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

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    Date
    2007-10-16
    Authors
    Freel, CD
    Guo, Y
    Hansen, DV
    Jackson, PK
    Kornbluth, S
    Tang, W
    Tung, Jeffrey J
    Wang, MZ
    Wu, JQ
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    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.
    Type
    Journal article
    Subject
    Amino Acid Sequence
    Animals
    F-Box Proteins
    Humans
    Meiosis
    Molecular Sequence Data
    Ovum
    Phosphorylase Phosphatase
    Phosphorylation
    Proto-Oncogene Proteins c-mos
    Ribosomal Protein S6 Kinases
    Signal Transduction
    Xenopus
    Xenopus Proteins
    Permalink
    http://hdl.handle.net/10161/8391
    Published Version (Please cite this version)
    10.1073/pnas.0707537104
    Publication Info
    Freel, CD; Guo, Y; Hansen, DV; Jackson, PK; Kornbluth, S; Tang, W; ... Wu, JQ (2007). Control of Emi2 activity and stability through Mos-mediated recruitment of PP2A. Proc Natl Acad Sci U S A, 104(42). pp. 16564-16569. 10.1073/pnas.0707537104. Retrieved from http://hdl.handle.net/10161/8391.
    This is constructed from limited available data and may be imprecise. To cite this article, please review & use the official citation provided by the journal.
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    Scholars@Duke

    Kornbluth

    Sally A. Kornbluth

    Jo Rae Wright University Professor
    Our lab studies the regulation of complex cellular processes, including cell cycle progression and programmed cell death (apoptosis). These tightly orchestrated processes are critical for appropriate cell proliferation and cell death, and when they go awry can result in cancer and degenerative disorders. Within these larger fields, we have focused on understanding the cellular mechanisms that prevent the onset of mitosis prior to the completion of DNA replication, the process
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