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J Biol Chem, Vol. 275, Issue 2, 1439-1448, January 14, 2000
From the BNIP3 (formerly NIP3) is a pro-apoptotic,
mitochondrial protein classified in the Bcl-2 family based on limited
sequence homology to the Bcl-2 homology 3 (BH3) domain and
COOH-terminal transmembrane (TM) domain. BNIP3 expressed in yeast and
mammalian cells interacts with survival promoting proteins Bcl-2,
Bcl-XL, and CED-9. Typically, the BH3 domain of
pro-apoptotic Bcl-2 homologues mediates Bcl-2/Bcl-XL heterodimerization and confers pro-apoptotic activity. Deletion mapping
of BNIP3 excluded its BH3-like domain and identified the NH2 terminus (residues 1-49) and TM domain as critical for
Bcl-2 heterodimerization, and either region was sufficient for
Bcl-XL interaction. Additionally, the removal of the
BH3-like domain in BNIP3 did not diminish its killing activity. The TM
domain of BNIP3 is critical for homodimerization, pro-apoptotic
function, and mitochondrial targeting. Several TM domain mutants were
found to disrupt SDS-resistant BNIP3 homodimerization but did not
interfere with its killing activity or mitochondrial localization.
Substitution of the BNIP3 TM domain with that of cytochrome
b5 directed protein expression to
nonmitochondrial sites and still promoted apoptosis and
heterodimerization with Bcl-2 and Bcl-XL. We propose that BNIP3 represents a subfamily of Bcl-2-related proteins that functions without a typical BH3 domain to regulate apoptosis from both
mitochondrial and nonmitochondrial sites by selective
Bcl-2/Bcl-XL interactions.
BNIP3 Heterodimerizes with Bcl-2/Bcl-XL and Induces
Cell Death Independent of a Bcl-2 Homology 3 (BH3) Domain at Both
Mitochondrial and Nonmitochondrial Sites*
§¶,
,§,,,§§§
Manitoba Institute of Cell Biology,
University of Manitoba, Winnipeg, Manitoba R3E 0V9, Canada, the
Institute for Biological Sciences, Ottawa K1A 0R6, Canada, the
** Department of Pathology, Kyung Hee University College of Medicine,
Seoul 130-701, Korea, the Burnham
Institute, La Jolla, California 92037-1062, and the
§ Department of Biochemistry and Medical Genetics, Faculty
of Medicine, University of Manitoba,
Winnipeg, Manitoba R3E 0W3, Canada
*
This work was supported by the Medical Research Council of
Canada and the National Cancer Institute of Canada.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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