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CYLD deubiquitinates TRAF6. 19 / 19
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"CYLD binding to one of its targets, TRAF6, requires the adaptor protein p62, which promotes the deubiquitylation of TRAF6 by CYLD 17 and probably also modulates the DUB activity of CYLD through induction of CYLD ubiquitylation 34."

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"Conversely, the PB1 domain of p62 also interacts with CYLD, a deubiquitinase, which inhibits TRAF6 polyubiquitination and serves as a negative regulator for RANK mediated NF-kappaB activation and osteoclastogenesis 113."

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"In support of this notion, in vivo poly-ubiquitination assays demonstrate that depletion of beta-TRCP impaired TRAF6 self ubiquitination likely due to enhancement of TRAF6 deubiquitination by CYLD, concomitant with a reduction in beta-TRCP-dependent ubiquitination of CYLD and impairment of auto-phosphorylation of TRAF6-downstream kinase IKKalpha."

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"CYLD deubiquitylates TRAF6, which transduces the RANK-mediated signal [99]."

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"For instance, p62, one adaptor protein, can promote the deubiquitylation of TRAF6 (one of p62 targets) by CYLD."

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"Here we demonstrated that during the RANKL dependent signaling pathway, CYLD stabilization by depletion of beta-TRCP decreased the ubiquitination of TRAF6 and impaired auto-phosphorylation of the TRAF6-downstream kinase IKKalpha."

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"OPTN negatively regulates IRAK-1 mediated NF-kappaB activation possibly by facilitating CYLD dependent deubiquitination of TRAF6."

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"Another example is already mentioned CYLD, which is an important inflammatory mediator that deubiquitinates TRAF2 and TRAF6, resulting in negative regulation of the NF-kappaB pathway [XREF_BIBR, XREF_BIBR, XREF_BIBR, XREF_BIBR]."

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"Previously it has been known that TNF receptor associated factor 6 (TRAF6) acts as an E3 ligase for Akt-K63 polyubiquitination, and CYLD deubiquitinates TRAF6."

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"CYLD also decreased IFN promotor activation by deubiquitinating TRAF2 and TRAF6 in HEK293 T cells, respectively [29, 30] ."

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"Then we investigated the roles A20 and CYLD in CK8 mediated inhibition of TRAF6 ubiquitination."

"Moreover, additional studies showed that CYLD specifically deubiquitinates polyubiquitin chains at K63 of different substrates (e.g., TRAF2 and TRAF6), or tyrosine kinase receptors such as TrkA."

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"Specifically, as suggested by Jin et al. [XREF_BIBR], deubiquitinating enzyme CYLD negatively regulated TRAF6 ubiquitination by interacting with P62 and subsequently inhibited proangiogenesis function of TRAF6."

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"[XREF_BIBR] CYLD deubiquitination of TRAF6, RIP1, and NF-kappaB-essential modulator (NEMO) leads to inactivation of NF-kappaB signaling."

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"CYLD deubiquitinates TRAF6 and TRAF7 to negatively regulate peptidoglycan-induced Toll-Like receptor 2 (TLR2) signaling and inflammation [45]."

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"In the absence of any robust stimulation of NF-kappaB (such as TCR engagement or cytokine signaling), CYLD deubiquitylates TRAF2, TRAF6, and NEMO, dampening NF-kappaB signaling by removing activating K63 chains formed by TRAF2/6."

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"Numerous studies in vitro and in vivo have validated that CYLD mediates NF-κB activation by deubiquitinating TRAF2, TRAF6, and NEMO, making it an important regulator in the adaptive immune response."

"The nf-kappab activation by cyld is mediated, at least in part, by the deubiquitination and inactivation of tnfr-associated factor 2 (traf2) and, to a lesser extent, traf6."

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"As it has previously been demonstrated that CYLD deubiquitinates TRAF6 these results suggests that CYLD deubiquitinates and suppresses the activity of both the E3 ligase and its kindred substrate [184[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"