Caspase recruitment domains for protein�interactions in cellular signaling (Review)

Abstract

The caspase recruitment domain (CARD), a well-known protein interaction module, belongs to the death domain (DD) superfamily, which includes DDs, death effector domains, and pyrin domains. The DD superfamily mediates the protein interactions necessary for apoptosis and immune cell signaling pathways. Among these domains, the CARD has been studied extensively as it mediates important cellular signaling events that are associated with various human diseases including cancer, neuro-degenerative diseases and immune disorders. Homo-type and hetero-type CARD-CARD interactions mediate the formation of large signaling complexes, including caspase-activating complexes and downstream signaling complexes. The present review summarizes and discusses the results of structural studies of various CARDs and their complexes. These studies shed light on the mechanisms that control the assembly and disassembly of signaling complexes and provide an improved understanding of cellular signaling processes.

Effect of Bitis gabonica and Dendroaspis angusticeps snake venoms on apoptosis-related genes in human thymic epithelial cells

“…CARDs are known as protein interaction modules, implicated in protein interactions required for apoptosis and immunity [ 120 ]. The CARD9 signalosome is known to mediate NF-κB and mitogen-activated protein kinase (MAPK) signaling, although the exact mechanisms underlying this activation process and the outcome of these molecular interactions are yet to be elucidated [ 121 ].…”

A Mitocentric View of the Main Bacterial and Parasitic Infectious Diseases in the Pediatric Population

“… Types of caspases: classification and main functions. Initiator caspases, including CARD [ 17 ] and DED [ 18 ], and effector caspases, including procaspases, as well as their functions are represented. CARD, caspase activation and recruitment domain; DED, death effector domain.…”

Assembly of platforms for signal transduction in the new era: dimerization, helical filament assembly, and beyond

“…Each member of the DD superfamily interacts with members of its own subfamily 3,8,[36][37][38] . The general strategy of DD superfamily assembly was revealed via a structural study of the PIDDosome core complex, a molecular complex that activates caspase-2 and is composed of RAIDD DD and PIDD DD 7 .…”