Suppression of Translation During in vitro Maturation of Pig Oocytes Despite Enhanced Formation of Cap-binding Protein Complex eIF4F and 4E-BP1 hyperphosphorylation.

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985904%3A_____%2F06%3A00040774" target="_blank" >RIV/67985904:_____/06:00040774 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Suppression of Translation During in vitro Maturation of Pig Oocytes Despite Enhanced Formation of Cap-binding Protein Complex eIF4F and 4E-BP1 hyperphosphorylation.

Original language description

In this study, we document that the overall rate of protein synthesis decreases during in vitro maturation (IVM) of pig oocytes despite enhanced formation of the 50 cap structure eIF4F. Within somatic/interphase cells, formation of the eIF4F protein complex correlates very well with overall rates of protein translation, and the formation of this complex is controlled primarily by the availability of the 50 cap binding protein eIF4E. We show that the eIF4E inhibitory protein, 4E-BP1, becomes phosphorylated during IVM, which results in gradual release of eIF4E from 4E-BP1, as documented by immunoprecipitation analyses. Isoelectric focusing and Western blotting experiments show conclusively that eIF4E becomes gradually phosphorylated with a maximum at metaphase II (M II). The activity of eIF4E and its ability to bind mRNA also increases during oocyte maturation as documented in experiments with m7-methyl GTPSepharose, which mimics the cap structure of mRNA. Complementary analysis of flow-

Czech name

Suprese translace v průběhu in vitro zrání prasečích oocytů bez ohledu na zvýšenou tvorbu čepičku- vázajícího komplexu eIF4F a 4E-BP1 hyperfosforylaci

Czech description

V této studii dokumentujeme, že celková rychlost syntézy proteinů se snižuje v průběhu in vitro meiotického zrání prasečích oocytů bez ohledu na zvýšenou tvorbu čepičkové struktury eIF4F. Ukázali jsme, že 4E-BP1 protein se fosforyluje v průběhu IVM což vede k uvolnění vazby eIF4E. Současně dochází k fosforylaci eIF4E. Komplementární analýza eIF4G proteinu poskytla další důkaz pro zvýšenou tvorbu proteinového komplexu eIF4F. Tyto výsledky objasňují regulaci iniciace translace během meiotického dělení.

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

ED - Physiology

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2006

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Molecular Reproduction and Development

ISSN

1040-452X

e-ISSN

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Volume of the periodical

73

Issue of the periodical within the volume

1

Country of publishing house

US - UNITED STATES

Number of pages

9

Pages from-to

68-76

UT code for WoS article

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EID of the result in the Scopus database

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