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. 2022 Dec 6;12(12):1825. doi: 10.3390/biom12121825

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© 2022 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Overview of DUBs-mediated regulation of necroptosis. TNFRSF1A activates recruitment complex 1 (TRADD-TRAF2-RIPK1-BIRC2/3 complex), and RIPK1 is a core regulatory kinase regulated by ubiquitination. The DUBs CYLD and OTULIN stabilize RIPK1 for further ripoptosome formation (complex IIb). The ripoptosome complex has TRADD, FADD, CASP8/10, and RIPK1/3. If the activity of CASP8/10 is inhibited, RIPK1/3 and MLKL form necrosomes in which MLKL is phosphorylated by RIPK3. Translocation of active MLKL to the plasma membrane results in membrane rupture. USP22 and TNFAIP3 reduce RIPK3 K518 and K5 ubiquitination, respectively. TNFAIP3 inhibits necroptosis, whereas USP22 accelerates necroptosis.