IndraLab

Statements

RIPK2 binds OTUD1. 12 / 12
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"Strikingly, our findings revealed that OTUD1 interacted with RIP2 through the kinase domain or CARD domain and removed its K63-linked polyubiquitin chains, resulting in the inhibition of RIP2-induced NF-κB activation in cerebral ischemic lesion."
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"Overall, our study proposed a model for OTUD1–RIP2 interaction and function in cerebral ischemia."
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"Immunoprecipitation and confocal microscopy were used to study the interaction of RIP2 and OTUD1."
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"Mechanistically, OTUD1 interacted with RIP2 and sequentially removed the K63-linked polyubiquitin chains of RIP2, thereby inhibiting NF-κB activation."
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"OTUD1 interacted with RIP2."
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"Given the OTUD1 and RIP2 protein expression were both elevated and localized in microglia and astrocytes of mice with cerebral ischemia, we hypothesize that OTUD1 interacted with RIP2, thus regulate the ubiquitination of RIP2."
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"The endogenous interaction between OTUD1 and RIP2 was determined by Co-IP and immunofluorescence in BV2 cells subjected to OGD/R injury."
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"To dig out the necessary domains of RIP2 interaction with OTUD1, a series of truncated mutants of RIP2 were transfected for Co-IP experiments."
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"Immunoprecipitation and confocal microscopy were used to study the interaction of RIP2 and OTUD1."
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"The endogenous interaction between OTUD1 and RIP2 was determined by Co-IP and immunofluorescence in BV2 cells subjected to OGD/R injury."
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"Intriguingly, we provided direct evidence that OTUD1 interacted with RIP2 and cleaved its K63-linked polyubiquitin chains, rather than the K48-linked chains, which led to suppression of the RIP2-induced inflammatory response."
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"These results implied the importance of OTUD1–RIP2 in mediating inflammation in ischemic stroke pathogenesis."
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