Localization of an actin binding domain in smooth muscle myosin light chain kinase

Patricia J. Gallagher, James T. Stull

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Phosphorylation of the regulatory light chain of myosin II by myosin light chain kinase is important for regulating many contractile processes. Smooth muscle myosin light chain kinase has been shown to be associated with both actin and myosin filaments in vitro and in vivo. In this report we define an actin binding region by using molecular deletions to generate recombinant mutant proteins that were analyzed by co-sedimentation with F-actin. An actin binding region restricted to residues 2-42 in the animo terminus of the rabbit smooth muscle myosin light chain kinase was identified.

Original languageEnglish (US)
Pages (from-to)51-57
Number of pages7
JournalMolecular and Cellular Biochemistry
Volume173
Issue number1-2
DOIs
StatePublished - 1997

Fingerprint

Smooth Muscle Myosins
Myosin-Light-Chain Kinase
Actins
Myosin Type II
Mutant Proteins
Myosins
Actin Cytoskeleton
Recombinant Proteins
Recombinant proteins
Phosphorylation
Sedimentation
Rabbits
Light

Keywords

  • Actin binding
  • Contraction
  • Myosin light chain kinase
  • Protein kinase

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Localization of an actin binding domain in smooth muscle myosin light chain kinase. / Gallagher, Patricia J.; Stull, James T.

In: Molecular and Cellular Biochemistry, Vol. 173, No. 1-2, 1997, p. 51-57.

Research output: Contribution to journalArticle

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