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J. Biol. Chem., Vol. 276, Issue 19, 16365-16373, May 11, 2001
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From the Smooth Muscle Research Group and Canadian Institutes of
Health Research Group in Regulation of Vascular Contractility,
Department of Biochemistry and Molecular Biology, University of Calgary
Faculty of Medicine, Calgary, Alberta T2N 4N1, Canada
Smooth muscle contraction follows an increase in
cytosolic Ca2+ concentration, activation of myosin
light chain kinase, and phosphorylation of the 20-kDa light chain of
myosin at Ser19. Several agonists acting via G
protein-coupled receptors elicit a contraction without a change in
[Ca2+]i via inhibition of myosin light chain
phosphatase and increased myosin phosphorylation. We showed that
microcystin (phosphatase inhibitor)-induced contraction of skinned
smooth muscle occurred in the absence of Ca2+ and
correlated with phosphorylation of myosin light chain at Ser19 and Thr18 by a kinase distinct from
myosin light chain kinase. In this study, we identify this kinase as
integrin-linked kinase. Chicken gizzard integrin-linked kinase cDNA
was cloned, sequenced, expressed in E. coli, and shown to
phosphorylate myosin light chain in the absence of Ca2+ at
Ser19 and Thr18. Subcellular fractionation
revealed two distinct populations of integrin-linked kinase, including
a Triton X-100-insoluble component that phosphorylates myosin in a
Ca2+-independent manner. These results suggest a novel
function for integrin-linked kinase in the regulation of smooth muscle
contraction via Ca2+-independent phosphorylation of myosin,
raise the possibility that integrin-linked kinase may also play a role
in regulation of nonmuscle motility, and confirm that integrin-linked
kinase is indeed a functional protein-serine/threonine kinase.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF296130.
Ca2+-independent Smooth Muscle Contraction
A NOVEL FUNCTION FOR INTEGRIN-LINKED KINASE*
*
This work was supported by a grant from the Canadian
Institutes of Health Research.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.
An Alberta Heritage Foundation for Medical Research Medical
Scientist and recipient of a Canada Research Chair in Biochemistry. To
whom correspondence should be addressed: Dept. of Biochemistry and
Molecular Biology, University of Calgary Faculty of Medicine, 3330 Hospital Dr. NW, Calgary, Alberta T2N 4N1, Canada. Tel.: 403-220-3021;
Fax: 403-270-2211; E-mail: walsh@ucalgary.ca.
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