J Biol Chem. 1997 Jul 11;272(28):17255-7.

I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1- and CD-95-induced apoptosis.External

Hu, S., Vincenz, C., Ni, J., Gentz, R., Dixit, V. M.,
--- - Department of Pathology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
The pivotal discovery that the death proteases caspase 8 (FLICE) and caspase 10 (Mch4/FLICE2) are recruited to the CD-95 and tumor necrosis factor receptor-1 signaling complexes suggested a mechanism used by these cytotoxic receptors to initiate apoptosis. In this report, we describe the cloning and characterization of I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1- and CD-95-induced apoptosis. The overall architecture of I-FLICE is strikingly similar to that of FLICE and Mch4/FLICE2. However, I-FLICE lacks both a catalytic active site and residues that form the substrate binding pocket, in keeping with its dominant negative inhibitory function. I-FLICE is the first example of a catalytically inert caspase that can inhibit apoptosis.
PMID: 9211860External
Arrow2 In vitro interaction Arrow2 In vivo interaction Arrow2 Characterization Arrow2 Functional role Arrow2 top
In vivo interaction
  Endogenous
expression
Overexpression DD1 DD2 Reference
Family DD1 DD2 Method Species Region Species Region
DED Caspase10 Link FLIP Co-immunoprecipitation HEK293 Not specified Not specified Human Full length 9211860
DED Caspase8 Link FLIP Co-immunoprecipitation HEK293 Not specified Not specified Human Full length 9211860
(Link: click this icon to show interactions only between the two corresponding DDs)