IndraLab

Statements

CYLD activates RIGI. 7 / 7
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"CYLD can also mediate necroptosis independently of TNF receptors via TLR3 and TLR4 (Schworer et al., 2014) or via RIG-1 (Schock et al., 2017), and can mediate necroptosis-like cell death in response to oxidative stress in neuronal cells (Ganjam et al., 2018)."
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"We hypothesized that the inhibition of CYLD cleavage by a caspase inhibitor may attenuate the activation of the TLR3 and RIG-I pathways."
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"The effect of CYLD was not specific to RIG-I , as CYLD also deubiquitinated and inhibited the signaling activities of TBK1 and IKKepsilon ."
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"miR-526a downregulates the expression of the deubiquitylating enzyme CYLD, which ultimately promotes RIG-I K63 linked ubiquitylation and interferon responses 152."
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"Ubiquitylation events are reversible processes, and, accordingly, several deubiquitylating enzymes, in particular ubiquitin specific peptidase 3 (USP3), USP21 and CYLD lysine 63 deubiquitinase (CYLD), modulate RIG-I signalling by removing K63-polyubiquitin chains, although with unique kinetics."
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"The data indicate that CYLD targets RIG-I as well as TBK1 for deubiquitination that leads to inactivation of the signaling."
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"Ubiquitylation events are reversible processes , and , accordingly , severaldeubiquitylating enzymes , in particular ubiquitin specific peptidase 3 ( USP3 ) , USP21 and CYLD lysine 63 deubiquitinase ( CYLD ) , modulate RIG-I signalling by removing K63-polyubiquitin chains , although with unique kinetics ( reviewed elsewhere112 ,118 ) ."
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