GTP/ggS-Induced phosphorylation of myosin light chain kinase in smooth muscle

Da Chun Tang, Yasutaka Kubota, Kristine E. Kamm, James T. Stull

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Phosphorylation of myosin light chain kinase by a Ca2+-dependent protein kinase increases the concentration of Ca2+/calmodulin required for half-maximal activation. The Ca2+ concentrations required for myosin light chain kinase phosphorylation in permeable smooth muscle are similar to those required for myosin light chain phosphorylation. Both GTPγS and carbachol increase the Ca2+ sensitivity of myosin light chain kinase phosphorylation as well as light chain phosphorylation. It is proposed that a similar G-protein mediated mechanism regulates the Ca2+-dependent phosphorylation of these two contractile proteins in smooth muscle.

Original languageEnglish (US)
Pages (from-to)272-275
Number of pages4
JournalFEBS Letters
Volume331
Issue number3
DOIs
StatePublished - Oct 4 1993

Keywords

  • GTPγS
  • Myosin light chain
  • Myosin light chain kinase
  • Protein phosphatase
  • Smooth muscle contraction

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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