Control of Emi2 activity and stability through Mos-mediated recruitment of PP2A

Before fertilization, vertebrate eggs are arrested in meiosis II by cytostatic factor (CSF), which holds the anaphase-promoting complex (APC) in an inactive state. It was recently reported that Mos, an integral component of CSF, acts in part by promoting the Rsk-mediated phosphorylation of the APC i...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2007-10, Vol.104 (42), p.16564-16569
Main Authors: Wu, Judy Qiju, Hansen, David V, Guo, Yanxiang, Wang, Michael Zhuo, Tang, Wanli, Freel, Christopher D, Tung, Jeffrey J, Jackson, Peter K, Kornbluth, Sally
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animals
Biochemistry
Biological Sciences
Cell division
Cells
Cyclins
Eggs
F-Box Proteins - genetics
F-Box Proteins - metabolism
Humans
Interphase
Kinases
Meiosis
Mitosis
Molecular Sequence Data
Ovum - physiology
Phosphatases
Phosphorylase Phosphatase - metabolism
Phosphorylation
Physiological regulation
Proteins
Proto-Oncogene Proteins c-mos - genetics
Proto-Oncogene Proteins c-mos - metabolism
Ribosomal Protein S6 Kinases - metabolism
Room temperature
Signal Transduction
Xenopus
Xenopus Proteins - genetics
Xenopus Proteins - metabolism
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Summary:Before fertilization, vertebrate eggs are arrested in meiosis II by cytostatic factor (CSF), which holds the anaphase-promoting complex (APC) in an inactive state. It was recently reported that Mos, an integral component of CSF, acts in part by promoting the Rsk-mediated phosphorylation of the APC inhibitor Emi2/Erp1. We report here that Rsk phosphorylation of Emi2 promotes its interaction with the protein phosphatase PP2A. Emi2 residues adjacent to the Rsk phosphorylation site were important for PP2A binding. An Emi2 mutant that retained Rsk phosphorylation but lacked PP2A binding could not be modulated by Mos. PP2A bound to Emi2 acted on two distinct clusters of sites phosphorylated by Cdc2, one responsible for modulating its stability during CSF arrest and one that controls binding to the APC. These findings provide a molecular mechanism for Mos action in promoting CSF arrest and also define an unusual mechanism, whereby protein phosphorylation recruits a phosphatase for dephosphorylation of distinct sites phosphorylated by another kinase.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0707537104