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    J Biol Chem. 1994 Mar 25;269(12):9368-73.

    Identification of the phosphorylation site for cAMP-dependent protein kinase on Na+,K(+)-ATPase and effects of site-directed mutagenesis.

    Fisone G, Cheng SX, Nairn AC, Czernik AJ, Hemmings HC Jr, Höög JO, Bertorello AM, Kaiser R, Bergman T, Jörnvall H, et al.

    Source

    Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, New York 10021.

    Abstract

    Phosphorylation of purified Na+,K(+)-ATPase by cAMP-dependent protein kinase (protein kinase A) decreases the activity of this enzyme. We have now shown, using several experimental approaches, that a highly conserved seryl residue on the catalytic (alpha) subunit of Na+,K(+)-ATPase, corresponding to Ser943 of the rat alpha 1 isoform, is the phosphorylation site for protein kinase A. cDNAs corresponding to wild-type Na+,K(+)-ATPase and Na+,K(+)-ATPase in which Ser943 was mutated to Ala were transfected into COS cells. Treatment of the transfected cells with forskolin plus 3-isobutyl-1-methylxanthine resulted in a decrease in the activity of the wild-type enzyme but not in that of the mutated enzyme. The results suggest that, in intact cells, the activity of the Na+,K(+)-ATPase is regulated in part by signal transduction pathways that use protein kinase A-dependent phosphorylation of the Na+,K(+)-ATPase alpha subunit.

    PMID:
    7510709
    [PubMed - indexed for MEDLINE]

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