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CYLD deubiquitinates RIPK1. 111 / 112
1 | 111
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"RIPK1 is then de-ubiquitinated by the enzymes Cezanne and CYLD, and the complex of TRADD and RIPK1 moves to the cytosol as Complex II."
21981915
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"53 Finally, caspase-8 also cleaves the deubiquitylase CYLD (cylindromatosis), which is required to deubiquitylate and activate RIPK1 mediated necroptosis in response to TNF, 54 thus potentially providing an alternative or additional mechanism for silencing necroptosis."
28197335
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"Contributing to the " death signal ", CYLD deubiquitylates TRAF2 and RIPK1, allowing the formation of the ripoptosome."
| PMC
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"CYLD, a K63-specific deubiquitinating enzyme (DUB) critical for the activation of necroptosis [28] , mediates the deubiquitination of RIP1 to facilitate the formation of complex IIb in necroptosis [29[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
25087983
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"The suppression of CYLD by overexpression of LEF-1 stimulates sustained ubiquitination of RIPK1, causing the defection of necroptosis and survival of CLL cells."
32764983
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"TNFR1 activation with no integration of c-IAPs (e.g. with the treatment of IAP antagonists), or with inhibition of translation, or with deubiquitination of RIPK1 by the deubiquitinating enzyme CYLD may induce RIPK1 translocation to a secondary complex in the cytoplasm called complex II [XREF_BIBR - XREF_BIBR]."
29587748
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"In complex I, a cellular inhibitor of apoptosis proteins (cIAPs) keep Receptor Interacting Serine/Threonine Kinase 1 (RIPK1) ubiquitinated,245 while CYLD deubiquitinates RIPK1 and converts complex I to complex II."
37415620
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"As the deubiquitination of RIP1 by CYLD, a major deubiquitinase in the NF-kappaB pathway that functions by hydrolysing K63 and linear ubiquitin chains XREF_BIBR, is a key step to induce complex II formation XREF_BIBR and OPTN associates with CYLD XREF_BIBR, defects in CYLD deubiquitination activity, due to the absence of OPTN, may result in enhanced complex II formation."
27552911
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"XREF_BIBR, XREF_BIBR, XREF_BIBR, XREF_BIBR Deubiquitination of RIPK1 by CYLD 81 stimulates the dissociation of Complex I into a secondary cytoplasmic Complex IIa where RIPK1 and/or TRADD recruit FADD via their DDs."
26313917
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"On the other hand, RIPK1 can be deubiquitinated by cylindromatosis (CYLD), leading to the suppression of the NF-κB pathway and instead, activation of cell death pathways."
36077828
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"Deubiquitination of RIP1 by CYLD triggers the disassociation of RIP1from TNFR1 and the subsequent formation of Complex II, which is comprised of FADD, RIP1, and caspase-8, leading to caspase-8 activation and apoptosis [XREF_BIBR]."
27154074
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"Deubiquitination of RIP1 by CYLD in the necrosome was also suggested to facilitate necroptosis [XREF_BIBR]."
33432113
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"However, untrammeled CYLD activity can lead to deubiquitination of RIPK1 and recruitment and activation of RIPK3 as a consequence ( O’Donnell et al., 2011 )."
28306512
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"This process leads to de-ubiquitination of receptor interacting protein kinase 1 (RIPK1) by the de-ubiquitination enzyme CYLD (170)."
38274789
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"When RIPK1 is not ubiquitinated, complex IIb is formed; in order for this to occur, the cylindromatosis tumour suppressor protein DUB (CYLD) enzyme deubiquitinates RIPK1, thereby allowing it to disassociate from complex I 42 and form complex IIb, whereby TRADD is replaced by RIPK3, upon degradation of cIAP1 and 2 XREF_BIBR, XREF_BIBR, XREF_BIBR."
30755793
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"Indeed, RIP1 polyubiquitination leads to NF-kappaB activation and promotes cell survival, whereas deubiquitination of RIP1 by CYLD promotes the assembly of the cytosolic complex termed Ripoptosome, which leads to cell death."
