Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins.
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 is analyzed. 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.
Gusev
N B
NB
Department of Biochemistry, School of Biology, Lomonosov Moscow State University, Moscow, 119992, Russia. NBGusev@mail.ru
Bogatcheva
N V
NV
Marston
S B
SB
D000595:Amino Acid Sequence; D000818:Animals; D002465:Cell Movement; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D009132:Muscles / Q000502:physiology; D010766:Phosphorylation; D020836:Protein Structure, Quaternary
D003598:Cytoskeletal Proteins; D006360:Heat-Shock Proteins