Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 613-623 |
| Number of pages | 11 |
| Journal | Biokhimiya |
| Volume | 67 |
| Issue number | 5 |
| State | Published - 2002 |
| Externally published | Yes |
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Keywords
- Actin
- Crystallins
- Cytoskeleton
- Heat shock proteins
- Phosphorylation
ASJC Scopus subject areas
- Chemistry(all)
Cite this
Review : Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins. / Gusev, N. B.; Bogatcheva, Natalia; Marston, S. B.
In: Biokhimiya, Vol. 67, No. 5, 2002, p. 613-623.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Review
T2 - Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins
AU - Gusev, N. B.
AU - Bogatcheva, Natalia
AU - Marston, S. B.
PY - 2002
Y1 - 2002
N2 - 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.
AB - 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.
KW - Actin
KW - Crystallins
KW - Cytoskeleton
KW - Heat shock proteins
KW - Phosphorylation
UR - http://www.scopus.com/inward/record.url?scp=0036412964&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036412964&partnerID=8YFLogxK
M3 - Article
VL - 67
SP - 613
EP - 623
JO - Biokhimiia (Moscow, Russia)
JF - Biokhimiia (Moscow, Russia)
SN - 0320-9725
IS - 5
ER -