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J Biol Chem, Vol. 274, Issue 2, 1156-1163, January 8, 1999
From the Howard Hughes Medical Institute, Departments of Medicine
and Pathology, Washington University School of Medicine, St. Louis,
Missouri 63110 and the § Memorial Sloan-Kettering Cancer
Center, New York, New York 10021
"BH3 domain only" members of the BCL-2 family
including the pro-apoptotic molecule BID represent candidates to
connect with proximal signal transduction. Tumor necrosis factor
Caspase Cleaved BID Targets Mitochondria and Is Required for
Cytochrome c Release, while BCL-XL Prevents
This Release but Not Tumor Necrosis Factor-R1/Fas Death
(TNF) treatment induced a caspase-mediated cleavage of cytosolic,
inactive p22 BID at internal Asp sites to yield a major p15 and minor
p13 and p11 fragments. p15 BID translocates to mitochondria as an
integral membrane protein. p15 BID within cytosol targeted normal
mitochondria and released cytochrome c. Immunodepletion of
p15 BID prevents cytochrome c release. In vivo,
anti-Fas Ab results in the appearance of p15 BID in the cytosol of
hepatocytes which translocates to mitochondria where it releases
cytochrome c. Addition of activated caspase-8 to normal
cytosol generates p15 BID which is also required in this system for
release of cytochrome c. In the presence of BCL-XL/BCL-2, TNF still induced BID cleavage and p15 BID
became an integral mitochondrial membrane protein. However,
BCL-XL/BCL-2 prevented the release of cytochrome
c, yet other aspects of mitochondrial dysfunction still
transpired and cells died nonetheless. Thus, while BID appears to be
required for the release of cytochrome c in the TNF death
pathway, the release of cytochrome c may not be required
for cell death.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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