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dc.contributor.authorGroisman, Irina
dc.contributor.authorJung, Mi-Young
dc.contributor.authorSarkissian, Madathia
dc.contributor.authorCao, Quiping
dc.contributor.authorRichter, Joel D.
dc.date2022-08-11T08:08:58.000
dc.date.accessioned2022-08-23T16:14:00Z
dc.date.available2022-08-23T16:14:00Z
dc.date.issued2002-06-28
dc.date.submitted2008-09-17
dc.identifier.citation<p>Cell. 2002 May 17;109(4):473-83.</p>
dc.identifier.issn0092-8674 (Print)
dc.identifier.doi10.1016/S0092-8674(02)00733-X
dc.identifier.pmid12086604
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33758
dc.description.abstractThe synthesis and destruction of cyclin B drives mitosis in eukaryotic cells. Cell cycle progression is also regulated at the level of cyclin B translation. In cycling extracts from Xenopus embryos, progression into M phase requires the polyadenylation-induced translation of cyclin B1 mRNA. Polyadenylation is mediated by the phosphorylation of CPEB by Aurora, a kinase whose activity oscillates with the cell cycle. Exit from M phase seems to require deadenylation and subsequent translational silencing of cyclin B1 mRNA by Maskin, a CPEB and eIF4E binding factor, whose expression is cell cycle regulated. These observations suggest that regulated cyclin B1 mRNA translation is essential for the embryonic cell cycle. Mammalian cells also display a cell cycle-dependent cytoplasmic polyadenylation, suggesting that translational control by polyadenylation might be a general feature of mitosis in animal cells.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12086604&dopt=Abstract">Link to article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1016/S0092-8674(02)00733-X
dc.subjectAnimals; Cell Cycle; Cell Cycle Proteins; Cyclin B; Cytoplasm; Embryo, Nonmammalian; Female; Gene Expression Regulation, Developmental; Mammals; Mitosis; Oocytes; Polyadenylation; Protein Biosynthesis; Protein-Serine-Threonine Kinases; RNA, Messenger; RNA-Binding Proteins; Transcription Factors; Tumor Cells, Cultured; *Xenopus Proteins; Xenopus laevis; *mRNA Cleavage and Polyadenylation Factors
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleTranslational control of the embryonic cell cycle
dc.typeJournal Article
dc.source.journaltitleCell
dc.source.volume109
dc.source.issue4
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/419
dc.identifier.contextkey632029
html.description.abstract<p>The synthesis and destruction of cyclin B drives mitosis in eukaryotic cells. Cell cycle progression is also regulated at the level of cyclin B translation. In cycling extracts from Xenopus embryos, progression into M phase requires the polyadenylation-induced translation of cyclin B1 mRNA. Polyadenylation is mediated by the phosphorylation of CPEB by Aurora, a kinase whose activity oscillates with the cell cycle. Exit from M phase seems to require deadenylation and subsequent translational silencing of cyclin B1 mRNA by Maskin, a CPEB and eIF4E binding factor, whose expression is cell cycle regulated. These observations suggest that regulated cyclin B1 mRNA translation is essential for the embryonic cell cycle. Mammalian cells also display a cell cycle-dependent cytoplasmic polyadenylation, suggesting that translational control by polyadenylation might be a general feature of mitosis in animal cells.</p>
dc.identifier.submissionpathgsbs_sp/419
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages473-83


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