IndraLab

Statements


CYLD inhibits GS26575. 6 / 6
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"Once recruited, CYLD limits NF-kappaB activation by removing K63 linked and M1 linked poly-Ub chains on several components of complex I, including RIPK1 [XREF_BIBR, XREF_BIBR - XREF_BIBR]."

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"CYLD inhibited M1 microglial activation and improved M2 microglial activation after 72 h of reperfusion."

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"We show here that A20 binding to M1 chains in the TNF-RSC stabilizes them, whereas CYLD antagonizes M1 chains in this complex."

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"CYLD, another DUB, is reported to limit NF-kappaB activation by removing K63- and M1 linked poly-ubiquitin chains on several complex I components (including TRAF2, NEMO and RIPK1), thereby disrupting the ubiquitin scaffold required for the recruitment and activation of the TAB2/3-TAK 1 and NEMO-IKKalpha-IKKbeta complexes [XREF_BIBR, XREF_BIBR - XREF_BIBR]."

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"Moreover, in addition to cleaving K63 ubiquitin linkages, CYLD has been shown to degrade M1 linked polyubiquitin chains from various components of the TNF-R1 and NOD2 signalling complexes, including RIP1."

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"Previous studies report that CYLD negatively regulates NF-kappaB signaling by removing K63- and M1 linked polyubiquitin chains from key signaling molecules, including NF-kappaB essential modulator, tumor necrosis factor (TNF)-associated factor (TRAF) 2, TRAF6, and Receptor interacting serine/threonine protein kinase 1, in familial cylindromatosis tumors."