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  • Original Paper
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Caspase-8 sumoylation is associated with nuclear localization

Oncogene volume 24, pages 3268–3273 (2005)Cite this article

Abstract

The cysteine protease caspase-8 plays a pivotal role in the initiation of different apoptotic pathways and controls the maturation and differentiation of various cell types including neurons, fibroblasts and lymphocytes. Specific substrates of caspase-8 are present in both the cytoplasm and the nucleus, which may determine the ultimate biological effect of caspase-8. However, the mechanisms regulating the cellular localization of caspase-8 are still unknown. We show here that, in contrast to other caspases such as caspase-9 and -3, caspase-8 can be sumoylated at lysine 156. This sumoylation (i) is associated with the nuclear localization of caspase-8 and (ii) did not impair caspase-8 activation.

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Acknowledgements

This work was supported by INSERM and by grants from the Fondation de France and Association pour la Recherche sur le Cancer (ARC). L Besnault-Mascard holds fellowships from Fondation pour la Recherche Médicale (2001–2002) and Académie Nationale de Médecine (2002–2003).

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Authors and Affiliations

  1. INSERM U542, Hôpital Paul Brousse, Bâtiment Lavoisier, 14 Avenue Paul Vaillant Couturier, 94807, Villejuif cedex, France

    Laurence Besnault-Mascard, Marie Thérèse Auffredou, Marie Françoise Bourgeade, Hans Kristian Lorenzo & Aimé Vazquez

  2. INSERM 528, Institut Curie, Paris, France

    Corinne Leprince, Brigitte Meunier & Jacques Camonis

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  1. Laurence Besnault-Mascard
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Correspondence to Aimé Vazquez.

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Besnault-Mascard, L., Leprince, C., Auffredou, M. et al. Caspase-8 sumoylation is associated with nuclear localization. Oncogene 24, 3268–3273 (2005). https://doi.org/10.1038/sj.onc.1208448

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