22435549
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"However, in apoptosis, the ubiquitination of RIPK1 can be reversed by cylindromatosis (CYLD), hence excluding the intervention of TAK1, and triggers cell death through caspase-8 independently of the kinase activity of RIPK1 [58,59]."
37895022
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"CYLD promotes necroptosis by facilitating RIPK1 deubiquitination at the TNFR1 membrane receptor complex [100] ."
25736836
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"The Lys 63 linked polyubiquitination of RIP1 or TRAF2 by cIAPs induces the translocation of NF-kappaB into the nucleus to induce the transcription of A20 and cylindromatosis (CYLD), which can both deubiquitinate RIP1."
33628745
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"CYLD, a K63 specific deubiquitinating enzyme, also mediates the deubiquitination of RIP1 to facilitate the formation of complex IIb, which is RIP1/RIP3/MLKL necrosome."
33064829
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"Once bound to RIP1, OPTN directly interacted with cylindromatosis (CYLD) to mediate deubiquitination of RIP1 by CYLD and thereby blocked downstream of NF-κB signaling pathway (19)."
30519240
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"When RIP1 is deubiquitinated by the deubiquitinase cylindromatosis (CYLD), the NF-κB pathway is constrained, leading to the formation of complex II consisting of RIP1, TRADD, caspase 8, and FAS-associated death domain protein (FADD) [50, 52]."
40064873
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"CYLD, a deubiquitinating enzyme that targets both M1- and K63 linked ubiquitin chains, is recruited to TNF-RSC to negatively regulate ubiquitinations of RIPK1, TNFR1, NEMO and TRADD to attenuate the NF-kappaB pathway and promote both apoptosis and necroptosis."
27984721
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"The deubiquitination of RIPK1 by CYLD is critical for the activation of necroptosis and complex II formation [16]."
31752870
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"We found that overexpression of HOIP in 293T cells increased the M1 ubiquitination of RIPK1, while overexpression of SPATA2 or CYLD limited the M1 ubiquitination of RIPK1 (Fig. 4D–F)."
28701375
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"Moreover, Bcl-3-induced RIP1 deubiquitination can be largely rescued by KO of CYLD (Fig. 7E) and the loss of Bcl-3 similarly suppressed the deubiquitination activity of CYLD (Fig. 7F)."
34853447
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"CYLD also promotes cell death through apoptosis and necrosis [XREF_BIBR, XREF_BIBR], possibly by inhibiting RIP1 ubiquitination or removing ubiquitin chains from RIP1."
23312890
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"RIP1 deubiquitination by CYLD promotes caspase-8 activation."
24577083
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"Increased Bcl-3 might promote TNF-induced apoptosis in hepatocytes after challenge with the liver injury risk factors by facilitating the deubiquitination of RIP1 mediated by CYLD."
34853447
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"When the activities of cIAPs, TAK1, and NEMO are blocked (IAPs inhibitor therapy), the deubiquitinases cylindromatosis (CYLD) and A20 are activated, resulting in the deubiquitination of RIPK1 and form[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
37196683
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"Since CYLD is less efficient at deubiquitinating RIP1, this results in a much lower overall rate of RIP1 deubiquitination and a significant increase in TTD, i.e., CYLD, counterintuitively, inhibits necroptosis in this mode."
36710493
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"Furthermore, despite the results of in silico KO experiments that show RIP1 deubiquitination in mode 4 is driven exclusively by CYLD (Fig. 3 D), we do not see a sensitivity in TTD to variations in CYLD concentration, even for a 70% KD (Fig. 5, bottom row)."
36710493
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"With this in mind, numerous published experimental studies in mammalian cells (human and mouse) have shown that RIP1 deubiquitination in complex I is driven by A20, CYLD, or both, depending on cell type."
36710493
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"Moreover, Moquin et al. (11) reported that RIP1 deubiquitination in MEFs is mediated by CYLD, but proposed that it occurs in the necrosome rather than complex I, since KD of CYLD had no effect on RIP1 deubiquitination."
