Cited by 187Autophagy in Disease and TherapyUbiquitin and proteasome pathwaysGenetics, Aging, and Longevity in Model Organisms

Uba1 functions in Atg7- and Atg3-independent autophagy

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Chang, Tsun-Kai, Shravage, Bhupendra V., Hayes, Sebastian D., Powers, Christine M., Simin, Rachel T., Wade Harper, J., Baehrecke, Eric H.·2013·Nature Cell Biology

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.

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  • In D. melanogaster, autophagy-dependent midgut degradation proceeds independently of Atg7, Atg3, and several other Atg genes required for starvation-induced autophagy in fat body, but relies on Uba1.

    “For example, the autophagy-dependent degradation of the midgut tissue proceeds independently of Atg7, Atg3, and several other Atg genes that are required for starvation-induced autophagy in the fat body, but relies on ubiquitin activating enzyme 1 (Uba1) [837, 838].”
  • In D. melanogaster, molecular machinery of autophagy-dependent cell death and adaptive autophagy exhibit differences.

    “Of note, the molecular machinery of autophagy-dependent cell death and adaptative autophagy exhibit some differences (at least in D. melanogaster) [837, 838].”

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Authors
Chang, T.-K., Shravage, B. V., Hayes, S. D., Powers, C. M., Simin, R. T., Wade Harper, J., & Baehrecke, E. H.
Affiliations
  • University of Massachusetts Chan Medical School (US)
  • Harvard University (US)
Corresponding author
Baehrecke, Eric H.
Venue
Nature Cell Biology
Published
2013-07-21
Volume
15
Issue
9
Pages
1067-1078
ISSN
  • 1465-7392 (ISSN-L)
  • 1476-4679
OpenAlex
W2026860604
Cited by
187
References
40
Citations by year
2026: 8 · 2025: 7 · 2024: 13 · 2023: 11 · 2022: 12 · 2021: 22 · 2020: 15 · 2019: 12 · 2018: 20 · 2017: 10 · 2016: 15 · 2015: 21 · 2014: 18 · 2013: 3
FWCI
13.84
Type
journal article
Language
en
Open access
Locations
  • Nature Cell Biology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
  • Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
  • The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
Funders
  • National Institute of General Medical Sciences (R01GM095567, GM079431, R01GM079431, GM095567)
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK 32520, P30DK032520)
  • National Center for Research Resources (S10RR027897)
Topics
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Keywords
autophagy, UBA1, ATG7, ATG3, E1 ubiquitin-activating enzyme, ATG8, programmed cell death, cell size reduction, midgut development, Drosophila, ubiquitin activation
MeSH terms
Autophagy-Related Protein 7, Animals, Autophagy, Drosophila melanogaster, Epithelial Cells, Gene Expression Regulation, Intestines, Larva, Organ Specificity, Signal Transduction, Protein Isoforms, Ubiquitin, Drosophila Proteins, Ubiquitin-Conjugating Enzymes, Ubiquitin-Activating Enzymes, Cell Size, Ubiquitination

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