IndraLab

Statements

CYLD ubiquitinates RIPK1. 11 / 11
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"It regulates NF-kappaB signaling by facilitating deubiquitination of ubiquitinated RIP by CYLD [7,14]."
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"A20 and CYLD block the de-ubiquitination of RIP1 block formation of Complex II and apoptosis."
35602592
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"Mediating the interaction between CYLD and polyUb RIP, optineurin may act as an adaptor protein bringing CYLD and the CYLD substrate RIP together to facilitate deubiquitination of ubiquitinated RIP by CYLD."
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"RIPK1 ubiquitination inhibits RIPK1 kinase activity, and the deubiquitinating enzyme CylD supports necroptosis by deubiquitinating RIP1 XREF_BIBR, XREF_BIBR."
25939025
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"In vitro, downregulation of CYLD increased RIP1 ubiquitination, prevented RIP1 and RIP3 complex formation, and protected neuronal cells from oxidative death."
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"It seems that the ubiquitination of RIP1 protein by CYLD still via apoptosis signaling."
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"The cIAPs can ubiquitinate RIP1, which leads to activation of NF-κB and MAPK pathways to promote cell survival.39 40 Upon cIAP degradation, RIP1 can be de-ubiquitinated by deubiquitinase cylindromatosis (CYLD).41 Upon deubiquitination, Complex IIa forms (Fig. 3), which typically includes RIP1, caspase-8, and FADD.38 42 Formation of this complex can trigger cell death by apoptosis."
36157481
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"Thus an important function of optineurin in the regulation of NF-kappaB signalling is to act as an adaptor protein bringing CYLD and its substrate RIP together to facilitate deubiquitination of ubiquitinated RIP by CYLD."
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"CYLD can inhibit NF-kappaB activity by deubiquitinating and inactivating TRAF2 and TRAF6, RIP, NEMO, and the NF-kappaB co-activator BCL-3."
18718859
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"CYLD deficiency leads to hyperubiquitinated RIPK1 in the necrosome and impaired phosphorylation of RIPK1 and RIPK3, thereby blocking caspase-8 activation."
26491219
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"CpA also impaired the ubiquitination of RIPK1 in response to TNF, and depletion of CYLD partially restored RIPK1 ubiquitination (XREF_FIG B, compare lanes 4 and 8, and XREF_SUPPLEMENTARY B)."
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