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Am J Physiol Cell Physiol 296: C1207-C1217, 2009. First published February 25, 2009; doi:10.1152/ajpcell.00511.2008
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PROTEIN AND VESICLE TRAFFICKING, CYTOSKELETON

The eIF4E-binding proteins are modifiers of cytoplasmic eIF4E relocalization during the heat shock response

R. Sukarieh,1 N. Sonenberg,1,2 and J. Pelletier1,2

1Department of Biochemistry and 2McGill Cancer Center, McGill University, Montreal, Quebec, Canada

Submitted 9 October 2008 ; accepted in final form 23 February 2009

Stress granules (SGs) arise as a consequence of cellular stress, contain stalled translation preinitiation complexes, and are associated with cell survival during environmental insults. SGs are dynamic entities with proteins relocating into and out of them during stress. Among the repertoire of proteins present in SGs is eukaryotic initiation factor 4E (eIF4E), a translation factor required for cap-dependent translation and that regulates a rate-limiting step for protein synthesis. Herein, we demonstrate that localization of eIF4E to SGs is dependent on the presence of a family of repressor proteins, eIF4E-binding proteins (4E-BPs). Our results demonstrate that 4E-BPs regulate the SG localization of eIF4E.

eukaryotic initiation factor 4E; stress granules


Address for reprint requests and other correspondence: J. Pelletier, McIntyre Medical Sciences Bldg., Rm. 810, 3655 Promenade Sir William Osler, McGill Univ., Montreal, Quebec, Canada, H3G 1Y6 (e-mail: jerry.pelletier{at}mcgill.ca)






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