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J. Biol. Chem., Vol. 276, Issue 43, 39667-39678, October 26, 2001
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From the In this study, two alternatively spliced
forms of the mouse death-associated protein kinase (DAPK) have
been identified and their roles in apoptosis examined. The mouse
DAPK-
Identification of a New Form of Death-associated Protein Kinase
That Promotes Cell Survival*
§¶,§,,
,
Department of Cellular and Integrated
Physiology, Indiana University School of Medicine, Indianapolis,
Indiana 46202 and the ** Department of Pathology, St. Louis
University School of Medicine, St. Louis, Missouri 63104
sequence is 95% identical to the previously described human
DAPK, and it has a kinase domain and calmodulin-binding region closely
related to the 130-150 kDa myosin light chain kinases. A 12-residue
extension of the carboxyl terminus of DAPK-
distinguishes it from
the human and mouse DAPK-. DAPK phosphorylates at least one
substrate in vitro and in vivo, the myosin II
regulatory light chain. This phosphorylation occurs preferentially at
Ser-19 and is stimulated by calcium and calmodulin. The mRNA
encoding DAPK is widely distributed and detected in mouse embryos and
most adult tissues, although the expression of the encoded 160-kDa DAPK
protein is more restricted. Overexpression of DAPK-, the mouse
homolog of human DAPK has a negligible effect on tumor necrosis factor
(TNF)-induced apoptosis. Overexpression of DAPK- has a strong
cytoprotective effect on TNF-treated cells. Biochemical analysis of
TNF-treated cell lines expressing mouse DAPK- suggests that the
cytoprotective effect of DAPK is mediated through both intrinsic and
extrinsic apoptotic signaling pathways and results in the inhibition of
cytochrome c release from the mitochondria as well as
inhibition of caspase-3 and caspase-9 activity. These results
suggest that the mouse DAPK- is a negative regulator of TNF-induced apoptosis.
*
This work was supported by American Heart Association Grant
GIA 95009230 (to P. J. G.) and National Institutes of Health Grants RO1HL54118 (to P. J. G.) and RO1HL45788 (to R. B. W).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.
Supported by an American Heart Association-Midwest Affiliate
post-doctoral fellowship. Current Address: National Institute of
Neurological Disorders and Stroke, NIH, Bethesda, MD 208920-4160.
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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