IndraLab

Statements

TNFAIP3 binds CYLD and TRAF6. 7 / 7
| 7
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"In this regard, here we provide evidence that the adaptor protein TRIP6 (thyroid hormone receptor-interacting protein 6), a specific interacting protein of the LPA2 receptor but not other LPA receptors, recruits TRAF6 to the LPA2 receptor and enhances the E3 ligase activity of TRAF6 by antagonizing the association of A20 and CYLD to TRAF6."
27134758
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"Overexpression of TRIP6 interferes with the recruitment of A20 to TRAF6, whereas depletion of TRIP6 enhances the association of TRAF6 with A20 and CYLD, and eliminates LPA-promoted K63-linked polyubiquitination of TRAF6."
27134758
sparser
"To address this issue, we expressed FLAG-TRAF6 in HEK293T cells and treated cells with LPA for various times to determine how TRAF6 associates with deubiquitinase A20 or CYLD."
27134758
sparser
"On the other hand, in ovarian cancer cells and glioblastoma cells that show persistent NF-κB activity and high levels of TRIP6, both A20 and CYLD bind to TRAF6 very weakly."
27134758
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"Nonetheless, depletion of TRIP6 can significantly enhance the association of A20 or CYLD with TRAF6 in ovarian cancer cells and promote the binding of A20 to TRAF6 in glioblastoma cells, suggesting that targeting TRIP6 may prove to be an effective strategy to restore the function of A20 and CYLD in restricting the NF-κB activity in these cancer cells."
27134758
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"Nonetheless, depletion of TRIP6 by either shRNA ( xref ) or Cas9/sgRNA ( xref ) not only enhanced the association of TRAF6 with A20, but also with CYLD in untreated and treated cells, suggesting a significant role for TRIP6 in antagonizing the binding of TRAF6 to both A20 and CYLD in ovarian cancer cells."
27134758
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"In contrast, depletion of TRIP6 by TRIP6-specific shRNA or Cas9/sgRNA greatly enhances the association of TRAF6 with A20 and CYLD, and attenuates lysophosphatidic acid-induced muclear factor-κB and JNK/p38 activation in ovarian cancer cells."
27134758
TNFAIP3 binds CYLD. 6 / 6
| 6
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"IP assay results indicated that the methylated TRAF2 weakened the interaction with A20 or CYLD."
| PMC
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"ITCH is a E3 ubiquitin ligase that has been shown to be part of the A20 and CYLD ubiquitin-editing complexes, aiming at the regulation/termination of NF-κB signaling ( xref )."
37595047
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"In protecting M1-linked chains from degradation, A20 suppresses TNF-induced cell death by stabilising complex I. Antagonising interactions between A20 and CYLD may provide a mechanism for regulating the interplay between complex I and complex II-mediated signalling pathways (Fig. xref )."
38467621
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"Adding just another level of complexity to an already crowded CD137 signalosome, we have recently observed the functional association of K63-DUBs A20 and CYLD to the CD137 signalosome."
30524423
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"Furthermore, A20 and CYLD are recognized for their tumor suppressing functions because deficiency or mutation of A20 or CYLD is associated with lymphoma and familiar cylindromatosis, respectively [ xref – xref ]."
30471562
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"These results suggest that ITCH modulates TRAF6 deubiquitylation by interacting with A20 and CYLD in cardiomyocytes."
39802494
TNFAIP3 binds CYLD and ITCH. 3 / 3
| 3
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"A20 and Cyld can form independent complexes with Itch to disassemble K63 chains and to add K48 polyubiquitination ( xref , xref )."
31515257
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"Both A20 and Cyld can independently associate with Itch and Cyld interacts with Cbl-b to facilitate the removal of K63 polyubiquitin chains and to add K48 polyubiquitination ( xref , xref , xref )."
31515257
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"DUB-E3 interactions are used for mutual ubiquitin-dependent regulation (e.g., to control each other’s stability, see above) or for editing ubiquitin chain architecture on particular substrates (as shown for the hybrid DUB/E3 enzyme A20 and CYLD-ITCH complexes during inflammatory signaling [ xref , xref ])."
33335288
Phosphatase binds PPP2, PP2C, TNFAIP3, and CYLD. 1 / 1
| 1
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"Furthermore, IKKγ has been implicated in interactions with protein phosphatases PP2A and PP2C as well as deubiquitinases A20 and CYLD (Solt & May, xref ; Liu et al ., xref )."
25082354
USP25 binds TNFAIP3, CYLD, carD, and RIGI. 1 / 1
| 1
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"The comparison between the deubiquitinase activities and binding affinities to RIG-I-CARD of USP21, A20, and CYLD indicate that USP21 is a bona fide RIG-I deubiquitinase, since among these three DUBs, USP21 is the only one that has the potential to inhibit RIG-I-CARD polyubiquitination both in vivo and in vitro and co-immunoprecipitates with RIG-I-CARD [ xref ]."
33138315
OTULIN binds CYLD, TNFAIP3, and UBE2L3. 1 / 1
| 1
sparser
"DUBs can directly regulate E2 enzymes, xref which raises the question as to whether OTULIN, CYLD, or A20 interact with UBE2L3."
25640675
TNFAIP3 binds CYLD, TNFRSF9, and TRAF2. 1 / 1
| 1
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"The deubiquitinases A20 and CYLD interact with the 4-1BB and TRAF2 complex and, by regulating the ubiquitination of TRAF2 and TAK1 ( xref ), they decrease 4-1BB activation [ xref ]."
| PMC
NMRAL1 binds TNFAIP3 and CYLD. 1 / 1
| 1
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"Several DUBs, including A20, CYLD and USP7, have been reported to downregulate NF- κ B. Co-IP assays were thus carried out to examine the interactions between these enzymes and HSCARG, and the results showed that HSCARG interacts weakly with A20 or CYLD but strongly interacts with USP7 ( xref , xref )."
24832601
TNFAIP3 binds CYLD and IKK_complex. 1 / 1
| 1
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"In this way, p47 negatively regulates IKKγ/NEMO independently of the other two known regulators of the IKK complex, A20 and CYLD ( xref , xref )."
33869030
RNF31 binds CYLD, OTULIN, TNFAIP3, and MYSM1. 1 / 1
| 1
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"Upon immunoprecipitation, we observed no direct interaction between MYSM1 with HOIP, NEMO or the negative regulators CYLD, OTULIN or A20 (Fig.  xref )."
30405132