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CYLD activates RIPK1. 16 / 17
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"CYLD Is Critical for Protection Against the Apoptosis Inducing Potential of RIPK1 in a Subset of Melanoma Cells."
32252875
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"In contrast, overexpression of CYLD caused downregulation of RIPK1 in Mel-CV and ME1007 cells, which was nevertheless reversed by the treatment with the proteasome inhibitor MG132 (XREF_FIG), substantiating that downregulation of RIPK1 expression by CYLD is mediated by the proteasomal degradation XREF_BIBR."
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"Cylindromatosis (CYLD), an enzyme that deubiquitinates K63 specifically, can mediate the RIPK1 deubiquitinating process to expedite the complex IIb-forming process, covering pro-caspase-8, FADD and TRADD [33]."
36100321
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"These observations strongly suggest that in ATLL cells, either viral encoded oncogenic proteins or mutations sustain the early cell death checkpoint by driving multiple IKKs to phosphorylate and suppress CYLD in order to prevent RIPK1 from becoming a death-signaling molecule (Fig. 8a)."
32024820
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"However, in the absence of caspase-8 (or its regulators FADD/FLIP), RIPK1 becomes deubiquitinated, due to CYLD stabilization, which leads to excessive RIPK1-driven RIPK3 activation."
22633487
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"Then, we found that RIP3 accounts for shikonin induced activation of MLKL, and activated MLKL reversely up-regulates the protein level of CYLD and promotes the activation of RIP1 and RIP3."
31560934
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"CYLD is an essential mediator of RIPK1 - and RIPK3-dependent necroptosis [ 145 ] ."
32354135
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"An alternative explanation for the embellished necroptotic sensitivity observed in casp8 deficient cells has been raised by Ting and colleagues, observing that casp8 mediated cleavage of the E3 ubiquitin ligase CYLD enhances RIP1 and RIP3 dependent necroptosis [XREF_BIBR]."
24856110
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"These data suggest that, in (CXCL4 + TLR8) costimulation, activation of TBK1 suppresses CYLD activation by phosphorylation, thereby reducing its cleavage by Caspase-8.RIPK1 kinase activity is regulated by TBK1 and Caspase-8 through direct phosphorylation at serine 320 and cleavage, respectively, while CYLD increases RIPK1 kinase activity by deubiquitylating K63 ubiquitin chain of RIPK1 [10, 15–17] (Fig. 1B)."
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"The finding that CYLD increases the enzymatic activity of RIPK1 in complex II [ 76 ] led to the hypothesis that its cleavage by CASP8 would prevent RIPK1 kinase-dependent necroptosis induction."
37357102
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"Cointroduction of CYLD or RIPK1 siRNA abolished apoptosis induced by introduction of miR-99b-3p mimics (XREF_FIG), confirming that downregulation of CYLD and subsequent upregulation of RIPK1 are responsible for induction of apoptosis by the mimics."
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"Mouse RIP3, RIP1, MLKL, and CYLD siRNAs were synthesized by GenePharma : RIP3-1 (cccgacgaugucuucugucaa), RIP3-2 (cuccuuaaagucaauaaacau), RIP1-1 (ccacuagucugacugauga), RIP1-2 (ucaccaauguugcaggaua), CYLD-1 (uccauugaggauguaaauaaa), CYLD-2 (aaggguugaaccauuguuaaa), MLKL-1 (gagauccaguucaacgaua), and MLKL-2 (uaccaucaaaguauucaacaa)."
25093162
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"CYLD and A20 function as deubiquitination enzymes to inhibit IKK by targeting RIP1 upstream of IKK, while CUEDC2 acts as an adaptor protein to keep IKK in an inactivated status by recruiting a phospha[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"CYLD destabilizes complex I and allows RIP1 to dissociate from the plasma membrane."
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"However, a reduction in RIPK1 ubiquitination, either by deubiquitinating enzyme cylindromatosis protein (CYLD) or inhibition of cIAPs with SMAC mimetic (SM), leads to RIPK1 dissociation from complex I. Subsequently, RIPK1 binds to RIPK3, FADD, TRADD, and caspase-8, thereby forming complex II. Active caspase-8 cleaves downstream caspase-3/7 and RIPK1, inducing cell apoptosis while simultaneously inhibiting necroptosis (43)."
38576612
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"Rather than inhibiting RipK1 degradation, knock-down of CYLD and/or A20 appeared to enhance the degradation of RipK1, suggesting that CYLD and A20 promote maintenance of RipK1."
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