Regulated CPEB phosphorylation during meiotic progression suggests a mechanism for temporal control of maternal mRNA translation
Document Type
Journal ArticlePublication Date
2003-06-20Keywords
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; XenopusLife Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
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.Source
Genes Dev. 2003 Jun 15;17(12):1457-62. Link to article on publisher's siteDOI
10.1101/gad.1071403Permanent Link to this Item
http://hdl.handle.net/20.500.14038/32678PubMed ID
12815066Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1101/gad.1071403