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CYLD inhibits RIPK1. 12 / 13
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"In support, overexpression of Snail1 reduced CYLD expression and upregulated RIP1 in Mel-CV."
29880840
eidos
"This was demonstrated by the findings that knockdown of CYLD resulted in upregulation of RIPK1 that was associated with enhancement in K63-linked polyubiquitination of the protein and that co-knockdown of RIPK1 diminished CYLD knockdown-induced apoptosis in sensitive cells ."
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"Formation of the secondary, receptor-free cytoplasmic complex II is largely dependent on the activity of DUBs, specifically cylindromatosis (CYLD), A20 (also known as TNFAIP3) and ubiquitin thioesterase OTULIN, which destabilize complex I, abrogate NF-kappaB activation and release RIPK1 from complex I, which then forms the cytosolic complex II XREF_BIBR, XREF_BIBR."
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"Thus, CYLD inhibits MyD88, RIP1 (receptor interacting serine/threonine protein kinase 1), TRAF2, TRAF6, TRAF7 and NEMO downstream to TLR signaling and regulates exaggerated inflammation which can lead to the development of severe infection causing sepsis and associated organ damage."
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"We now report that phosphorylation of CYLD by IKK family kinases in HTLV-1 transformed T cells inhibits RIPK1 from activating the cell death pathway and inhibiting these kinases reactivates CYLD and RIPK1-dependent tumor cell death."
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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."
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"Caspase-8 also targets the deubquitinase CYLD preventing RIPK1 initiation of necroptosis [XREF_BIBR, XREF_BIBR]."
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"Silencing of CYLD caused upregulation of RIPK1 in Mel-CV, ME1007, Mel-FH, and ME4405 cells regardless of their differential apoptotic responses (XREF_FIG)."
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"Our observations suggest that in cells transformed by HTLV-1, TAX induces the phosphorylation of CYLD to keep it inactive in order to prevent RIPK1 from inducing cell death."
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"This was demonstrated by the findings that knockdown of CYLD resulted in upregulation of RIPK1 that was associated with enhancement in K63 linked polyubiquitination of the protein and that co-knockdown of RIPK1 diminished CYLD knockdown induced apoptosis in sensitive cells."
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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."
29789521
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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 ( Fig. 4C ) , substantiating that downregulation of RIPK1 expression by CYLD is mediated by the proteasomal degradation20 ,30,32,33 ."
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