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J. Biol. Chem., Vol. 277, Issue 38, 35597-35604, September 20, 2002
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From the Department of Physiology, University of Texas Southwestern
Medical Center, Dallas, Texas 75390-9040
Short and long myosin light chain kinases (MLCKs)
are Ca2+/calmodulin-dependent enzymes
that phosphorylate the regulatory light chain of myosin II in thick
filaments but bind with high affinity to actin thin filaments. Three
repeats of a motif made up of the sequence DFRXXL at the N
terminus of short MLCK are necessary for actin binding (Smith, L., Su,
X., Lin, P., Zhi, G., and Stull, J. T. (1999) J. Biol.
Chem. 274, 29433-29438). The long MLCK has two additional
DFRXXL motifs and six Ig-like modules in an N-terminal extension, which may confer unique binding properties for cellular localization. Two peptides containing either five or three
DFRXXL motifs bound to F-actin and smooth muscle
myofilaments with maximal binding stoichiometries consistent with each
motif binding to an actin monomer in the filaments. Both peptides
cross-linked F-actin and bound to stress fibers in cells. Long MLCK
with an internal deletion of the five DFRXXL motifs and the
unique NH2-terminal fragment containing six Ig-like motifs
showed weak binding. Cell fractionation and extractions with
MgCl2 indicate that the long MLCK has a greater affinity
for actin-containing filaments than short MLCK in vitro and
in vivo. Whereas DFRXXL motifs are necessary and sufficient for short MLCK binding to actin-containing filaments, the DFRXXL motifs and the N-terminal extension of long MLCK
confer high affinity binding to stress fibers in cells.
Properties of Long Myosin Light Chain Kinase Binding to
F-Actin in Vitro and in Vivo*
§,,,
*
This work was supported by National Institutes of Health
Grant HL26093, Training Grant HD07190, and the Fouad A. and Val Imm Bashour Distinguished Chair in Physiology.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
These authors contributed equally to this work.
§
Present address: Dept. of Biological Sciences, Alabama State
University, P.O. Box 271, Montgomery, AL 36101-0271.
¶
To whom correspondence should be addressed. Tel.:
214-648-6849; Fax: 214-648-2974; E-mail:
James.Stull@UTSouthwestern.edu.
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