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J. Biol. Chem., Vol. 276, Issue 2, 1459-1465, January 12, 2001
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From the Department of Molecular Pharmacology, Stanford University,
Stanford, California 94305-5174
The c-Jun N-terminal kinases (JNKs) are members
of the mitogen-activated protein kinase family that play critical roles
in stress responses and apoptosis. We have discovered that JNK is present in Xenopus oocytes, an experimental system that
offers a variety of powerful experimental approaches to questions of protein function and regulation. Like ERK2/p42 MAPK, JNK is activated just prior to germinal vesicle breakdown during Xenopus
oocyte maturation and remains active throughout meiosis I and II.
However, unlike p42 MAPK, which is inactivated about 30 min after eggs are fertilized or parthenogenetically activated, JNK stays
constitutively active until the early gastrula stage of embryogenesis.
These findings suggest that the JNK pathway may play a role in oocyte maturation and embryogenesis. JNK was activated by microinjection of
Mos, by activation of an estrogen-inducible form of Raf, and by a
constitutively active MEK-1 (MEK R4F), indicating that the p42 MAPK
cascade can trigger JNK activation. However, the MEK inhibitor U0126
blocked progesterone-induced p42 MAPK activation but not
progesterone-induced JNK activation. Thus, progesterone can stimulate
JNK activation both through the MEK/p42 MAPK pathway and through
MEK/p42 MAPK-independent pathways. Many of the key substrates of JNKs
identified to date are transcriptional regulators. However, since
transcription is not required for germinal vesicle breakdown in
progesterone-treated oocytes or for the early embryonic cell cycles,
our findings suggest that in these contexts the JNK pathway exerts
nongenomic effects.
c-Jun N-terminal Kinase Activation in Xenopus
laevis Eggs and Embryos
A POSSIBLE NON-GENOMIC ROLE FOR THE JNK SIGNALING PATHWAY*
*
This work was supported by National Institutes of Health
Grant GM46383 and a Deutsche Forschungsgemeinschaft Postdoctoral Fellowship.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 Molecular
Pharmacology, Stanford University, 269 West Campus Dr., Stanford, CA
94305-5174. Tel.: 650-725-0765; Fax: 650-723-2253; E-mail: ferrell@cmgm.stanford.edu.
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