MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death.

Abstract:

:Activation of the cascade of proteolytic caspases has been identified as the final common pathway of apoptosis in diverse biological systems. We have isolated a gene, termed MRIT, that possesses overall sequence homology to FLICE (MACH), a large prodomain caspase that links the aggregated complex of the death domain receptors of the tumor necrosis factor receptor family to downstream caspases. However, unlike FLICE, the C-terminal domain of MRIT lacks the caspase catalytic consensus sequence QAC(R/Q)G. Nonetheless MRIT activates caspase-dependent death. Using yeast two-hybrid assays, we demonstrate that MRIT associates with caspases possessing large and small prodomains (FLICE, and CPP32/YAMA), as well as with the adaptor molecule FADD. In addition, MRIT simultaneously and independently interacts with BclXL and FLICE in mammalian cells. Thus, MRIT is a mammalian protein that interacts simultaneously with both caspases and a Bcl-2 family member.

authors

Han DK,Chaudhary PM,Wright ME,Friedman C,Trask BJ,Riedel RT,Baskin DG,Schwartz SM,Hood L

doi

10.1073/pnas.94.21.11333

subject

Has Abstract

pub_date

1997-10-14 00:00:00

pages

11333-8

issue

21

eissn

0027-8424

issn

1091-6490

journal_volume

94

pub_type

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