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Vol. 10, Issue 9, 2971-2986, September 1999
European Molecular Biology Laboratory, 69117 Heidelberg, Germany
The efficient activation of p90rsk by MAP kinase
requires their interaction through a docking site located at the
C-terminal end of p90rsk. The MAP kinase
p42mpk1 can associate with p90rsk in
G2-arrested but not in mature Xenopus
oocytes. In contrast, an N-terminally truncated p90rsk
mutant named D2 constitutively interacts with p42mpk1. In
this report we show that expression of D2 inhibits
Xenopus oocyte maturation. The inhibition requires the
p42mpk1 docking site. D2 expression uncouples the
activation of p42mpk1 and p34cdc2/cyclin B in
response to progesterone but does not prevent signaling through
p90rsk. Instead, D2 interferes with a
p42mpk1-triggered pathway, which regulates the
phosphorylation and activation of Plx1, a potential activator of the
Cdc25 phosphatase. This new pathway that links the activation of
p42mpk1 and Plx1 during oocyte maturation is independent of
p34cdc2/cyclin B activity but requires protein
synthesis. Using D2, we also provide evidence that the sustained
activation of p42mpk1 can trigger nuclear migration in
oocytes. Our results indicate that D2 is a useful tool to study MAP
kinase function(s) during oocyte maturation. Truncated substrates such
as D2, which constitutively interact with MAP kinases, may also be
helpful to study signal transduction by MAP kinases in other cellular processes.
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