Myosin light chain kinase binding to actin filaments

Lula Smith, James T. Stull

Research output: Contribution to journalArticle

28 Citations (Scopus)

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

Fingerprint

Myosin-Light-Chain Kinase
Actin Cytoskeleton
Actins
Smooth Muscle Myosins
Myofibrils
Smooth Muscle
Muscle
Phosphotransferases
Fusion reactions
Monomers
Proteins

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Myosin light chain kinase binding to actin filaments. / Smith, Lula; Stull, James T.

In: FEBS Letters, Vol. 480, No. 2-3, 01.09.2000, p. 298-300.

Research output: Contribution to journalArticle

Smith, Lula ; Stull, James T. / Myosin light chain kinase binding to actin filaments. In: FEBS Letters. 2000 ; Vol. 480, No. 2-3. pp. 298-300.
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