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First published online March 7, 2007


Journal of Cell Science 120, 604e (2007)
© The Company of Biologists Limited
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In this issue

Oocyte maturation: new route MAP(K)


Figure 1

During steroid-induced maturation of Xenopus oocytes, activation of the cytoplasmic polyadenylation element binding protein (CPEB) by phosphorylation induces the translation of maternal mRNAs that encode cell-cycle regulators. But what controls CPEB activation? The answer, claim Laura Hake and colleagues, is a complex containing mitogen-activated protein kinase (MAPK) and the Rho-family guanine nucleotide exchange factor XGef (see p. 1093). XGef overexpression is known to accelerate meiotic progression and XGef interacts with CPEB throughout meiosis. Given previous reports that Aurora kinase A (Aur-A) activates CPEB by phosphorylation, the authors asked whether XGef controls the activity of Aur-A towards CPEB. Unexpectedly, they found that inhibition of Aur-A does not impair CPEB phosphorylation but that inhibition of MAPK does. In addition, they report that XGef forms a complex with MAPK and CPEB, and that MAPK phosphorylates several residues in CPEB although not S174, which is key to activating CPEB function. The authors propose, therefore, that MAPK drives meiotic progression by priming CPEB for phosphorylation on S174 by an as-yet-unidentified kinase.


Related articles in JCS:

MAPK interacts with XGef and is required for CPEB activation during meiosis in Xenopus oocytes
Brian T. Keady, Peiwen Kuo, Susana E. Martínez, Lei Yuan, and Laura E. Hake
JCS 2007 120: 1093-1103. [Abstract] [Full Text]  




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