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Titolo:
CPEB phosphorylation and cytoplasmic polyadenylation are catalyzed by the kinase IAK1/Eg2 in maturing mouse oocytes
Autore:
Hodgman, R; Tay, J; Mendez, R; Richter, JD;
Indirizzi:
Univ Massachusetts, Sch Med, Dept Mol Genet & Microbiol, Worcester, MA 01605 USA Univ Massachusetts Worcester MA USA 01605 robiol, Worcester, MA 01605 USA
Titolo Testata:
DEVELOPMENT
fascicolo: 14, volume: 128, anno: 2001,
pagine: 2815 - 2822
SICI:
0950-1991(200107)128:14<2815:CPACPA>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOS MESSENGER-RNA; ELEMENT-BINDING PROTEIN; C-MOS; REGULATED POLYADENYLATION; TRANSLATIONAL CONTROL; MEIOTIC MATURATION; SPECIFICITY FACTOR; XENOPUS-LAEVIS; CYCLIN; RECRUITMENT;
Keywords:
polyadenylation; oocyte maturation; CPEB; mouse; IAK1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Richter, JD Univ Massachusetts, Sch Med, Dept Mol Genet & Microbiol, Worcester, MA 01605 USA Univ Massachusetts Worcester MA USA 01605 ester, MA 01605 USA
Citazione:
R. Hodgman et al., "CPEB phosphorylation and cytoplasmic polyadenylation are catalyzed by the kinase IAK1/Eg2 in maturing mouse oocytes", DEVELOPMENT, 128(14), 2001, pp. 2815-2822

Abstract

In both vertebrates and invertebrates, the expression of several maternal mRNAs is regulated by cytoplasmic polyadenylation. In Xenopus oocytes, where most of the biochemical details of this process have been examined, polyadenylation is controlled by CPEB, a sequence-specific RNA binding protein. The activity of CPEB, which is to recruit cleavage and polyadenylation specificity factor (CPSF) and poly(A) polymerase (PAP) into an active cytoplasmic polyadenylation complex, is controlled by Eg2-catalyzed phosphorylation. Soon after CPEB phosphorylation and resulting polyadenylation take place, the interaction between maskin, a CPEB-associated factor, and eIF4E, the cap-binding protein, is destroyed, which results in the recruitment of mRNA into polysomes. Polyadenylation also occurs in maturing mouse oocytes, although the biochemical events that govern the reaction in these cells are not known. In this study, we have examined the phosphorylation of CPEB and haveassessed the necessity of this protein for polyadenylation in maturing mouse oocytes. Immunobistochemistry has revealed that all the factors that control polyadenylation and translation in Xenopus oocytes (CPEB, CPSF, PAP, maskin, and IAK1, the murine homologue of Eg2) are also present in the cytoplasm of mouse oocytes. After the induction of maturation, a kinase is activated that phosphorylates CPEB on a critical regulatory residue, an event that is essential for CPEB activity. A peptide that competitively inhibits the activity of IAK1/Eg2 blocks the progression of meiosis in injected oocytes. Finally, a CPEB protein that acts as a dominant negative mutation because it cannot be phosphorylated by IAK1/Eg2, prevents cytoplasmic polyadenylation. These data indicate that cytoplasmic polyadenylation in mouse oocytesis mediated by IAK1/Eg2-catalyzed phosphorylation of CPEB.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 21:09:22