Caspases‑8/10-associated RING protein 2: an update

Abstract

Caspases-8/10-associated RING protein 2 (CARP-2) is a novel E3 ubiquitin ligase that has a special protein spatial structure, containing three conserved domains: an FYVE-like domain, a caspase interaction domain, and a RING domain. CARP-2 can regulate biological processes via the ubiquitin-proteasome pathway, including indirectly promoting cell migration by polyubiquitinating and degrading PRR5L protein, negatively regulating the extrinsic cell death pathway by ubiquitin-mediated degradation of caspases 8 and 10, promoting the ubiquitination and degradation of the receptor-interacting kinase (RIP) to negatively regulate NF-κB activation, and directly or indirectly promoting P53 protein ubiquitination and degradation. Inhibiting the expression of CARP-2 impedes cell proliferation, growth, and migration and enhances tumor cell response to chemotherapeutic agents. This review summarizes the structure and functions of CARP-2.text