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J. Biol. Chem., Vol. 276, Issue 49, 46099-46103, December 7, 2001
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From the Howard Hughes Medical Institute and Department of
Pharmacology, University of Colorado School of Medicine,
Denver, Colorado 80262
The protein kinase p90Rsk has
previously been implicated as a key target of the MAPK pathway during M
phase of meiosis II in Xenopus oocytes. To determine
whether Rsk is a mediator of MAPK for stimulation of the
G2/M transition early in meiosis I, we sought to generate a
form of Rsk that would be constitutively active in resting,
G2 phase oocytes. Initial studies revealed that an
N-terminal truncation of 43 amino acids conferred enhanced specific
activity on the enzyme in G2 phase, and stability was highest if the C terminus was not truncated. The full-length enzyme is
known to be activated by phosphorylation at five sites. Two of these
sites and flanking residues were replaced with either aspartic or
glutamic acid, and Tyr699 was mutated to alanine.
The resulting construct, termed fully activated (FA) Rsk, had
constitutive activity in G2 phase, with a specific activity
equivalent to that of wild type Rsk in M phase. In eight independent
experiments ~45% of oocytes expressing FA-Rsk underwent germinal
vesicle breakdown (GVBD, the G2/M transition) in the
absence of progesterone, and this effect could be observed even in the
presence of the MAPK kinase inhibitor U0126. Moreover, the specific
activity of FA-Rsk in vivo was unaffected by U0126. In
oocytes that did not undergo GVBD with FA-Rsk expression, subsequent treatment with progesterone resulted in a very rapid rate of GVBD even
in the presence of U0126 to inhibit the endogenous MAPK/Rsk pathway.
These results indicate that Rsk is the mediator of MAPK effects for the
G2/M transition in meiosis I and in a subpopulation of
oocytes Rsk is sufficient to trigger the G2/M transition.
A Constitutively Active Form of the Protein Kinase
p90Rsk1 Is Sufficient to Trigger the G2/M
Transition in Xenopus Oocytes*
,
*
This work was supported by Grant DK28353-20 from the
National Institutes of Health.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 Associate of the Howard Hughes Medical Institute. Present
address: Agouron Pharmaceuticals, La Jolla, CA 92037.
§
An Investigator of the Howard Hughes Medical Institute. To whom
correspondence should be addressed: HHMI/Dept. of Pharmacology, University of Colorado School of Medicine, 4200 E. 9th
Ave., Denver, CO 80262. Tel.: 303-315-7075; Fax: 303-315-7160; E-mail:
Jim.Maller@uchsc.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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