Substrate specificity of Ca2+/CaM-dependent multifunctional protein kinases: comparison of isoenzymes from brain, liver and skeletal muscle.

Journal Article (Journal Article)

Ca2+/CaM-dependent multifunctional protein kinase isoenzymes from brain, skeletal muscle and liver were compared by their phosphorylation of a number of protein substrates. Under the conditions of assay, the three isoenzymes demonstrated rapid phosphorylation of synapsin I and glycogen synthase. In contrast, rates of phosphorylation of pyruvate kinase and phenylalanine hydroxylase were almost two orders of magnitude slower. Differences in phosphorylation specifically of the latter two substrates was also observed among the three protein kinases. Phosphorylation by Ca2+/CaM-dependent protein kinases was contrasted with cAMP-dependent protein kinase, which phosphorylates these proteins in vitro and in vivo. The potential role of Ca2+/CaM-dependent multifunctional protein kinases in the Ca2+-dependent phosphorylation of these substrates is discussed.

Full Text

Duke Authors

Cited Authors

  • Shenolikar, S; Langston, J; Schworer, CM; Kelly, PT

Published Date

  • March 30, 1988

Published In

Volume / Issue

  • 151 / 3

Start / End Page

  • 1332 - 1338

PubMed ID

  • 3355559

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1016/s0006-291x(88)80508-4


  • eng

Conference Location

  • United States