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J. Biol. Chem., Vol. 275, Issue 42, 32983-32990, October 20, 2000
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From the Department of Molecular Pharmacology, Stanford University
School of Medicine, Stanford, California 94305-5174
The 90-kDa ribosomal S6 kinases, the p90 Rsks,
are a family of intracellular serine/threonine protein kinases
distinguished by two distinct kinase domains. Rsks are activated
downstream of the ERK1 (p44) and ERK2 (p42) mitogen-activated protein
(MAP) kinases in diverse biological contexts, including progression through meiotic and mitotic M phases in Xenopus oocytes and
cycling Xenopus egg extracts, and are critical for the M
phase functions of Xenopus p42 MAPK. Here we report the
cloning and biochemical characterization of Xenopus Rsk2.
Xenopus Rsk1 and Rsk2 are specifically recognized by
commercially available RSK1 and RSK2 antisera on immunoblots, but both
Rsk1 and Rsk2 are immunoprecipitated by RSK1, RSK2, and RSK3 sera. Rsk2
is about 20-fold more abundant than the previously described
Xenopus Rsk1 protein; their concentrations are
approximately 120 and 5 nM, respectively. Rsk2, like Rsk1, forms a heteromeric complex with p42 MAP kinase. This interaction depends on sequences at the extreme C terminus of Rsk2 and can be
disrupted by a synthetic peptide derived from the C-terminal 20 amino
acids of Rsk2. Finally, we demonstrate that p42 MAP kinase can activate
recombinant Rsk2 in vitro to a specific activity comparable
to that found in Rsk2 that has been activated maximally in
vivo. These findings underscore the importance of the Rsk2 isozyme in the M phase functions of p42 MAP kinase and provide tools
for further examining Rsk2 function.
Cloning and Characterization of Xenopus Rsk2, the
Predominant p90 Rsk Isozyme in Oocytes and Eggs*
and
*
This work was supported by Grant GM46383 from the National
Institutes of Health (to J. E. F.) and National Research Service Award Predoctoral Fellowship GM16415 (to R. R. B.).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.
Present address: Eli Lilly, Dept. of Research Technologies and
Proteins, Indianapolis, IN 46285.
§
To whom correspondence should be addressed: Tel.: 650-725-0765;
Fax: 650-723-2253; E-mail: ferrell@cmgm.stanford.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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