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Small heat shock protein Hsp20 (HspB6) as a partner of 14-3-3 gammaстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Chernik Ivan S., Seit-Nebi Alim S., Marston Steven B., Gusev Nikolai B.
- Журнал: Molecular and Cellular Biochemistry
- Том: 295
- Номер: 1-2
- Год издания: 2007
- Издательство: Kluwer Academic/Plenum Publishers
- Местоположение издательства: United States
- Первая страница: 9
- Последняя страница: 17
- DOI: 10.1007/s11010-006-9266-8
- Аннотация: Interaction of human 14-3-3 gamma with the small heat shock protein Hsp20 was analyzed by means of size-exclusion chromatography and chemical crosslinking. Unphosphorylated Hsp20 and its mutant S16D mimicking phosphorylation by cAMP-dependent protein kinase did not interact with 14-3-3. Phosphorylated Hsp20 formed a tight complex with 14-3-3 in which dimer of 14-3-3 was bound to dimer of Hsp20. 14-3-3 did not affect the chaperone activity of unphosphorylated Hsp20 but increased the chaperone activity of phosphorylated Hsp20 if insulin was used as a model substrate. Estimation of the effect of 14-3-3 on the chaperone activity of Hsp20 with other model substrates was complicated by the fact that under in vitro conditions isolated 14-3-3 possessed its own high chaperone activity. Taken into account high content of Hsp20 in different muscles it is supposed that upon phosphorylation Hsp20 might effectively compete with multiple protein targets of 14-3-3 and by this means indirectly affect many intracellular processes.
- Добавил в систему: Гусев Николай Борисович