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SDC4 binds CYLD. 11 / 14
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"As shown in the co-IP assays ( xref ), CYLD, but not TRIM25, was present in the SDC4 immunoprecipitate, suggesting a strong association of SDC4 with the deubiquitinating enzyme CYLD, rather than the ubiquitin E3 ligase TRIM25."
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"Interestingly, the association between CYLD and SDC4 was significantly enhanced after the cells were infected with Sendai virus (XREF_SUPPLEMENTARY)."
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"Mechanistically, we show that SDC4 interacts with both RIG-I and deubiquitinase CYLD via its carboxyl-terminal intracellular region."
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"Mechanistically, we show that SDC4 interacts with both RIG-I and deubiquitinase CYLD via its carboxyl-terminal intracellular region."
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No evidence text available
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"We provide extensive biochemical evidence to demonstrate that SDC4, via its carboxyl-terminal intracellular domain, interacts with RIG-I and CYLD, thereby facilitating the interaction between RIG-I and CYLD."
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"Of note, our finding that SDC4 strongly interacts with CYLD is very intriguing."
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"As shown in XREF_SUPPLEMENTARY, both the wild-type and catalytically inactive mutant proteins were present in the SDC4 immunoprecipitate, suggesting that the association between SDC4 and CYLD is independent of the enzymatic activity of CYLD."
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"SDC4 interacts with and recruits CYLD to the RIG-I complex."
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"Of note, our finding that SDC4 strongly interacts with CYLD is very intriguing."
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"To test whether SDC4 regulates RIG-I ubiquitination through TRIM25 or CYLD, we first tested whether SDC4 could form a complex with TRIM25 or CYLD."
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