36710493
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"Similarly, Liu et al. (66) showed in hippocampal neurons that KD of CYLD blocks necroptosis and Wright et al. (20) showed that CYLD deubiquitinates RIP1 in human cervical adenocarcinoma (HCAC) cells.To reconcile these contrasting reports, we have associated with each of the above experimental studies one or more modes of necroptosis execution identified from our model analysis (Table 3)."
36710493
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"If inhibition of cIAP in concert with deubiquitination of RIPK1 by cylindromatosis protein (CYLD) triumphs or if RIPK3 is absent or present at a low level, RIPK1 dislodges from complex I and forms a c[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
34838807
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"In one case, A20 and CYLD both contribute to RIP1 deubiquitination, in another RIP1 deubiquitination is driven exclusively by CYLD, and in two modes either A20 or CYLD acts as the driver with the other enzyme, counterintuitively, inhibiting necroptosis."
36710493
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"However, CYLD- and A20-driven deubiquitination of RIP1 have been variously reported as pro- and antinecroptotic in different cell types: some studies have shown that CYLD drives RIP1 deubiquitination (11,17,19,20), while others have implicated A20 (13,21,22) or reported equal contributions from both enzymes (23,24,25)."
36710493
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"Then, a tumor suppressor cylindromatosis (CYLD) protein promotes the deubiquitination of RIP1 in either complex I or complex II."
28789335
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"In one case, A20 and CYLD contribute approximately equally to RIP1 deubiquitination, such that both must be knocked out to delay necroptosis induction (knocking out one has no effect, since the signal can be rerouted through the other)."
36710493
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"Taken together, these results indicate that selenite triggered upregulation of CYLD transcription induced RIP1 deubiquitination and apoptosis."
24577083
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"In another, RIP1 deubiquitination is driven exclusively by CYLD, with A20 being effectively inactive."
36710493
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"TNFα combines with TNFR1 to initiate the assembly of complex I. RIPK1 is deubiquitinated by CYLD or is incapable of undergoing ubiquitination with pharmacological or genetic inhibition of cIAP1/2."
38164133
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"RIPK-1 is deubiquitinated by cylindromatotis deubiquitinase (CYLD) to form the Complex II, composed by TRADD, FADD, RIPK1, and caspase 8. Function of caspase 8 is inhibited by the interaction of RIPK3[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
29410006
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"For example, TNFAIP3, CYLD, USP3, USP4, USP15, USP25, and OTUD5 deubiquitinate key components of the IFN production pathway, including RIG-I, TRAF2, TRAF3, TRAF6, RIP1, and TRIF (reviewed in [93,94])."
38716888
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"The deubiquitination of RIP1 by CYLD leads to the formation of complex II, including the TRADD, FASassociated protein with a death domain (FADD), caspase-8, and RIP3, which activate caspase-8 and induce apoptosis."
26149913
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"CYLD Deubiquitinates RIP1 in the TNFalpha Induced Necrosome to Facilitate Kinase Activation and Programmed Necrosis."
24098568
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"Importantly, CYLD physically interacts with and inhibits the ubiquitination of receptor-interacting protein 1 (RIP1), a key upstream signaling molecule involved in the ubiquitin-dependent activation o[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
17981138
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"Importantly, CYLD physically interacts with and inhibits the ubiquitination of receptor-interacting protein 1 (RIP1), a key upstream signaling molecule involved in the ubiquitin-dependent activation o[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
17981138
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"We reveal that CYLD deubiquitinates RIP1 to facilitate TNF induced necrosis."
24098568
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"We show that CYLD does not promote RIP1 deubiquitination within the membrane associated TNFR-1 complex."
24098568
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"Moreover, the inducible ubiquitination of RIP1 was blocked by CYLD ( Figure S6 D)."
17981138
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"The potent activity of CYLD in suppressing RIP1 ubiquitination under both transfected and endogenous conditions suggests the intriguing possibility that RIP1 may be a target of CYLD."
