Death effector domain DEDa, a self-cleaved product of caspase-8/Mch5, translocates to the nucleus by binding to ERK1/2 and upregulates procaspase-8 expression via a p53-dependent mechanism
Open Access
- 8 February 2007
- journal article
- research article
- Published by Wiley in The EMBO Journal
- Vol. 26 (4) , 1068-1080
- https://doi.org/10.1038/sj.emboj.7601571
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- The death effector domain protein familyOncogene, 2003
- Interdimer processing mechanism of procaspase-8 activationThe EMBO Journal, 2003
- Pro-caspase-3 Is a Major Physiologic Target of Caspase-8Journal of Biological Chemistry, 1998
- Caspases: Enemies WithinScience, 1998
- Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of ApoptosisPublished by Elsevier ,1998
- Death-effector Filaments: Novel Cytoplasmic Structures that Recruit Caspases and Trigger ApoptosisThe Journal of cell biology, 1998
- FLICE is activated by association with the CD95 death-inducing signaling complex (DISC)The EMBO Journal, 1997
- Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteasesProceedings of the National Academy of Sciences, 1996
- In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains.Proceedings of the National Academy of Sciences, 1996
- Involvement of MACH, a Novel MORT1/FADD-Interacting Protease, in Fas/APO-1- and TNF Receptor–Induced Cell DeathCell, 1996