Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2α phosphorylation

Rachid Mazroui, Rami Sukarieh, Marie Eve Bordeleau, Randal J. Kaufman, Peter Northcote, Junichi Tanaka, Imed Gallouzi, Jerry Pelletier

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239 Scopus citations

Abstract

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. © 2006 by The American Society for Cell Biology.
Original languageEnglish (US)
Pages (from-to)4212-4219
Number of pages8
JournalMolecular Biology of the Cell
Volume17
Issue number10
DOIs
StatePublished - Jan 1 2006
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

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