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MYD88 binds OTUD4. 20 / 20
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"Consequently, we speculated that the interaction between SPARC and OTUD4 may inhibit the binding of MYD88 to OTUD4, thereby activating the MYD88‐dependent signal transduction."
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"This suggests that SPARC can competitively bind to OTUD4, effectively obstructing the interaction between MYD88 and OTUD4."
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"BCA2 enhances the interaction between myeloid differentiation primary response protein 88 (MyD88) and Toll-like receptor 4 (TLR4) and inhibits the interaction of MyD88 with deubiquitinase OTUD4 in the LPS-mediated NF-κB signaling pathway."
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"Furthermore, BCA2 positively regulates LPS-induced NF-κB signaling activation by augmenting the interaction between MyD88 and TLR4 while hindering the interaction between MyD88 and OTUD4."
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"Furthermore, BCA2 positively regulates LPS-induced NF-κB signaling activation by augmenting the interaction between MyD88 and TLR4 while hindering the interaction between MyD88 and OTUD4."
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"BCA2 inhibits the interaction between MyD88 and OTUD4 and increases MyD88 ubiquitination."
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"We speculated that BCA2 prevents the binding of OTUD4 to MyD88."
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"Indeed, endogenous immunoprecipitation experiments following BCA2 knockout showed an increased interaction between MyD88 and OTUD4 (Fig. xref B)."
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"We speculated that BCA2 prevents the binding of OTUD4 to MyD88."
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"BCA2 inhibits the interaction between MyD88 and OTUD4 and increases MyD88 ubiquitination."
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"Indeed, endogenous immunoprecipitation experiments following BCA2 knockout showed an increased interaction between MyD88 and OTUD4 (Fig. 5B)."
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"These findings suggested that BCA2 prevents the binding of OTUD4 to MyD88, which in turn, increases the ubiquitination of MyD88, independent of its E3 ligase enzymatic activity."
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"We confirmed the interaction of OTUD4 with MyD88 by immunoprecipitation (IP) of Flag-tagged MyD88, along with HA-tagged OTUD4 co-expressed in HEK293 cells ( xref )."
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"Immunoprecipitation of OTUD4 from mouse embryonic fibroblast (MEF) cell extracts demonstrated the interaction between OTUD4 and MyD88, suggesting that this interaction exists at the endogenous level ( xref )."
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"On the other hand, the amount of MyD88 associated with OTUD4 appeared minimally changed under the same conditions ( xref )."
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"Consequently, we speculated that the interaction between SPARC and OTUD4 may inhibit the binding of MYD88 to OTUD4, thereby activating the MYD88‐dependent signal transduction."
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"This suggests that SPARC can competitively bind to OTUD4, effectively obstructing the interaction between MYD88 and OTUD4."
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"Mechanistically, we discovered that SPARC competitively binds OTUD4 with MYD88, leading to the translocation of P65 from cytoplasm to nucleus and activation of the P65‐MLCK/MLC2 pathway, ultimately disrupting barrier integrity."
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"Taken together, these results demonstrated that OTUD4 associates directly with MyD88."
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"These findings suggested that BCA2 prevents the binding of OTUD4 to MyD88, which in turn, increases the ubiquitination of MyD88, independent of its E3 ligase enzymatic activity."
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