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

CARP-2
E3 ubiquitin ligase

How to Cite

Long, Q.-Q., Wang, X.-Z., Su, Q.-Y., Zhu, X.-Y., Wang, J., & Long, , X.-D. (2023). Caspases‑8/10-associated RING protein 2: an update. American Journal of Translational Medicine, 7(1), 3–16. Retrieved from https://ajtm.journals.publicknowledgeproject.org/index.php/ajtm/article/view/2721

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

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