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dc.contributor.authorChang, Tsun-Kai
dc.contributor.authorShravage, Bhupendra V.
dc.contributor.authorHayes, Sebastian D.
dc.contributor.authorPowers, Christine M.
dc.contributor.authorSimin, Rachel T.
dc.contributor.authorWade Harper, J.
dc.contributor.authorBaehrecke, Eric H.
dc.date2022-08-11T08:08:30.000
dc.date.accessioned2022-08-23T15:57:31Z
dc.date.available2022-08-23T15:57:31Z
dc.date.issued2013-09-01
dc.date.submitted2014-10-24
dc.identifier.citation<p>Nat Cell Biol. 2013 Sep;15(9):1067-78. doi: 10.1038/ncb2804. Epub 2013 Jul 21. <a href="http://dx.doi.org/10.1038/ncb2804">Link to article on publisher's site</a></p>
dc.identifier.issn1465-7392 (Linking)
dc.identifier.doi10.1038/ncb2804
dc.identifier.pmid23873149
dc.identifier.urihttp://hdl.handle.net/20.500.14038/30218
dc.description.abstractAutophagy is a conserved process that delivers components of the cytoplasm to lysosomes for degradation. The E1 and E2 enzymes encoded by Atg7 and Atg3 are thought to be essential for autophagy involving the ubiquitin-like protein Atg8. Here, we describe an Atg7- and Atg3-independent autophagy pathway that facilitates programmed reduction of cell size during intestine cell death. Although multiple components of the core autophagy pathways, including Atg8, are required for autophagy and cells to shrink in the midgut of the intestine, loss of either Atg7 or Atg3 function does not influence these cellular processes. Rather, Uba1, the E1 enzyme used in ubiquitylation, is required for autophagy and reduction of cell size. Our data reveal that distinct autophagy programs are used by different cells within an animal, and disclose an unappreciated role for ubiquitin activation in autophagy.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=23873149&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3762904
dc.subjectAnimals
dc.subjectAutophagy
dc.subjectCell Size
dc.subjectDrosophila Proteins
dc.subjectDrosophila melanogaster
dc.subjectEpithelial Cells
dc.subjectGene Expression Regulation
dc.subjectIntestines
dc.subjectLarva
dc.subjectOrgan Specificity
dc.subjectProtein Isoforms
dc.subjectSignal Transduction
dc.subjectUbiquitin
dc.subjectUbiquitin-Activating Enzymes
dc.subjectUbiquitin-Conjugating Enzymes
dc.subjectUbiquitination
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectCell Biology
dc.subjectCells
dc.subjectCellular and Molecular Physiology
dc.subjectEnzymes and Coenzymes
dc.subjectInvestigative Techniques
dc.titleUba1 functions in Atg7- and Atg3-independent autophagy
dc.typeJournal Article
dc.source.journaltitleNature cell biology
dc.source.volume15
dc.source.issue9
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/faculty_pubs/467
dc.identifier.contextkey6282123
html.description.abstract<p>Autophagy is a conserved process that delivers components of the cytoplasm to lysosomes for degradation. The E1 and E2 enzymes encoded by Atg7 and Atg3 are thought to be essential for autophagy involving the ubiquitin-like protein Atg8. Here, we describe an Atg7- and Atg3-independent autophagy pathway that facilitates programmed reduction of cell size during intestine cell death. Although multiple components of the core autophagy pathways, including Atg8, are required for autophagy and cells to shrink in the midgut of the intestine, loss of either Atg7 or Atg3 function does not influence these cellular processes. Rather, Uba1, the E1 enzyme used in ubiquitylation, is required for autophagy and reduction of cell size. Our data reveal that distinct autophagy programs are used by different cells within an animal, and disclose an unappreciated role for ubiquitin activation in autophagy.</p>
dc.identifier.submissionpathfaculty_pubs/467
dc.contributor.departmentDepartment of Cancer Biology
dc.source.pages1067-78


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