title: Commentary on paper: Small heat shock proteins and the cytoskeleton: an essential interplay for cell integrity? (Wettstein et al.).
abstract: The recently published paper by Wettstein et al. (2012) reviews the data of literature dealing with participation of small heat shock proteins (sHsp) in cytoskeleton regulation. Analyzing the effect of sHsp on microfilaments, the authors come to conclusion that depending on phosphorylation HspB1 can function as barbed-end-capping protein and can prevent aggregation of F-actin under stress conditions. The modern data do not confirm all these suggestions. We propose that stabilization effect of HspB1 on microfilaments is due to HspB1 interaction with partially unfolded actin or with genuine actin-binding proteins. In addition, HspB1 can exert its stabilizing effect on F-actin by modulating other elements of the cytoskeleton (intermediate filaments and microtubules) or by controlling homeostasis (for instance, redox state). Without being genuine actin-binding proteins, HspB1 and HspB6 predominantly protect microfilaments via an indirect mechanism that is yet to be characterized.
authors.affiliation: Department of Biochemistry, School of Biology, Moscow State University, Moscow 119991, Russian Federation.
authors.forename: Alim S
authors.initials: AS
authors.lastname: Seit-Nebi
authors.forename: Petr
authors.initials: P
authors.lastname: Datskevich
authors.forename: Nikolai B
authors.initials: NB
authors.lastname: Gusev
mesh_terms: D000818:Animals; D005355:Fibrosis / Q000378:metabolism*; D050888:Heat-Shock Proteins, Small / Q000378:metabolism*; D006801:Humans; D007382:Intermediate Filaments / Q000378:metabolism*; D009369:Neoplasms / Q000378:metabolism*
chemical_list: D050888:Heat-Shock Proteins, Small