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J Biol Chem, Vol. 273, Issue 6, 3140-3143, February 6, 1998
From the Department of Biochemistry, McGill University, Montreal,
Quebec H3G 1Y6, Canada
Bap31 is a polytopic integral membrane protein of
the endoplasmic reticulum and forms a complex with
Bcl-2/Bcl-XL and procaspase-8 (Ng, F. W. H., Nguyen, M., Kwan, T., Branton, P. E., Nicholson, W. D.,
Cromlish, J. A., and Shore, G. C. (1997) J. Cell Biol. 139, 327-338). In co-transfected human cells, procaspase-8 is capable of interacting with Ced-4, an important adaptor molecule in
Caenorhabditis elegans that binds to and activates the
C. elegans procaspase, proCed-3. Here, we show that the
predicted death effector homology domain within the cytosolic region of
Bap31 interacts with Ced-4 and contributes to recruitment of
procaspase-8. Bcl-XL, which binds directly but weakly to
the polytopic transmembrane region of Bap31, indirectly and
cooperatively associates with the Bap31 cytosolic domain, dependent on
the presence of procaspase-8 and Ced-4. Ced-4
c does not interact
with Bcl-XL but rather displaces it from Bap31, suggesting
that an endogenous Ced-4-like adaptor is a normal constituent of the
Bap31 complex and is required for stable association of
Bcl-XL with Bap31 in vivo. These findings indicate that Bap31 is capable of recruiting essential components of a
core death regulatory machinery.
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