Phosphorylation of myosin light chain by protease activated kinase I

Polygena T. Tuazon, James T. Stull, Jolinda A. Traugh

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Protease activated kinase I from rabbit reticulocytes has been shown to phosphorylate the P-light chain of myosin light chains isolated from rabbit skeletal muscle. The enzyme is not activated by Ca2+ and calmodulin or phospholipids. Protease activated kinase I is not inhibited by trifluoperazine at concentrations up to 200 μM or by the antibody to the Ca2+, calmodulin-dependent myosin light chain kinase from rabbit skeletal muscle. Two-dimensional peptide mapping of chymotryptic digests of myosin P-light chain show the site phosphorylated by the protease activated kinase is different from that phosphorylated by the Ca2+, calmodulin-dependent myosin light chain kinase.

Original languageEnglish (US)
Pages (from-to)910-917
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume108
Issue number2
DOIs
StatePublished - Sep 30 1982

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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