17981138
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"Deubiquitination of RIP1 by CYLD facilitates programmed necrosis."
24098568
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"However, when RIPK1 is deubiquitinated by cylindromatosis (CYLD), the NF-κB pathway is suppressed, forming the complex II consisting of RIPK1, TRADD, caspase-8, and FADD."
37313458
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"In the course of complex II formation, RIP1 deubiquitination by CYLD, a deubiquitinase that cleaves linear- and K63-ubiquitin chains, plays a crucial role."
33815386
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"CYLD can deubiquitinate RIPK1, freeing it to be phosphorylated and complex with RIPK3 (Complex IIb) to form the necrosome [XREF_BIBR - XREF_BIBR]."
25342597
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"When not cleaved by the caspase-8-cFLIP L heterodimer, CYLD promotes the deubiquitination of RIP1, enabling its association with RIP3 to mediate necroptosis."
23069594
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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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"Cyld can deubiquitylate RIPK1 and facilitate TNF-induced necroptosis, which can be cleaved by caspase 8 ."
30442927
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"CYLD acts as a negative regulator of necroptosis by deubiquitinating RIPK1 and RIPK3, thereby preventing their activation."
37719475
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"Necroptosis can be initiated by activation of Toll like receptors (TLR) 3 and 4, TNF-alpha receptor 1 or, as more recently shown by us and others, by cylindromatosis (CYLD)-mediated deubiquitination of RIPK1 [XREF_BIBR]."
| PMC
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"But the degradation of cIAP1/2 would promotes the deubiquitination of RIPK1 by deubiquitinase cylindromatosis (CYLD) releases RIPK1 from this complex and results in the interaction of RIPK1 with FADD (Fas‐associated death domain protein), RIPK3, and Caspase 8 to form a cytosolic protein complex (Complex II), leading to the activation of Caspase 8. 7 , 8 Activated Caspase 8 can cleave and activate the executor caspases such as Caspase 3 and Caspase 7."
34796721
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"After receiving the “death signal”, receptor-interacting protein kinase 1 (RIPK1) can be deubiquitinated by cylindromatosis (CYLD) and leads to recruitment of RIPK3 to form a complex and phosphorylate mixed-lineage kinase domain-like (MLKL)."
39061897
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"Lys 63 linked polyubiquitination of RIP1 or TRAF2 by cIAPs results in NF-kappaB translocation into nucleus to induce transcription of its target genes including A20 and cylindromatosis (CYLD), both of which can deubiquitinate RIP1."
24938416
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"At the same time, RIP1 can also be deubiquitinated by CYLD, the NF-κB pathway is restricted, and the trend toward cell death pathway."
34381023
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"Taken together, the computational analysis helped to resolve the controversy in experimental observations by showing that CYLD- and A20-driven deubiquitination of RIP1 may act as pro- and anti-necroptotic in different cell types."
37420422
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"Upon deubiquitination of RIP1 by cylindromatosis (CYLD) or inhibition by cIAP proteins, the complex I converts to the complex II, containing RIP1, FADD, caspase-8 and TRADD, which inhibits NF-κB activ[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
28065786
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"Conversely, deubiquitination of RIP1 by CYLD or the absence of cIAPs and LUBAC renders complex I unstable and facilitates other complexes assembled to initiate apoptosis or necroptosis."
26938298
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"In this context, RIP1 is deubiquitinated by enzymes such as Cezanne [36] and CYLD [37] ."
24780723
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"TNFR1 activation together with the absence of c-IAPs (IAP antagonist treatment), translation inhibition (cyclohexamide treatment), or RIP1 deubiquitination by the deubiquitinating enzyme (DUB) CYLD may promote the translocation of RIP1 to a secondary cytoplasmatic complex, Complex II [XREF_BIBR - XREF_BIBR]."
26045969
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"Deubiquitination of RIPK1 by CYLD promotes the recruitment of multiple proteins, including FADD (Fas-associated via death domain), Caspase-8, and receptor-interacting protein kinase 3 (RIPK3), by RIPK1 [4, 5]."
