Unique sequence of a high molecular weight myosin light chain kinase is involved in interaction with actin cytoskeleton

Dmitry S. Kudryashov, Margarita V. Chibalina, Konstantin G. Birukov, Thomas J. Lukas, James R. Sellers, Linda J. Van Eldik, D. Martin Watterson, Vladimir P. Shirinsky*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

Abstract

Myosin light chain kinase (MLCK) is the key regulator of cell motility and smooth muscle contraction in higher vertebrates. We searched for the features of the high molecular weight MLCK (MLCK-210) associated with its unique N-terminal sequence not found in a more ubiquitous lower molecular weight MLCK (MLCK-108). MLCK-210 demonstrates stronger association with the Triton-insoluble cytoskeletons than MLCK-108, suggesting the role for this sequence in subcellular targeting. Indeed, the expressed unique domain of MLCK-210 binds and bundles F-actin in vitro and colocalises with the microfilaments in transfected cells reproducing endogenous MLCK-210 distribution. Thus, MLCK-210 features an extensive actin binding interface and, perhaps, acts as an actin cytoskeleton stabiliser.

Original languageEnglish (US)
Pages (from-to)67-71
Number of pages5
JournalFEBS Letters
Volume463
Issue number1-2
DOIs
StatePublished - Dec 10 1999

Keywords

  • Calmodulin
  • Cytoskeleton
  • Microfilament
  • Myosin light chain kinase

ASJC Scopus subject areas

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

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