Matches in SemOpenAlex for { <https://semopenalex.org/work/W3036585903> ?p ?o ?g. }
- W3036585903 abstract "Damaged mitochondria are selectively eliminated in a process called mitophagy. Parkin and PINK1, proteins mutated in Parkinson’s disease, amplify ubiquitin signals on damaged mitochondria with the subsequent activation of autophagic machinery. Autophagy adaptors are thought to link ubiquitinated mitochondria and autophagy through ATG8 protein binding. Here, we establish methods for inducing mitophagy by mitochondria-targeted ubiquitin chains and chemical-induced mitochondrial ubiquitination. Using these tools, we reveal that the ubiquitin signal is sufficient for mitophagy and that PINK1 and Parkin are unnecessary for autophagy activation per se. Furthermore, using phase-separated fluorescent foci, we show that the critical autophagy adaptor OPTN forms a complex with ATG9A vesicles. Disruption of OPTN–ATG9A interactions does not induce mitophagy. Therefore, in addition to binding ATG8 proteins, the critical autophagy adaptors also bind the autophagy core units that contribute to the formation of multivalent interactions in the de novo synthesis of autophagosomal membranes near ubiquitinated mitochondria." @default.
- W3036585903 created "2020-06-25" @default.
- W3036585903 creator A5019548450 @default.
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- W3036585903 date "2020-06-17" @default.
- W3036585903 modified "2023-10-14" @default.
- W3036585903 title "Critical role of mitochondrial ubiquitination and the OPTN–ATG9A axis in mitophagy" @default.
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- W3036585903 doi "https://doi.org/10.1083/jcb.201912144" @default.
- W3036585903 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7480101" @default.
- W3036585903 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32556086" @default.
- W3036585903 hasPublicationYear "2020" @default.
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