Details

Autor(en) / Beteiligte

• 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

Titel

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

Ist Teil von

• Proceedings of the National Academy of Sciences - PNAS, 1997-10, Vol.94 (21), p.11333-11338

Ort / Verlag

United States: National Acad Sciences

Erscheinungsjahr

1997

Quelle

Free E-Journal (出版社公開部分のみ）

Beschreibungen/Notizen

• 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 BclX L and FLICE in mammalian cells. Thus, MRIT is a mammalian protein that interacts simultaneously with both caspases and a Bcl-2 family member.