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Caspase-8 sumoylation is associated with nuclear localization

Authors :
Jacques Camonis
Laurence Besnault-Mascard
Hans Kristian Lorenzo
Marie Françoise Bourgeade
Brigitte Meunier
Marie Thérèse Auffredou
Aimé Vazquez
Corinne Leprince
Greffes d'Epitheliums et Regulation de l'Activation Lymphocytaire
Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Transduction du signal et oncogénèse
Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM)
Source :
Oncogene, Oncogene, Nature Publishing Group, 2005, 24 (20), pp.3268-73. ⟨10.1038/sj.onc.1208448⟩
Publication Year :
2005
Publisher :
HAL CCSD, 2005.

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.

Details

Language :
English
ISSN :
09509232 and 14765594
Database :
OpenAIRE
Journal :
Oncogene, Oncogene, Nature Publishing Group, 2005, 24 (20), pp.3268-73. ⟨10.1038/sj.onc.1208448⟩
Accession number :
edsair.doi.dedup.....ab42bae6a32ad047f1982687d0b9acbc
Full Text :
https://doi.org/10.1038/sj.onc.1208448⟩