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CA2 — MAP2

Text-mined interactions from Literome

Jefferson et al., J Biol Chem 1991 (Pituitary Neoplasms) : We conclude that activation of cAMP- and Ca2 ( + ) -based signaling pathways leads to phosphorylation of MAP-2 in GH3 cells and that cAMP kinase and CaM kinase mediate phosphorylation by these pathways, respectively
Levine et al., Eur J Biochem 1987 : The fragment phosphorylates microtubule associated protein ( MAP-2 ) but is not activated by Ca+2/calmodulin nor is it inhibited by trifluoperazine
Sobue et al., Biochim Biophys Acta 1985 : Ca2+ and calmodulin regulate microtubule associated protein-actin filament interaction in a flip-flop switch ... MAP2- or tau factor induced bundle formation of actin filaments was inhibited only in the presence of Ca2+ and calmodulin, but not in the presence or absence of Ca2+ ... In conclusion, the interaction of MAP2- and tau factor-actin filaments is regulated by Ca2+ and calmodulin in a flip-flop switch
Kotani et al., J Biol Chem 1985 : A well-known Ca2+ dependent regulatory protein, calmodulin, inhibited both MAP2-actin and Tau-actin interaction in a Ca2+ dependent manner
Johnson et al., J Neurosci Res 1993 : The effects of cAMP dependent protein kinase ( cAMP-PK ) and Ca2+/calmodulin dependent protein kinase II ( CaMKII ) phosphorylation on the calpain mediated degradation of microtubule associated protein 2 (MAP-2) were studied