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J Biol Chem. 2009 Jun 19;284(25):16711-5. doi: 10.1074/jbc.R900002200. Epub 2009 Feb 23.

eIF4E: new family members, new binding partners, new roles.

Author information

1
Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, Louisiana 71130-3932, USA. rrhoad@lsuhsc.edu

Abstract

Eukaryotic initiation factor 4E (eIF4E) has long been known as the cap-binding protein that participates in recruitment of mRNA to the ribosome. A number of recent advances have not only increased our understanding of how eIF4E acts in translation but also uncovered non-translational roles. New structures have been determined for eIF4E in complex with various ligands and for other cap-binding proteins. We have also learned that most eukaryotic organisms express multiple eIF4E family members, some involved in general translation but others having specialized functions, including repression of translation. A number of new eIF4E-binding proteins have been reported, some of which tether it to specific mRNAs.

PMID:
19237539
PMCID:
PMC2719305
DOI:
10.1074/jbc.R900002200
[Indexed for MEDLINE]
Free PMC Article
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