Ontology highlight
ABSTRACT:
SUBMITTER: Ann-Kathrin Otto
PROVIDER: MODEL2210170001 | biostudies-other |
SECONDARY ACCESSION(S): 35994517
REPOSITORIES: biostudies-other

Cell reports 20151206 10
Ubiquitination and deubiquitination are crucial for assembly and disassembly of signaling complexes. LUBAC-generated linear (M1) ubiquitin is important for signaling via various immune receptors. We show here that the deubiquitinases CYLD and A20, but not OTULIN, are recruited to the TNFR1- and NOD2-associated signaling complexes (TNF-RSC and NOD2-SC), at which they cooperate to limit gene activation. Whereas CYLD recruitment depends on its interaction with LUBAC, but not on LUBAC's M1-chain-for ...[more]