NDLI: Inhibition of Xenopus oocyte meiotic maturation by catalytically inactive protein kinase A.

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Inhibition of Xenopus oocyte meiotic maturation by catalytically inactive protein kinase A.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Schmitt, Anja Nebreda, Angel R.
Description	Author Affiliation: Schmitt A ( European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.);
Abstract	Progesterone induces G2-arrested Xenopus oocytes to develop into fertilizable eggs in a process called meiotic maturation. Protein kinase A (PKA), the cAMP-dependent protein kinase, has long been known to be a potent inhibitor of meiotic maturation, but little information is available on how PKA functions. We have cloned two Xenopus PKA catalytic subunit isoforms, XPKAalpha and XPKAbeta. These proteins are 89% identical and both inhibit progesterone-induced meiotic maturation when overexpressed at low levels, suggesting that PKA activity is tightly regulated in the oocyte. Unexpectedly, catalytically inactive XPKA mutants are able to block progesterone-induced maturation as efficiently as the wild-type active XPKA. These mutants also block meiotic maturation induced by Mos, but are less efficient at inhibiting Cdc25C-induced maturation. Our results indicate that PKA can inhibit meiotic maturation by a novel mechanism, which does not require its kinase activity and is also independent of binding to the PKA regulatory subunits.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	7
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cyclic AMP-Dependent Protein Kinases Physiology Meiosis Oocytes Animals Cell Cycle Proteins Drug Effects Molecular Sequence Data Progesterone Pharmacology Protein Subunits Ribosomal Protein S6 Kinases Xenopus Cdc25 Phosphatases Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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