Small heat shock proteins and the cytoskeleton: an essential interplay for cell integrity?
The cytoskeleton is a highly complex network of three major intracellular filaments, microfilaments (MFs), microtubules (MTs) and intermediate filaments (IFs). This network plays a key role in the control of cell shape, division, functions and interactions in animal organs and tissues. Dysregulation of the network can contribute to numerous human diseases. Although small HSPs (sHSPs) and in particular HSP27 (HSPB1) or αB-crystallin (HSPB5) display a wide range of cellular properties, they are mostly known for their ability to protect cells under stress conditions. Mutations in some sHSPs have been found to affect their ability to interact with cytoskeleton proteins, leading to IF aggregation phenotypes that mimick diseases related to disorders in IF proteins (i.e. desmin, vimentin and neuro-filaments). The aim of this review is to discuss new findings that point towards the possible involvement of IFs in the cytoprotective functions of sHSPs, both in physiological and pathological settings, including the likelihood that sHSPs such as HSPB1 may play a role during epithelial-to-mesenchymal transition (EMT) during fibrosis or cancer progression. This article is part of a Directed Issue entitled: Small HSPs in physiology and pathology.
INSERM U866, University of Burgundy, Dijon 21079, France.
G
G
Wettstein
P S
PS
Bellaye
O
O
Micheau
Ph
P
Bonniaud
D000818:Animals; D058750:Epithelial-Mesenchymal Transition; D005355:Fibrosis / Q000378:metabolism* / Q000473:pathology; D030342:Genetic Diseases, Inborn / Q000235:genetics / Q000378:metabolism / Q000473:pathology; D050888:Heat-Shock Proteins, Small / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007382:Intermediate Filaments / Q000378:metabolism*; D009154:Mutation; D009369:Neoplasms / Q000378:metabolism* / Q000473:pathology; D013312:Stress, Physiological
D050888:Heat-Shock Proteins, Small