IndraLab

Statements

USP53 binds RIPK1. 10 / 10
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"Targeting the USP53–RIPK1 axis could be a potential strategy for the treatment of alcohol-associated myocardial damage."
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"Our work elucidates the pathogenic role of the USP53–RIPK1 signaling axis in EtOH-induced cardiomyopathy, providing a novel molecular target for therapeutic intervention."
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"USP53 interacts with the intermediate domain of RIPK1 via its C-terminal region."
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"Cotransfection of USP53 mutants and HA-tagged RIPK1 in HEK-293T cells showed that both the full length and the C terminus of USP53 could interact with RIPK1, but not the N terminus of USP53, which indicated that the C terminus of USP53 was essential for interacting with RIPK1 (Fig. xref J)."
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"Subsequently, USP53 interacted with the intermediate domain of RIPK1 and removed K63-linked ubiquitination at lysine-377 (K377), facilitating RIPK1 phosphorylation and triggering downstream apoptotic and necroptotic pathways in cardiac cells."
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"USP53 directly binds to RIPK1 and triggers its kinase activity by removing the K63-linked ubiquitin chain at the lysine-377 (K377) site, which in turn drives apoptosis and necroptosis, and exacerbates ACM."
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"However, Co-IP assay revealed that the K377R mutation did not affect the interaction between RIPK1 and USP53 (Fig. xref G)."
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"These results highlight the USP53–RIPK1 signaling axis as a potential therapeutic target for mitigating ACM progression."
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"These findings revealed the critical role of USP53–RIPK1 interaction in driving alcoholic CM injury and ACM."
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"Mechanistically, USP53 directly interacts with RIPK1 and activates RIPK1 kinase activity by disrupting K63-linked ubiquitination at K377, the major K63 ubiquitination site in human RIPK1 [ xref ]."
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