Differential phosphorylation of MAP-2 stimulated by calcium-calmodulin and cyclic AMP.

AUTOR(ES)

Schulman, H

RESUMO

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.

Documentos Relacionados

• Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase.
• Calcium-calmodulin dependence of actin accretion and lethality in cultured HEp-2 cells infected with enteropathogenic Escherichia coli.
• The unique insert in myosin VI is a structural calcium–calmodulin binding site
• Mechanism of calcium/calmodulin inhibition of rod cyclic nucleotide-gated channels
• A Calcium-Calmodulin Antagonist Blocks Experimental Vibrio vulnificus Cytolysin-Induced Lethality in an Experimental Mouse Model