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J Biomol Struct Dyn. 2013 Oct;31(10):1150-9. doi: 10.1080/07391102.2012.726531. Epub 2012 Oct 17.

An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sites.

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1
a Department of Chemistry , Western Washington University , MS-9150, 516 High Street , Bellingham , WA , 98225-9150 , USA.

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.

PMID:
23075227
PMCID:
PMC4454289
DOI:
10.1080/07391102.2012.726531
[Indexed for MEDLINE]
Free PMC Article

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