Interaction of Na,K-ATPase catalytic subunit with cellular proteins and other endogenous regulators.
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.
Lopina
O D
OD
Department of Biochemistry, School of Biology, Lomonosov Moscow State University, Moscow, 119899, Russia. od_lopina@mail.ru
D000818:Animals; D017487:Ankyrins / Q000378:metabolism; D020134:Catalytic Domain; D004070:Digitalis / Q000378:metabolism; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism; D008555:Melitten / Q000378:metabolism; D008958:Models, Molecular; D010766:Phosphorylation; D011485:Protein Binding; D011494:Protein Kinases / Q000378:metabolism; D020836:Protein Structure, Quaternary; D021122:Protein Subunits; D015398:Signal Transduction; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000378:metabolism*
D017487:Ankyrins; D007527:Isoenzymes; D021122:Protein Subunits; D008555:Melitten; D011494:Protein Kinases; D000254:Sodium-Potassium-Exchanging ATPase