Phosphorylation of the Na,K-ATPase by Ca,phospholipid-dependent and cAMP-dependent protein kinases. Mapping of the region phosphorylated by Ca,phospholipid-dependent protein kinaseстатья
Информация о цитировании статьи получена из
Scopus,
Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
Аннотация:Ca,phospholipid-dependent (PKC) and cAMP-dependent (PKA) protein kinases phosphorylate the alpha-subunit of the Na,K-ATPase from duck salt gland with the incorporation of 0.3 and 0.5 mol 32P/mol of alpha-subunit, respectively. PKA (in contrast to PKC) phosphorylates the alpha-subunit only in the presence of detergents. Limited tryptic digestion of the Na,K-ATPase phosphorylated by PKC demonstrates that 32P is incorporated into the N-terminal 41-kDa fragment of the alpha-subunit. Selective chymotrypsin cleavage of phosphorylated enzyme yields a 35-kDa radioactive fragment derived from the central region of the alpha-subunit molecule. These findings suggest that PKC phosphorylates the alpha-subunit of the Na,K-ATPase within the region restricted by C3 and T1 cleavage sites.