Regulated CPEB phosphorylation during meiotic progression suggests a mechanism for temporal control of maternal mRNA translation
| dc.contributor.author | Tay, Joyce | |
| dc.contributor.author | Hodgman, Rebecca | |
| dc.contributor.author | Sarkissian, Madathia | |
| dc.contributor.author | Richter, Joel D. | |
| dc.date | 2022-08-11T08:08:49.000 | |
| dc.date.accessioned | 2022-08-23T16:09:22Z | |
| dc.date.available | 2022-08-23T16:09:22Z | |
| dc.date.issued | 2003-06-20 | |
| dc.date.submitted | 2009-01-13 | |
| dc.identifier.citation | Genes Dev. 2003 Jun 15;17(12):1457-62. <a href="http://dx.doi.org/10.1101/gad.1071403">Link to article on publisher's site</a> | |
| dc.identifier.issn | 0890-9369 (Print) | |
| dc.identifier.doi | 10.1101/gad.1071403 | |
| dc.identifier.pmid | 12815066 | |
| dc.identifier.uri | http://hdl.handle.net/20.500.14038/32678 | |
| dc.description.abstract | CPEB is an mRNA-binding protein that stimulates polyadenylation-induced translation of maternal mRNA once it is phosphorylated on Ser 174 or Thr 171 (species-dependent). Disruption of the CPEB gene in mice causes an arrest of oogenesis at embryonic day 16.5 (E16.5), when most oocytes are in pachytene of prophase I. Here, we show that CPEB undergoes Thr 171 phosphorylation at E16.5, but dephosphorylation at the E18.5, when most oocytes are entering diplotene. Although phosphorylation is mediated by the kinase aurora, the dephosphorylation is due to the phosphatase PP1. The temporal control of CPEB phosphorylation suggests a mechanism in which CPE-containing mRNA translation is stimulated at pachytene and metaphase I. | |
| dc.language.iso | en_US | |
| dc.relation | <a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=12815066&dopt=Abstract">Link to Article in PubMed</a> | |
| dc.relation.url | http://dx.doi.org/10.1101/gad.1071403 | |
| dc.subject | Animals; Antibody Specificity; Female; Genomic Imprinting; Meiosis; Mice; Mice, Knockout; Mutation; Oocytes; Ovary; Phosphoprotein Phosphatases; Phosphorylation; Polyadenylation; Prophase; Protein Biosynthesis; Protein-Serine-Threonine Kinases; RNA, Messenger; RNA-Binding Proteins; Threonine; Xenopus | |
| dc.subject | Life Sciences | |
| dc.subject | Medicine and Health Sciences | |
| dc.title | Regulated CPEB phosphorylation during meiotic progression suggests a mechanism for temporal control of maternal mRNA translation | |
| dc.type | Journal Article | |
| dc.source.journaltitle | Genes and development | |
| dc.source.volume | 17 | |
| dc.source.issue | 12 | |
| dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/gsbs_sp/1237 | |
| dc.identifier.contextkey | 693147 | |
| html.description.abstract | <p>CPEB is an mRNA-binding protein that stimulates polyadenylation-induced translation of maternal mRNA once it is phosphorylated on Ser 174 or Thr 171 (species-dependent). Disruption of the CPEB gene in mice causes an arrest of oogenesis at embryonic day 16.5 (E16.5), when most oocytes are in pachytene of prophase I. Here, we show that CPEB undergoes Thr 171 phosphorylation at E16.5, but dephosphorylation at the E18.5, when most oocytes are entering diplotene. Although phosphorylation is mediated by the kinase aurora, the dephosphorylation is due to the phosphatase PP1. The temporal control of CPEB phosphorylation suggests a mechanism in which CPE-containing mRNA translation is stimulated at pachytene and metaphase I.</p> | |
| dc.identifier.submissionpath | gsbs_sp/1237 | |
| dc.contributor.department | Program in Molecular Medicine | |
| dc.contributor.department | Graduate School of Biomedical Sciences | |
| dc.source.pages | 1457-62 |