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

dc.contributor.author

Wu, Judy Qiju

dc.contributor.author

Hansen, David V

dc.contributor.author

Guo, Yanxiang

dc.contributor.author

Wang, Michael Zhuo

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Tang, Wanli

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Freel, Christopher D

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Tung, Jeffrey J

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Jackson, Peter K

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Kornbluth, Sally

dc.coverage.spatial

United States

dc.date.accessioned

2014-03-06T18:21:49Z

dc.date.issued

2007-10-16

dc.description.abstract

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.

dc.identifier

https://www.ncbi.nlm.nih.gov/pubmed/17881560

dc.identifier

0707537104

dc.identifier.issn

0027-8424

dc.identifier.uri

https://hdl.handle.net/10161/8391

dc.language

eng

dc.publisher

Proceedings of the National Academy of Sciences

dc.relation.ispartof

Proc Natl Acad Sci U S A

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10.1073/pnas.0707537104

dc.subject

Amino Acid Sequence

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Animals

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F-Box Proteins

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Humans

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Meiosis

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Molecular Sequence Data

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Ovum

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Phosphorylase Phosphatase

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Phosphorylation

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Proto-Oncogene Proteins c-mos

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Ribosomal Protein S6 Kinases

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Signal Transduction

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Xenopus

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Xenopus Proteins

dc.title

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

dc.type

Journal article

pubs.author-url

https://www.ncbi.nlm.nih.gov/pubmed/17881560

pubs.begin-page

16564

pubs.end-page

16569

pubs.issue

42

pubs.organisational-group

Biology

pubs.organisational-group

Duke

pubs.organisational-group

Duke Cancer Institute

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Institutes and Centers

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School of Medicine

pubs.organisational-group

Staff

pubs.organisational-group

Trinity College of Arts & Sciences

pubs.publication-status

Published

pubs.volume

104

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