38331847
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"Deubiquitylation of RIPK1 by CYLD can promote the assembly of complex IIa and complex IIb."
40301325
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"CYLD deubiquitylates RIPK1, promoting necrosome assembly [18]."
40301325
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"Deubiquitination of E3 ubiquitin ligase, deletion of LUBAC, or deubiquitination of RIP1 by CYLD in complex I leads to the restriction of NF-κB activation, which promotes the formation of complex IIa and activates caspase-8-dependent apoptosis [22, 30, 33]."
40301325
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"When the deubiquitinase CYLD deubiquitinates RIPK1, it results in a reduction in the stability of multimeric complex I."
38249488
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"In the setting of caspase-8 deficiency or inactivation, cylindromatosis (CYLD), an enzyme that is normally deactivated by caspase-8, mediates a de-ubiquitination of RIPK1."
32470461
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"[XREF_BIBR] CYLD deubiquitination of TRAF6, RIP1, and NF-kappaB-essential modulator (NEMO) leads to inactivation of NF-kappaB signaling."
25025000
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"Additionally, CYLD, which deubiquitinates RIPK1 and favours the formation of the complex II/RIPoptosome, has also been proposed as a caspase-8 substrate to block necroptosis [10–12]."
38514849
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"It is well established that CYLD interacts with TRAF2, causing deubiquitination of both TRAF2 and RIP1 44,47–50 and that activation of CYLD can block NF-κB activation induced by TNF-α stimulation."
16936264
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"This process starts with the accelerated degradation of cIAP1/2 induced by Smac protein (or Smac mimetics), and proceeds with release of RIPK1 from the TNFRI, deubiquitination of RIPK1 by the deubiqui[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
19524512
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"Thus, apoptosis and necrosis induced by death inducing cytokines share a common biochemical pathway down to the step of RIPK1 activation following receptor activation, cIAP1/2 degradation, and deubiqu[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
19524512
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"However, when RIPK1 is dysfunctional in its ubiquitination or de-ubiquitinated by CYLD, RIPK1 forms a complex with RIPK3 and further activates downstream MLKL, which induces necrotic apoptosis, leading to DAMP release, exacerbating the inflammatory response (38)."
39720715
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"Furthermore, CYLD catalyses deubiquitination of RIPK1, which consequently dissociates from the TNFR1 complex and is released into the cytosol in order to form a complex with fas-associated protein with death domain (FADD) and Casp8 to promote cell death.6 7 RIPK1 protein expression was increased in the absence of FMRP following exposure to TNF when compared with controls (figure 5G)."
31409605
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"If RIPK1 is deubiquitinated by the DUB cylindromatosis (CYLD), which limits sustained activation of NF-κB signaling and leads to a tendency to form complex II [55]."
36551253
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"The resulting CYLD activation would result in further deubiquitination of RIPK1 and reduction in IKK activity."
32024820
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"CYLD depletion by siRNA prevented RIP1 deubiquitination, formation of the RIP1/RIP3 complex, and cell death."
29352268
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"These findings indicated that CYLD regulated RIP1/RIP3–necrosome formation in glutamate-induced oxytosis via the deubiquitination of RIP1."
29352268
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"However, we detected increased RIP1 ubiquitination following CYLD depletion in HT-22 cells exposed to glutamate, indicating that under oxidative stress, CYLD regulates RIP1 ubiquitination leading to RIP1/RIP3 complex formation."
29352268
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"Conversely, disrupting CYLD phosphorylation using IKK inhibitors reactivates CYLD, which in turn, deubiquitinates and switches RIPK1 into a death-signaling molecule (Fig. 8b)."
32024820
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"The cellular IAP ligases (cIAP1, cIAP2) are thought to mediate RIP1 ubiquitination, and the deubiquitinating enzyme CYLD restricts RIP1 ubiquitination."
26085203
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"Cylindromatosis tumor suppressor protein (CYLD) then deubiquitylates RIPK1 which allows this protein to leave Complex I and leads to association of FADD and RIPK3 (i.e., Complex II)."
