UMass Chan Affiliations
Program in Molecular MedicineDocument Type
Journal ArticlePublication Date
2013-01-01Keywords
AnimalsFemale
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
Metadata
Show full item recordAbstract
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.00904-12Permanent Link to this Item
http://hdl.handle.net/20.500.14038/30002PubMed ID
23090969Related Resources
Rights
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