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

dc.contributor.author Freel, CD
dc.contributor.author Guo, Y
dc.contributor.author Hansen, DV
dc.contributor.author Jackson, PK
dc.contributor.author Kornbluth, S
dc.contributor.author Tang, W
dc.contributor.author Tung, Jeffrey J
dc.contributor.author Wang, MZ
dc.contributor.author Wu, JQ
dc.coverage.spatial United States
dc.date.accessioned 2014-03-06T18:21:49Z
dc.date.issued 2007-10-16
dc.identifier https://www.ncbi.nlm.nih.gov/pubmed/17881560
dc.identifier 0707537104
dc.identifier.issn 0027-8424
dc.identifier.uri http://hdl.handle.net/10161/8391
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.language eng
dc.relation.ispartof Proc Natl Acad Sci U S A
dc.relation.isversionof 10.1073/pnas.0707537104
dc.subject Amino Acid Sequence
dc.subject Animals
dc.subject F-Box Proteins
dc.subject Humans
dc.subject Meiosis
dc.subject Molecular Sequence Data
dc.subject Ovum
dc.subject Phosphorylase Phosphatase
dc.subject Phosphorylation
dc.subject Proto-Oncogene Proteins c-mos
dc.subject Ribosomal Protein S6 Kinases
dc.subject Signal Transduction
dc.subject Xenopus
dc.subject 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
pubs.organisational-group Institutes and Centers
pubs.organisational-group 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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