IndraLab

Statements

OTUD5 leads to the ubiquitination of SYNM. 5 / 5
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"Meanwhile, OTUD5 knockout greatly decreased polyubiquitination of α‐Syn (Figure 3H)."
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"Based on our finding that OTUD5 promoted α‐Syn polyubiquitination independent of its enzymatic activity, we hypothesized that OTUD5 may serve as an adaptor protein to recruit an E3 ligase for K63‐linked polyubiquitination and degradation of α‐Syn."
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"Furthermore, OTUD5 deficiency further attenuated the endogenous K63‐linked polyubiquitination of α‐Syn induced by α‐Syn PFF (Figure 7D)."
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"Particularly, OTUD5 selectively promoted K63‐linked polyubiquitination of α‐Syn and mediated its endolysosomal degradation by recruiting the E3 ligase NEDD4."
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"Mechanically, we found that OTUD5 deficiency further reduced endogenous K63‐linked polyubiquitination of α‐Syn and upregulated its protein level, then promoted the formation of pathologic p‐α‐Syn and aggravated the pathogenic consequences induced by α‐Syn PFF.In summary, we demonstrated that OTUD5 negatively regulated α‐Syn protein levels by promoting endolysosomal degradation independent of its deubiquitinate activity."
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