Control of eIF4E cellular localization by eIF4E-binding proteins, 4E-BPs | Zendy

Liwei Rong | Zendy; Mark Livingstone | Zendy; Rami Sukarieh | Zendy; Emmanuel Petroulakis | Zendy; AnneClaude Gingras | Zendy; Katherine Crosby | Zendy; Bradley Smith | Zendy; Roberto D. Polakiewicz | Zendy; Jerry Pelletier | Zendy; Maria Ferraiuolo | Zendy; Nahum Sonenberg | Zendy

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Control of eIF4E cellular localization by eIF4E-binding proteins, 4E-BPs

Author(s) -

Liwei Rong,

Mark Livingstone,

Rami Sukarieh,

Emmanuel Petroulakis,

AnneClaude Gingras,

Katherine Crosby,

Bradley Smith,

Roberto D. Polakiewicz,

Jerry Pelletier,

Maria Ferraiuolo,

Nahum Sonenberg

Publication year - 2008

Publication title -

rna

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.037

H-Index - 171

eISSN - 1469-9001

pISSN - 1355-8382

DOI - 10.1261/rna.950608

Subject(s) - eif4e , biology , microbiology and biotechnology , nuclear export signal , poly(a) binding protein , nuclear transport , cell nucleus , nucleus , repressor , nuclear protein , initiation factor , eukaryotic translation , eif4a1 , eukaryotic translation initiation factor 4 gamma , messenger rna , translation (biology) , genetics , gene expression , gene , transcription factor

Eukaryotic initiation factor (eIF) 4E, the mRNA 5′-cap-binding protein, mediates the association of eIF4F with the mRNA 5′-cap structure to stimulate cap-dependent translation initiation in the cytoplasm. The assembly of eIF4E into the eIF4F complex is negatively regulated through a family of repressor proteins, called the eIF4E-binding proteins (4E-BPs). eIF4E is also present in the nucleus, where it is thought to stimulate nuclear-cytoplasmic transport of certain mRNAs. eIF4E is transported to the nucleus via its interaction with 4E-T (4E-transporter), but it is unclear how it is retained in the nucleus. Here we show that a sizable fraction (∼30%) of 4E-BP1 is localized to the nucleus, where it binds eIF4E. In mouse embryo fibroblasts (MEFs) subjected to serum starvation and/or rapamycin treatment, nuclear 4E-BPs sequester eIF4E in the nucleus. A dramatic loss of nuclear 4E-BP1 occurs in c-Ha-Ras–expressing MEFs, which fail to show starvation-induced nuclear accumulation of eIF4E. Therefore, 4E-BP1 is a regulator of eIF4E cellular localization.

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