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    An unusual two-step control of CPEB destruction by Pin1

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    Authors
    Nechama, Morris
    Lin, Chien-Ling
    Richter, Joel D.
    UMass Chan Affiliations
    Program in Molecular Medicine
    Document Type
    Journal Article
    Publication Date
    2013-01-01
    Keywords
    Animals
    Female
    HEK293 Cells
    Humans
    Oocytes
    Peptidylprolyl Isomerase
    Phosphorylation
    Progesterone
    Transcription Factors
    Xenopus Proteins
    mRNA Cleavage and Polyadenylation Factors
    Amino Acids, Peptides, and Proteins
    Cell Biology
    Molecular Biology
    Molecular Genetics
    Nucleic Acids, Nucleotides, and Nucleosides
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    Abstract
    Cytoplasmic polyadenylation is a conserved mechanism that controls mRNA translation and stability. A key protein that promotes polyadenylation-induced translation of mRNAs in maturing Xenopus oocytes is the cytoplasmic polyadenylation element binding protein (CPEB). During this meiotic transition, CPEB is subjected to phosphorylation-dependent ubiquitination and partial destruction, which is necessary for successive waves of polyadenylation of distinct mRNAs. Here we identify the peptidyl-prolyl cis-trans isomerase Pin1 as an important factor mediating CPEB destruction. Pin1 interacts with CPEB in an unusual manner in which it occurs prior to CPEB phosphorylation and prior to Pin1 activation by serine 71 dephosphorylation. Upon induction of maturation, CPEB becomes phosphorylated, which occurs simultaneously with Pin1 dephosphorylation. At this time, the CPEB-Pin1 interaction requires cdk1-catalyzed CPEB phosphorylation on S/T-P motifs. Subsequent CPEB ubiquitination and destruction are mediated by a conformational change induced by Pin1 isomerization of CPEB. Similar to M phase progression in maturing Xenopus oocytes, the destruction of CPEB during the mammalian cell cycle requires Pin1 as well. These data identify Pin1 as a new and essential factor regulating CPEB degradation.
    Source

    Mol Cell Biol. 2013 Jan;33(1):48-58. doi: 10.1128/MCB.00904-12. Epub 2012 Oct 22. Link to article on publisher's site

    DOI
    10.1128/MCB.00904-12
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/30002
    PubMed ID
    23090969
    Related Resources

    Link to Article in PubMed

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    Publisher PDF posted as allowed by the publisher's author rights policy at http://journals.asm.org/site/misc/ASM_Author_Statement.xhtml.
    ae974a485f413a2113503eed53cd6c53
    10.1128/MCB.00904-12
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