Proc Natl Acad Sci U S A. 1997 Oct 14;94(21):11333-8.

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

Han, D. K., Chaudhary, P. M., Wright, M. E., Friedman, C., Trask, B. J., Riedel, R. T., Baskin, D. G., Schwartz, S. M., Hood, L.,
--- - Department of Pathology, University of Washington, Seattle, WA 98195, USA.
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.
PMID: 9326610External
Arrow2 In vitro interaction Arrow2 In vivo interaction Arrow2 Characterization Arrow2 Functional role Arrow2 top
In vitro interaction
  DD1 DD2 Reference
Family DD1 DD2 Method Species Region Expression Species Region Expression
DED Caspase8 Link FLIP Yeast two-hybrid Not specified 1-480 In vitro translation Human 1-208 Not specified 9326610
DED Caspase8 Link FLIP Yeast two-hybrid Not specified 1-216 In vitro translation Human 1-180 Not specified 9326610
DED FADD Link FLIP Yeast two-hybrid Not specified 1-208 In vitro translation Human 1-180 Not specified 9326610
(Link: click this icon to show interactions only between the two corresponding DDs)