REVIEW: Structure and Properties of Small Heat Shock Proteins (sHsp) and Their Interaction with Cytoskeleton Proteins

N. B. Gusev^1*, N. V. Bogatcheva¹, and S. B. Marston²

¹Department of Biochemistry, School of Biology and Department of Biochemistry, School of Fundamental Medicine, Lomonosov Moscow State University, Moscow, 119992 Russia; fax: (095) 939-2747; E-mail: NBGusev@mail.ru

²Department of Cardiac Medicine, National Heart and Lung Institute, Imperial College of Science, Technology and Medicine, Dovehouse Street London SW3 6LY, UK; E-mail: S.Marston@ic.ac.uk

^* To whom correspondence should be addressed.

Received August 22, 2001

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The modern classification of small heat shock proteins (sHsp) is presented and peculiarities of their primary structure and the mechanism of formation of oligomeric complexes are described. Data on phosphorylation of sHsp by different protein kinases are presented and the effect of phosphorylation on oligomeric state and chaperone activity of sHsp is discussed. Intracellular location of sHsp under normal and stress conditions is described and it is emphasized that under certain condition sHsp interact with different elements of cytoskeleton. The literature concerning the effect of sHsp on polymerization of actin in vitro isanalyzed. An attempt is made to compare effects of sHsp on polymerization of actin in vitro with the results obtained on living cells under normal conditions and after heat shock or hormone action. The literature concerning possible effects of sHsp on cell motility is also analyzed.

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KEY WORDS: heat shock proteins, crystallins, phosphorylation, cytoskeleton, actin

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