Inhibition of Ribosome Recruitment Induces Stress Granule Formation Independently of Eukaryotic Initiation Factor 2α Phosphorylation

Molecular Biology of the Cell - Tập 17 Số 10 - Trang 4212-4219 - 2006
Rachid Mazrouï1, Rami Sukarieh2, Marie-Eve Bordeleau2, Randal J. Kaufman3,4, Peter T. Northcote5, Junichi Tanaka6, Imed‐Eddine Gallouzi2, Jerry Pelletier2,7
1Department of Biochemistry, McGill University Montreal, Quebec, Canada H3G 1Y6
2Department of Biochemistry and
3Departments of Biological Chemistry and Internal Medicine, University of Michigan, Ann Arbor, MI 48109;
4Howard Hughes Medical Institute, and
5School of Chemical and Physical Sciences, Victoria University of Wellington, Wellington 6140, New Zealand; and
6Department of Chemistry, Biology and Marine Sciences, University of the Ryukyus, Nishihara, Okinawa 903-0213, Japan
7McGill Cancer Center, McIntyre Medical Sciences Building, McGill University, Montreal, Quebec, Canada H3G 1Y6;

Tóm tắt

Cytoplasmic aggregates known as stress granules (SGs) arise as a consequence of cellular stress and contain stalled translation preinitiation complexes. These foci are thought to serve as sites of mRNA storage or triage during the cell stress response. SG formation has been shown to require induction of eukaryotic initiation factor (eIF)2α phosphorylation. Herein, we investigate the potential role of other initiation factors in this process and demonstrate that interfering with eIF4A activity, an RNA helicase required for the ribosome recruitment phase of translation initiation, induces SG formation and that this event is not dependent on eIF2α phosphorylation. We also show that inhibition of eIF4A activity does not impair the ability of eIF2α to be phosphorylated under stress conditions. Furthermore, we observed SG assembly upon inhibition of cap-dependent translation after poliovirus infection. We propose that SG modeling can occur via both eIF2α phosphorylation-dependent and -independent pathways that target translation initiation.

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Molecular Biology of the Cell

Tập 17 Số 10

4212-4219

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