35295146
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"TNFR1 endocytosis, cIAP1/2 inhibition, and RIPK1 deubiquitylation by CYLD triggers formation of cytosolic Complex II, which involves dissociation of TRAF2/5 and cIAP1/2 and association of FADD and pro-caspase-8 as previously described (Newton and Manning, 2016; Su et al., 2016)."
35295146
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"However, when caspase 8 is insufficiently activated, CYLD remains active for and de-ubiquitinates RIPK1, destabilizing complex I."
38135855
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"Inhibition of cIAP1/2 and/or deubiquitylation of RIPK1 by CYLD (not shown) induces formation of cytosolic Complex II, which consists of RIPK1, RIPK3, FADD, and pro-caspase-8 oligomers that proteolytically activate themselves."
35295146
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"Under these conditions, RIP1 can be deubiquitinated by CYLD [67] and so, recruited with RIP3 kinase into another molecular complex in which TRADD, FADD and procaspase-8 are also included."
22374304
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"As soon as the TNF family initiate the necroptosis process, RIP1 will be deubiquitinated by CYLD gene thus trigger the formation of complex IIa that composed of caspase 8, RIP1 and FADD."
38726321
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"RIPK1 ubiquitylation can be restricted by cIAP inhibition or by the deubiquitylase activity of CYLD, which is recruited to the complex-I through the LUBAC binding protein SPATA2 XREF_BIBR - XREF_BIBR."
29449584
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"The conversion of the membrane-associated complex I to the cytoplasmic complex II is mediated by the following: deubiquitylation of RIP1 by the deubiquitin enzyme CYLD; cIAPI/II degradation, which is [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
22265414
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"In contrast, CYLD deubiquitinates RIP1 and promotes the packaging of Complexes IIa and IIb."
26915291
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"cIAP1/2 are required for TNF induced K63 linked ubiquitination of RIP1, which functions to inhibit TNF induced apoptosis, whereas RIP1 deubiquitination by CYLD facilitates its direct interaction with caspase-8 and initiation of cell death."
21282461
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"Consistent with the ubiquitylation status of RIPK1 influencing cell survival, compromised IAP or LUBAC activity, or deubiquitylation of RIPK1 by cylindromatosis (CYLD), favors complex II assembly [26,[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
25662614
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"RIPK1 is deubiquitinated by the deubiquitinase cylindromatosis (CYLD), which subsequently limits the sustained activation of NF-κB signaling [13] and leads to a tendency toward the activation of cell death pathways."
36494757
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"Does CYLD require ubiquitin binding adaptors to inhibit RIP1 ubiquitination?"
21119682
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"Deubiquitination of RIPK1 by CYLD inhibits NF-κB signalling and promotes the RIPK1-mediated engagement and activation of caspase-8, which triggers apoptosis (Fig. 4)."
37387450
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"However, if caspases are inhibited, CYLD deubiquitination of RIPK1 enables its interaction with RIPK3 and MLKL to form the necrosome and trigger necroptosis (Moquin et al., 2013; Vanlangenakker et al., 2011) (Fig. 4)."
37387450
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"CYLD can also mediate TNFα-induced necroptosis by deubiquitinating RIPK1 and facilitating the interaction between RIPK1 and RIPK3 ( Hitomi et al., 2008; Moquin et al., 2013 )."
27865894
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"In the presence of Smac mimetic, cIAP1/2 are degraded and this process promotes the deubiquitination of RIPK1 by CYLD."
32411707
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"Indeed, knocking down CYLD with a siRNA oligo decreased the TNF-alpha plus Smac mimetic induced apoptosis, as well as caspase-8 activating complex formation, confirming that deubiquitination of RIPK1 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
18485876
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"The requirement of CYLD in forming RIPK1 dependent caspase-8 complex indicates that deubiquitination of RIPK1 by CYLD is an essential step in this process."
18485876
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"32 Last but not least, CYLD interacts with and deubiquitinates RIP1."
27383048