Characterization and analysis of an apparent autophosphorylation of chicken gizzard myosin light chain kinase.

Journal Article

A phosphorylation occurs at two sites in chicken gizzard myosin light chain kinase that appears to be catalyzed by an autophosphorylation reaction. This reaction is inhibited by approximately 75% in the presence of Ca2+-calmodulin, but is unaffected by the cAMP-dependent protein kinase inhibitor. Whereas the catalytic subunit of cAMP-dependent protein kinase phosphorylates myosin light chain kinase at only serine residues, the non cAMP-dependent phosphorylation occurs at both serine and threonine residues. One, if not both, of these latter sites are distinct from the sites recognized by the catalytic subunit of cAMP-dependent protein kinase. Consequently, there must be at least three and possibly four sites in myosin light chain kinase capable of incorporating phosphate, either in response to catalytic subunit or by autophosphorylation.

Full Text

Duke Authors

Cited Authors

  • Foyt, HL; Means, AR

Published Date

  • 1985

Published In

Volume / Issue

  • 10 / 2

Start / End Page

  • 143 - 155

PubMed ID

  • 3839002

International Standard Serial Number (ISSN)

  • 0746-3898

Language

  • eng

Conference Location

  • United States