How to translate text using browser tools
1 April 2002 Actin cytoskeleton and small heat shock proteins: how do they interact?
Nicole Mounier, André-Patrick Arrigo
Author Affiliations +

Actin and small heat shock proteins (sHsps) are ubiquitous and multifaceted proteins that exist in 2 reversible forms, monomers and multimers, ie, the microfilament of the cytoskeleton and oligomers of the sHsps, generally, supposed to be in a spherical and hollow form. Two situations are described in the literature, where the properties of actin are modulated by sHsps; the actin polymerization is inhibited in vitro by some sHsps acting as capping proteins, and the actin cytoskeleton is protected by some sHsps against the disruption induced by various stressful conditions. We propose that a direct actin-sHsp interaction occurs to inhibit actin polymerization and to participate in the in vivo regulation of actin filament dynamics. Protection of the actin cytoskeleton would result from an F-actin–sHsp interaction in which microfilaments would be coated by small oligomers of phosphorylated sHsps. Both proteins share common structural motives suggesting direct binding sites, but they remain to be demonstrated. Some sHsps would behave with the actin cytoskeleton as actin-binding proteins capable of either capping a microfilament when present as a nonphosphorylated monomer or stabilizing and protecting the microfilament when organized in small, phosphorylated oligomers.

Nicole Mounier and André-Patrick Arrigo "Actin cytoskeleton and small heat shock proteins: how do they interact?," Cell Stress & Chaperones 7(2), 167-176, (1 April 2002).<0167:ACASHS>2.0.CO;2
Received: 18 July 2001; Accepted: 1 November 2001; Published: 1 April 2002

This article is only available to subscribers.
It is not available for individual sale.

Get copyright permission
Back to Top