RAIDD/CRADD Products

Description

Apoptosis is triggered by activation of initiator caspases upon complex-mediated clustering of the inactive zymogen, as occurs in the caspase-9-activating apoptosome complex. Activation of caspase-2 occurs in a complex that contains the death domain-containing protein PIDD, whose expression is induced by p53, and the adaptor protein RAIDD (1). RAIDD 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. RAIDD is constitutively expressed in many tissues and thus could play a role in regulating apoptosis in mammalian cells (2). In metazoan cells there exists inactive polypeptide precursors (zymogens), each composed of a prodomain, which is cleaved to activate the protease, and a large and small catalytic subunit. The coupling of these proteases to signaling pathways is probably mediated by adaptor molecules that contain protein-protein interaction motifs such as the death domain (3).

Bioinformatics

Entrez	8738 Human
Uniprot	AAB42217 Human AAH17042 Human AAH37905 Human NM_003805 Human NP_003796 Human P78560 Human
Product By Gene ID	8738
Alternate Names	CASP2 and RIPK1 domain containing adaptor with death domain Caspase and RIP adapter with death domain caspase and RIP adaptor with death domain death domain containing protein CRADD death domain-containing protein CRADD MGC9163 RAIDDdeath adaptor molecule RAIDD RIP-associated ICH1/CED3-homologous protein with death domain RIP-associated protein with a death domain

Research Areas for RAIDD/CRADD

Find related products by research area and learn more about each of the different research areas below.

Apoptosis
Cancer
Cell Biology
Tumor Suppressors