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J. Biol. Chem., Vol. 276, Issue 32, 30342-30349, August 10, 2001
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From the Activation of myosin II by myosin light chain
kinase (MLCK) produces the force for many cellular processes
including muscle contraction, mitosis, migration, and other cellular
shape changes. The results of this study show that inhibition or
potentiation of myosin II activation via over-expression of a dominant
negative or wild type MLCK can delay or accelerate tumor necrosis
factor-
Myosin II Light Chain Phosphorylation Regulates
Membrane Localization and Apoptotic Signaling of Tumor Necrosis
Factor Receptor-1*
§,
Department of Cellular and
Integrative Physiology and the ¶ Department of Medicine, Indiana
University School of Medicine, Indianapolis, Indiana 46202
(TNF)-induced apoptotic cell death in cells. Changes in the
activation of caspase-8 that parallel changes in regulatory light
chain phosphorylation levels reveal that myosin II motor
activities regulate TNF receptor-1 (TNFR-1) signaling at an early step
in the TNF death signaling pathway. Treatment of cells with either
ionomycin or endotoxin (lipopolysaccharide) leads to activation of
myosin II and increased translocation of TNFR-1 to the plasma membrane
independent of TNF signaling. The results of these studies establish a
new role for myosin II motor activity in regulating TNFR-1-mediated
apoptosis through the translocation of TNFR-1 to or within the plasma membrane.
*
This work was supported by National Institutes of Health
Grant HL54118 (to P. J. G.).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.
To whom correspondence should be addressed: Dept. of Cellular
and Integrative Physiology, 635 Barnhill Dr., Indianapolis, IN
46202-5120. Tel.: 317-278-2146; Fax: 317-274-3318; E-mail: pgallag@iupui.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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