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OTUD1 deubiquitinates PGAM5. 5 / 5
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"METTL3-mediated m6A modification of OTUD1 aggravates press overload induced myocardial hypertrophy by deubiquitinating PGAM5."
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"Mechanistically, OTUD1 facilitated the procession of cardiac hypertrophy by directly binding to and deubiquitinating PGAM5 in a manner dependent on K63 ubiquitin chains, leading to enhanced ASK1 phosphorylation and p38/JNK MAPK signal pathway activation in cardiomyocytes."
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"OTUD1 binds to and deubiquitinates PGAM5."
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"Our findings indicated that the deletion of the OTU domain did not exhibit any pro-hypertrophic effects on the NRVMs (Figure S7), suggesting the critical role of OTU domain in OTUD1-induced cardiac hypertrophy.Given that DUBs play a role in the modulation of biological activities by influencing the degradation or function of substrate proteins, our subsequent investigation aimed to determine whether Otud1 could deubiquitinating pgam5."
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"This upregulated OTUD1 then interacts with and deubiquitinates PGAM5, promoting ASK1 phosphorylation and the activation of the p38/JNK MAPK signaling pathway."
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