Uba1 functions in Atg7- and Atg3-independent autophagy
Chang, Tsun-Kai ; Shravage, Bhupendra V. ; Hayes, Sebastian D. ; Powers, Christine M. ; Simin, Rachel T. ; Wade Harper, J. ; Baehrecke, Eric H.
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UMass Chan Affiliations
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Keywords
Autophagy
Cell Size
Drosophila Proteins
Drosophila melanogaster
Epithelial Cells
Gene Expression Regulation
Intestines
Larva
Organ Specificity
Protein Isoforms
Signal Transduction
Ubiquitin
Ubiquitin-Activating Enzymes
Ubiquitin-Conjugating Enzymes
Ubiquitination
Amino Acids, Peptides, and Proteins
Cell Biology
Cells
Cellular and Molecular Physiology
Enzymes and Coenzymes
Investigative Techniques
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Abstract
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.
Source
Nat Cell Biol. 2013 Sep;15(9):1067-78. doi: 10.1038/ncb2804. Epub 2013 Jul 21. Link to article on publisher's site