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1. 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 kinase.

Author

Chibalin AV, Lopina OD, Petukhov SP, and Vasilets LA

Subjects
Animals, Ducks, In Vitro Techniques, Peptide Fragments isolation & purification, Phosphorylation, Protein Conformation, Protein Kinase C metabolism, Salt Gland metabolism, Sodium-Potassium-Exchanging ATPase chemistry, Protein Kinases metabolism, Sodium-Potassium-Exchanging ATPase metabolism
Abstract

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.

Published
1993
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