The N-terminus of MLCK binds with high affinity to actin filaments, likely due to DFRxxL motifs interacting with actin monomers.
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High-affinity MLCK N-terminus–actin binding in vitro; leaves open its role in regulating smooth muscle contractility in vivo.
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 microM and 0.8 microM. High-affinity binding of MLCK to actin-containing filaments may be due to each DFRxxL motif binding to one actin monomer in filaments.
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Smith et al. (2000) studied this question.
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