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Myosin light chain kinase binding to actin filaments
Author(s) -
Smith Lula,
Stull James T
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01931-1
Subject(s) - myosin light chain kinase , actin , myosin , myofilament , biochemistry , chemistry , actin binding protein , microbiology and biotechnology , microfilament , biophysics , biology , actin cytoskeleton , cytoskeleton , cell
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.