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The procaspase-8 isoform, procaspase-8L, ... ex at the endoplasmic reticulum
The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum
5394
BAP31 is an integral protein of the endoplasmic reticulum membrane and a substrate of caspase-8. Here, we describe the procaspase-8 isoform, procaspase-8L, which is ubiquitously expressed and selectively recruited to the BAP31 complex in response to apoptotic signaling by E1A. Procaspase-8L is characterized by the N-terminal extension (Nex) domain, which extends procaspase-8/a at the N terminus and is required for selective association of procaspase-8L with the BAP31 complex. Gene deletion identified BAP31 and related BAP29 as required for processing of procaspase-8L in response to E1A, by a FADD-independent mechanism that was blocked by BCL-2. Further, Bap29,31 deletion, as well as a Nex-domain dominant-negative mutant, curtailed the activation of downstream caspases (IETDase and DEVDase) and cell death in response to E1A. Preferential recruitment of procaspase-8L by the BAP31 complex at the endoplasmic reticulum suggests an additional pathway for regulating initiator caspase-8 during apoptosis.
Breckenridge DG, Nguyen M, Kuppig S, Reth M, Shore GC
Proceedings of the National Academy of Sciences of the United States of America
2002-04-02 00:00
99
7
4331-6
Adenovirus E1A Proteins,Amino Acid Sequence,Apoptosis,Base Sequence,Caspase 8,Caspase 9,Caspases,Endoplasmic Reticulum,Enzyme Precursors,Humans,Isoenzymes,KB Cells,Membrane Proteins,Molecular Sequence Data,Open Reading Frames,Proteins,Adenovirus E1A Proteins,BCAP29 protein, human,BCAP31 protein, human,Enzyme Precursors,Isoenzymes,Membrane Proteins,Proteins,CASP8 protein, human,CASP9 protein, human,Caspase 8,Caspase 9,Caspases
Department of Biochemistry, McIntyre Medical Sciences Building, McGill University, Montreal, QC, Canada H3G 1Y6.
Proc. Natl. Acad. Sci. U.S.A.
0027-8424
10.1073/pnas.072088099
072088099
0
False
11917123
