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First published online 17 August 2004
doi: 10.1242/jcs.01356

Journal of Cell Science 117, 4461-4468 (2004)
Published by The Company of Biologists 2004
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Research Article

Regulation of cytoplasmic stress granules by apoptosis-inducing factor

Céline Candé1, Nicola Vahsen1, Didier Métivier1, Hélène Tourrière2, Karim Chebli2, Carmen Garrido3, Jamal Tazi2 and Guido Kroemer1,*

1 CNRS-UMR8125, Institut Gustave Roussy, 39 rue Camille-Desmoulins, 94805 Villejuif, France
2 CNRS-UMR5535, Université de Montpellier II, 34293 Montpellier CEDEX 5, France
3 INSERM U-517, Faculty of Medicine and Pharmacy, 7 Boulevard Jeanne d'Arc, 21033 Dijon, France

* Author for correspondence (e-mail: kroemer{at}igr.fr)

Accepted 10 June 2004

Stress granules (SG) are dynamic cytoplasmic foci in which stalled translation initiation complexes accumulate. In conditions of acute cellular redox, stress cells manipulated to lose the expression of apoptosis-inducing factor (AIF) nucleate SG signature proteins (e.g. TIA-1, PABP1) more efficiently than AIF-positive controls. AIF also inhibited SG formation induced by the RasGAP-associated endoribonuclease G3BP. Retransfection of mouse AIF into cells subjected to human AIF-specific siRNA revealed that only AIF imported into mitochondria could repress SGs and that redox-active domains of AIF, which are dispensable for its apoptogenic action, were required for SG inhibition. In response to oxidative stress, AIF-negative cells were found to deplete non-oxidized glutathione more rapidly than AIF-expressing cells. Exogenous supplementation of glutathione inhibited SG formation elicited by arsenate or G3BP. Together, these data suggest that the oxidoreductase function of AIF is required for the maintenance of glutathione levels in stress conditions and that glutathione is a major regulator of SG.

Key words: G3BP, TIA-1, Mitochondria, Programmed cell death


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