Myosin light chain kinase binding to actin filaments

Lula Smith, James T. Stull

Research output: Contribution to journalArticle

28 Scopus citations

Abstract

Smooth muscle myosin light chain kinase (MLCK) plays important roles in contractile-motile processes of a variety of cells. Three DFRxxL motifs at the kinase N-terminus (residues 2-63) are critical for high-affinity binding to actin-containing filaments [Smith et al. (1999) J. Biol. Chem. 274, 29433- 29438]. A GST fusion protein containing residues 1-75 of MLCK (GST75-MLCK) bound maximally to both smooth muscle myofilaments and F-actin at 0.28 and 0.31 mol GST75-MLCK/mol actin with respective K(D) values of 0.1 μM and 0.8 μM. High-affinity binding of MLCK to actin-containing filaments may be due to each DFRxxL motif binding to one actin monomer in filaments. (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)298-300
Number of pages3
JournalFEBS Letters
Volume480
Issue number2-3
DOIs
StatePublished - Sep 1 2000

Keywords

  • Actin
  • Calcium
  • Calmodulin
  • Myofilament
  • Myosin light chain kinase

ASJC Scopus subject areas

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

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