IndraLab

Statements

CYLD binds OTULIN. 23 / 24
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"An interaction between HOIP and OTULIN or CYLD seems strange, since their highly specific yet counteracting activities would generate a futile energy consuming circle."
26503766
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"Suppression of LUBAC-mediated linear ubiquitination by a specific interaction between LUBAC and the deubiquitinases CYLD and OTULIN."
24461064
sparser
"Thus, CYLD and TAP-tagged OTULIN do not form part of the same individual LUBAC complexes, implying that they indeed cannot simultaneously interact with an individual HOIP protein."
26670046
sparser
"Furthermore, we identified the endogenous association of CYLD and OTULIN with LUBAC and the CBM complex by the immunoprecipitation with anti-MALT1 antibody ( xref )."
33329596
sparser
"As described in §4, both OTULIN and CYLD form a complex with the HOIP-PUB domain and this interaction is important for the negative regulation of the NF-κB signalling pathway [ xref ]."
28446710
sparser
"Interestingly, after caspase-mediated cleavage during apoptosis, the N-terminal fragment of HOIP also binds to the DUBs OTULIN and CYLD, which are down-regulators of LUBAC-mediated ubiquitination, providing a further regulatory feedback loop ( xref )."
29686669
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"Given that, LUBAC may form a putative complex which includes both OTULIN and CYLD bound to two HOIP molecules [ xref , xref ]."
33288901
sparser
"The PUB domain of HOIP, in particular, has been shown to be involved in its interaction with the deubiquitinating enzymes, OTULIN or CYLD."
37431163
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"Suppression of LUBAC mediated linear ubiquitination by a specific interaction between LUBAC and the deubiquitinases CYLD and OTULIN."
24461064
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"In addition, a mutant version of HOIP that can neither bind to OTULIN nor CYLD is also less capable of inducing canonical Wnt signaling than wildtype HOIP xref ."
26085216
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"OTULIN and CYLD form mutually exclusive complexes with LUBAC [ xref ]."
32231246
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"It contains an N-terminal region: N-glycanase/Ub-associated domain (UBA) or UBX-containing protein domain for interacting with two crucial deubiquitinases, OTULIN and CYLD, both of which can trim M1-linked Ub chains ( xref xref – xref ), and a B-box–type zinc finger (ZF) followed by a canonical ZF ( xref )."
35294289
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"Furthermore, LUBAC constitutively interacts with the deubiquitinating enzymes (DUBs) OTULIN and CYLD, which cleave linear ubiquitin chains generated by LUBAC."
34685685
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"The interaction of CYLD and OTULIN with HOIP synergistically suppresses LUBAC mediated linear polyubiquitination and NF-kappaB activation."
24461064
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"As described in S4, both OTULIN and CYLD form a complex with the HOIP-PUB domain and this interaction is important for the negative regulation of the NF-kappaB signalling pathway [XREF_BIBR]."
28446710
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"Furthermore, LUBAC constitutively interacts with the deubiquitinating enzymes (DUBs) OTULIN and CYLD, which cleave linear ubiquitin chains generated by LUBAC."
| PMC
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"Mutually Exclusive Binding of CYLD and OTULIN to HOIP Causes CYLD Selective Recruitment to SCs."
26670046
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"Intriguingly, HOIP’s relatively small PUB domain mediates the interaction with both CYLD and OTULIN and even short deletions in this domain abolished interaction with both factors ( xref B–S3D)."
26670046
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"The binding of CYLD and OTULIN to HOIP is mutually exclusive and controls different outcomes [ 39 ]."
34074601
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"Structural comparisons of diUb binding to OTULIN or CYLD reveal that the narrow channel in CYLD, which accommodates the C-terminal tail of distal Ub and thus locates the scissile bond near the active site, may not tolerate introduction of an alanine or Dha at the position G76 ( xref , xref , xref )."
28919039
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"Both CYLD and OTULIN associate with LUBAC via an N-terminal peptide:N-glycanase/UBA- or UBX-containing protein (PUB) domain in the catalytic subunit HOIP ( xref , xref , xref , xref , xref )."
27591049
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"Additionally, we used a HOIP-PUB domain point mutant (N102A), which abolishes the interaction of both OTULIN and CYLD with HOIP."
27545878
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"The above question was answered by the discovery that OTULIN and CYLD interact with LUBAC [ xref – xref ] ( xref ) and further consolidated the role of OTULIN as a bona fide regulator of Met1 signalling."
27913667