IndraLab

Statements

OTULIN binds CYLD. 20 / 21
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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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"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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"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
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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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"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 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
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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
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"Mutually Exclusive Binding of CYLD and OTULIN to HOIP Causes CYLD Selective Recruitment to SCs."
26670046
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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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"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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"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
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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
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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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"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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"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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"OTULIN and CYLD form mutually exclusive complexes with LUBAC [ xref ]."
32231246
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"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, LUBAC constitutively interacts with the deubiquitinating enzymes (DUBs) OTULIN and CYLD, which cleave linear ubiquitin chains generated by LUBAC."
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