Journal
FEBS LETTERS
Volume 480, Issue 2-3, Pages 298-300Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(00)01931-1
Keywords
myosin light chain kinase; myofilament; actin; calmodulin; calcium
Funding
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL029043] Funding Source: NIH RePORTER
- NHLBI NIH HHS [HL29043, HL06296] Funding Source: Medline
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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,vith respective K-D values of 0.1 mu M and 0.8 mu M. 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. Published by Elsevier Science B.V. All rights reserved.
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