Differential phosphorylation of MAP-2 stimulated by calcium-calmodulin and cyclic AMP.
Comparison of cyclic AMP- and calcium-dependent phosphorylation in rat brain cytosol reveals MAP-2 to be a common endogenous substrate. Examination of limited protease digestion patterns indicates that the two kinases phosphorylate MAP-2 at distinct sites and suggests that such phosphorylation may have differential effects on MAP-2 function.
D000818:Animals; D001921:Brain / Q000378:metabolism*; D002118:Calcium / Q000494:pharmacology*; D002147:Calmodulin / Q000494:pharmacology*; D000242:Cyclic AMP / Q000494:pharmacology*; D003600:Cytosol / Q000378:metabolism; D007700:Kinetics; D008297:Male; D008869:Microtubule-Associated Proteins; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D002147:Calmodulin; D008869:Microtubule-Associated Proteins; D009419:Nerve Tissue Proteins; D011506:Proteins; D000242:Cyclic AMP; D011494:Protein Kinases; D002118:Calcium