p28 Bap31, a Bcl-2/Bcl-XL- and Procaspase-8-associated Protein in the Endoplasmic Reticulum

doi:10.1083/jcb.139.2.327

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© The Rockefeller University Press, 0021-9525/1997//327 $5.00
The Journal of Cell Biology, Volume 139, Number 2, , 1997 327-338

Article

p28 Bap31, a Bcl-2/Bcl-X_L- and Procaspase-8–associated Protein in the Endoplasmic Reticulum

Florence W.H. Ng^*, Mai Nguyen^*, Tony Kwan^*, Philip E. Branton^*, Donald W. Nicholson, James A. Cromlish^*, and Gordon C. Shore^*

^* Department of Biochemistry, McIntyre Medical Sciences Building, McGill University, Montreal, Quebec, Canada H3G 1Y6; and Merck-Frosst Center for Therapeutic Research, Pointe Claire–Dorval, Quebec, Canada H9R 4P8

We have identified a human Bcl-2–interacting protein,p28 Bap31. It is a 28-kD (p28) polytopic integral protein ofthe endoplasmic reticulum whose COOH-terminal cytosolic regioncontains overlapping predicted leucine zipper and weak deatheffector homology domains, flanked on either side by identical caspase recognition sites. In cotransfected 293T cells, p28 is part of a complex that includes Bcl-2/Bcl-X_L and procaspase-8(pro-FLICE). Bax, a pro-apoptotic member of the Bcl-2 family,does not associate with the complex; however, it prevents Bcl-2from doing so. In the absence (but not presence) of elevatedBcl-2 levels, apoptotic signaling by adenovirus E1A oncoproteins promote cleavage of p28 at the two caspase recognition sites.Purified caspase-8 (FLICE/MACH/Mch5) and caspase-1(ICE), butnot caspase-3 (CPP32/apopain/ Yama), efficiently catalyze thisreaction in vitro. The resulting NH₂-terminal p20 fragmentinduces apoptosis when expressed ectopically in otherwise normalcells. Taken together, the results suggest that p28 Bap31 is part of a complex in the endoplasmic reticulum that mechanicallybridges an apoptosis-initiating caspase, like procaspase-8,with the anti-apoptotic regulator Bcl-2 or Bcl-X_L. This raisesthe possibility that the p28 complex contributes to the regulationof procaspase-8 or a related caspase in response to E1A, dependenton the status of the Bcl-2 setpoint within the complex.

Abbreviations used in this paper: GST, glutathione S-transferase; HMK, heart muscle kinase; TM, transmembrane.

Address all correspondence to Gordon C. Shore, Department ofBiochemistry, McIntyre Medical Sciences Building, McGill University,Montreal, QC, Canada H3G 1Y6. Tel.: (514) 398-7282; Fax: (514)398-7384; E-mail: shore{at}medcor.mcgill.ca

The present address for James A. Cromlish is Institut de Recherches Cliniques de Montréal, Montréal, QC, Canada H2W1R7.

This work was financed by operating grants from the NationalCancer Institute of Canada and the Medical Research Council.

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