Interaction of Na,K-ATPase Catalytic Subunit with Cellular Proteins and Other Endogenous Regulators

O. D. Lopina

Department of Biochemistry, School of Biology, Lomonosov Moscow State University, Moscow, 119899 Russia; fax: (095) 939-3955; E-mail: od_lopina@mail.ru

Received April 29, 2001; Revision received June 21, 2001

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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.

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KEY WORDS: Na,K-ATPase, signal transduction, protein kinases, beta- and gamma-subunits, conserved domains, melittin, digitalis-like factors

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