University of Massachusetts Medical School Faculty Publications


Uba1 functions in Atg7- and Atg3-independent autophagy

UMMS Affiliation

Department of Cancer Biology

Publication Date


Document Type



Animals; 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 | Animal Experimentation and Research | Cell Biology | Cells | Cellular and Molecular Physiology | Enzymes and Coenzymes | Investigative Techniques


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.

DOI of Published Version



Nat Cell Biol. 2013 Sep;15(9):1067-78. doi: 10.1038/ncb2804. Epub 2013 Jul 21. Link to article on publisher's site

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

Nature cell biology

PubMed ID