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J Biol Chem, Vol. 273, Issue 15, 8705-8710, April 10, 1998
,
From the Department of Pathology and Comprehensive Cancer Center,
The University of Michigan Medical School, Ann Arbor, Michigan 48109, the We have identified and characterized Mtd, a novel
regulator of apoptosis. Sequence analysis revealed that Mtd is a member of the Bcl-2 family of proteins containing conserved BH1, BH2, BH3, and
BH4 regions and a carboxyl-terminal hydrophobic domain. In adult
tissues, Mtd mRNA was predominantly detected in the brain, liver,
and lymphoid tissues, while in the embryo Mtd mRNA was detected in
the liver, thymus, lung, and intestinal epithelium. Expression of Mtd
promoted the death of primary sensory neurons, 293T cells and HeLa
cells, indicating that Mtd is a proapoptotic protein. Unlike all other
known death agonists of the Bcl-2 family, Mtd did not bind
significantly to the survival-promoting proteins Bcl-2 or
Bcl-XL. Furthermore, apoptosis induced by Mtd was not inhibited by Bcl-2 or Bcl-XL. A Mtd mutant with glutamine
substitutions of highly conserved amino acids in the BH3 domain
retained its ability to promote apoptosis, further indicating that Mtd
does not promote apoptosis by heterodimerizing with Bcl-2 or
Bcl-XL. Mtd-induced apoptosis was not blocked by broad
range synthetic caspase inhibitors z-VAD-fmk or a viral protein CrmA.
Mtd is the first example of a naturally occurring Bcl-2 family member
that can activate apoptosis independently of heterodimerization with survival-promoting Bcl-2 and Bcl-XL.
Department of Pathology, Centre Medical
Universitaire, 1211 Geneva 4, Switzerland, and the § Unidad
de Immunologia, Departamento de Biologia Molecular, Universidad de
Cantabria, Santander 39011, Spain
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