Oncogene. 2005 May 5;24(20):3268-73.

Caspase-8 sumoylation is associated with nuclear localization.External

Besnault-Mascard, L., Leprince, C., Auffredou, M. T., Meunier, B., Bourgeade, M. F., Camonis, J., Lorenzo, H. K., Vazquez, A.,
--- - INSERM U542, Hopital Paul Brousse, Batiment Lavoisier, 14 Avenue Paul Vaillant Couturier, 94807 Villejuif cedex, France.
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.
PMID: 15782135External
Arrow2 In vitro interaction Arrow2 In vivo interaction Arrow2 Characterization Arrow2 Functional role Arrow2 top
In vitro interaction
  DD1 DD2 Reference
Family DD1 DD2 Method Species Region Expression Species Region Expression
DED Caspase8 Link FADD Yeast two-hybrid Human Full length Yeast Not specified Not specified Yeast 15782135
(Link: click this icon to show interactions only between the two corresponding DDs)