 1-830) represents an IDR, which is the largest IDR known to date in the villin/gelsolin family. Moreover, this result suggests a potentially novel mechanism of regulation of myosin II and F-actin via the intrinsically disordered N-terminal region of hub protein supervillin.
Comments

Citation: J Biomol Struct Dyn. 2012 Oct 17. DOI: 10.1080/07391102.2012.726531

Related Resources
Link to article in PubMed
PubMed ID
23075227
Citation Information
Stanislav O. Fedechkin, Jacob Brockerman, Elizabeth J. Luna, Michail Yu. Lobanov, et al.. "An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sites" (2012) ISSN: 1538-0254
Available at: http://works.bepress.com/lunae/42/