Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins

被引：150

作者：

Gusev, NB ^{[1
]}

Bogatcheva, NV

Marston, SB

机构：

[1] Moscow MV Lomonosov State Univ, Sch Biol, Dept Biochem, Moscow 199992, Russia

[2] Moscow MV Lomonosov State Univ, Sch Fundamental Med, Dept Biochem, Moscow 199992, Russia

[3] Univ London Imperial Coll Sci Technol & Med, Natl Heart & Lung Inst, Dept Cardiac Med, London SW3 6LY, England

来源：

BIOCHEMISTRY-MOSCOW | 2002年 / 67卷 / 05期

基金：

英国惠康基金; 俄罗斯基础研究基金会;

关键词：

heat shock proteins; crystallins; phosphorylation; cytoskeleton; actin;

D O I：

10.1023/A:1015549725819

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：511 / 519

页数：9

共 73 条

[1] The small heat shock-related protein, HSP20, is phosphorylated on serine 16 during cyclic nucleotide-dependent relaxation [J].

Beall, A ;

Bagwell, D ;

Woodrum, D ;

Stoming, TA ;

Kato, K ;

Suzuki, A ;

Rasmussen, H ;

Brophy, CM .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (16) :11344-11351

[2] Cyclosporine-induced renal artery smooth muscle contraction is associated with increases in the phosphorylation of specific contractile regulatory proteins [J].

Beall, A ;

Epstein, A ;

Woodrum, D ;

Brophy, CM .

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 1999, 1449 (01) :41-49

[3]

Beall AC, 1997, J BIOL CHEM, V272, P11283

[4] Stress (heat shock) proteins - Molecular chaperones in cardiovascular biology and disease [J].

Benjamin, IJ ;

McMillan, DR .

CIRCULATION RESEARCH, 1998, 83 (02) :117-132

[5] HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 (3DHSP27) [J].

Benndorf, R ;

Sun, XK ;

Gilmont, RR ;

Biedermann, KJ ;

Molloy, MP ;

Goodmurphy, CW ;

Cheng, H ;

Andrews, PC ;

Welsh, MJ .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (29) :26753-26761

[6]

BENNDORF R, 1994, J BIOL CHEM, V269, P20780

[7] Site-directed spin labeling study of subunit interactions in the α-crystallin domain of small heat-shock proteins -: Comparison of the oligomer symmetry in αA-crystallin, HSP 27, and HSP 16.3 [J].

Berengian, AR ;

Parfenova, M ;

Mchaourab, HS .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (10) :6305-6314

[8] Negative charges in the C-terminal domain stabilize the αB-crystallin complex [J].

Boelens, WC ;

Cross, Y ;

de Ruwe, M ;

de Reu, L ;

de Jong, WW .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (43) :28085-28090

[9] Subunit exchange of small heat shock proteins -: Analysis of oligomer formation of αA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations [J].

Bova, MP ;

Mchaourab, HS ;

Han, Y ;

Fung, BKK .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (02) :1035-1042

[10] Phosphorylation of the small heat shock-related protein, HSP20, in vascular smooth muscles is associated with changes in the macromolecular associations of HSP20 [J].

Brophy, CM ;

Dickinson, M ;

Woodrum, D .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (10) :6324-6329

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