Phosphorylation of CPEB by Eg2 mediates the recruitment of CPSF into an active cytoplasmic polyadenylation complex

The release of Xenopus oocytes from prophase I arrest is largely driven by the cytoplasmic polyadenylation-induced translation of dormant maternal mRNAs. Two cis elements, the CPE and the hexanucleotide AAUAAA, and their respective binding factors, CPEB and a cytoplasmic form of CPSF, control polyad...

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Bibliographic Details
Published in:Molecular cell 2000-11, Vol.6 (5), p.1253-1259
Main Authors: Mendez, R, Murthy, K G, Ryan, K, Manley, J L, Richter, J D
Format: Article
Language:English
Subjects:
Animals
Aurora Kinases
Base Sequence
Cell Cycle Proteins
Cell Nucleus - metabolism
CPEB protein
CPSF protein
Cytoplasmic Structures - chemistry
Cytoplasmic Structures - metabolism
Eg2 protein
Macromolecular Substances
Molecular Weight
mRNA Cleavage and Polyadenylation Factors
Oocytes - cytology
Oocytes - metabolism
Phosphorylation
Polyadenylation
Precipitin Tests
Protein Binding
Protein Kinases - metabolism
Protein Subunits
Protein Transport
Protein-Serine-Threonine Kinases
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - metabolism
Thermodynamics
Transcription Factors - chemistry
Transcription Factors - metabolism
Xenopus
Xenopus laevis - metabolism
Xenopus Proteins
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Summary:The release of Xenopus oocytes from prophase I arrest is largely driven by the cytoplasmic polyadenylation-induced translation of dormant maternal mRNAs. Two cis elements, the CPE and the hexanucleotide AAUAAA, and their respective binding factors, CPEB and a cytoplasmic form of CPSF, control polyadenylation. The most proximal stimulus for polyadenylation is Eg2-catalyzed phosphorylation of CPEB serine 174. Here, we show that this phosphorylation event stimulates an interaction between CPEB and CPSF. This interaction is direct, does not require RNA tethering, and occurs through the 160 kDa subunit of CPSF. Eg2-stimulated and CPE-dependent polyadenylation is reconstituted in vitro using purified components. These results demonstrate that the molecular function of Eg2-phosphorylated CPEB is to recruit CPSF into an active cytoplasmic polyadenylation complex.
ISSN:1097-2765
DOI:10.1016/S1097-2765(00)00121-0