Cancer Res. 1997 Feb 15;57(4):615-9.

CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP.External

Ahmad, M., Srinivasula, S. M., Wang, L., Talanian, R. V., Litwack, G., Fernandes-Alnemri, T., Alnemri, E. S.,
--- - Kimmel Cancer Institute, Jefferson Medical College, Philadelphia, Pennsylvania 19107, USA.
FADD/MORT1 is a death domain (DD)-containing adaptor/signaling molecule that interacts with the intracellular DD of FAS/APO-I (CD95) and tumor necrosis factor receptor 1 and the prodomain of caspase-8 (Mch5/MACH/FLICE). FADD engagement of caspase-8 presumably activates this caspase and leads to apoptosis. Another DD-containing adaptor/signaling molecule, CRADD, was identified and was shown to induce apoptosis. CRADD has a dual-domain structure similar to that of FADD. It has an NH2-terminal caspase homology domain that interacts with caspase-2 and a COOH-terminal DD that interacts with RIP. CRADD is constitutively expressed in many tissues and thus could play a role in regulating apoptosis in mammalian cells.
PMID: 9044836External
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
CARD Caspase2 Link RAIDD GST fusion protein pull-down Not specified Not specified In vitro translation Human Not specified E.coli 9044836
DD RAIDD Link RIP GST fusion protein pull-down Human Not specified E.coli Human Not specified In vitro translation 9044836
(Link: click this icon to show interactions only between the two corresponding DDs)