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Interaction of Na,K-ATPase catalytic subunit with cellular proteins and other endogenous regulatorsстатья
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: 7 октября 2013 г.
- Автор: Lopina O.D.
- Журнал: Biochemistry (Moscow)
- Том: 66
- Номер: 10
- Год издания: 2001
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 1122
- Последняя страница: 1131
- Аннотация: Some mechanisms of regulation of Na,K-ATPase activity in various tissues including the phosphorylation of the catalytic subunit of the enzyme by different protein kinases (PKA, PKC, and tyrosine kinase) and the interaction of the alpha-subunit with different proteins (Na,K-ATPase beta- and gamma-subunits, ankyrin, phosphoinositide-3 kinase, and AP-2 protein) and endogenous digitalis-like factors are considered. Special attention is given to the search for possible protein-partners including melittin-like protein and to the mechanism of enzyme regulation connected with the change of Na,K-ATPase quaternary structure. A recently discovered role of Na,K-ATPase as a receptor providing signal transduction inside the cell not only by changing the concentration of biologically significant cations but also using direct interaction of the enzyme with the protein-partners is discussed.
- Добавил в систему: Лопина Ольга Дмитриевна