ArticleeLife2019
Two distinct mechanisms target the autophagy-related E3 complex to the pre-autophagosomal structure.
Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 71 citations in OpenAlex.
- Establishment of the phagophore-ERES membrane contact site initiates phagophore elongation.Nature structural & molecular biology · 2025Article
- Phase separation promotes Atg8 lipidation and vesicle condensation for autophagy progression.Nature structural & molecular biology · 2025Article
- Molecular bases of the interactions of ATG16L1 with FIP200 and ATG8 family proteins.Nature communications · 2025Article
- Recruitment of Atg1 to the phagophore by Atg8 orchestrates autophagy machineries.Nature structural & molecular biology · 2025Article
- Omic AI reveals new autophagy regulators from the Atg1 interactome inFrontiers in cell and developmental biology · 2025Article
- When an underdog becomes a major player: the role of protein structural disorder in the Atg8 conjugation system.Autophagy · 2024Review
- Faa1 membrane binding drives positive feedback in autophagosome biogenesis via fatty acid activation.The Journal of cell biology · 2024Article
- C16ORF70/MYTHO promotes healthy aging in C.elegans and prevents cellular senescence in mammals.The Journal of clinical investigation · 2024Article
- Complete set of the Atg8-E1-E2-E3 conjugation machinery forms an interaction web that mediates membrane shaping.Nature structural & molecular biology · 2024Article
- ATG5 is dispensable for ATG8ylation of cellular proteins.Autophagy reports · 2024Article
- Coiled-coil-mediated dimerization of Atg16 is required for binding to the PROPPIN Atg21.Open biology · 2023Article
- The Intrinsically Disordered N Terminus in Atg12 from Yeast Is Necessary for the Functional Structure of the Protein.International journal of molecular sciences · 2023Article
- Article
- The Atg1 complex, Atg9, and Vac8 recruit PI3K complex I to the pre-autophagosomal structure.The Journal of cell biology · 2023Article
- Review
- Apicoplast biogenesis mediated by ATG8 requires the ATG12-ATG5-ATG16L and SNAP29 complexes inAutophagy · 2023Article
- Targeted Protein Degradation via Lysosomes.Biochemistry · 2023Review
- Impact of interorganelle coordination between the conventional early secretory pathway and autophagy in cellular homeostasis and stress response.Frontiers in cell and developmental biology · 2023Review
- Article
- A dynamically evolving war between autophagy and pathogenic microorganisms.Journal of Zhejiang University. Science. B · 2022Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
In autophagy, Atg proteins organize the pre-autophagosomal structure (PAS) to initiate autophagosome formation. Previous studies in yeast revealed that the autophagy-related E3 complex Atg12-Atg5-Atg16 is recruited to the PAS via Atg16 interaction with Atg21, which binds phosphatidylinositol 3-phosphate (PI3P) produced at the PAS, to stimulate conjugation of the ubiquitin-like protein Atg8 to phosphatidylethanolamine. Here, we discover a novel mechanism for the PAS targeting of Atg12-Atg5-Atg16, which is mediated by the interaction of Atg12 with the Atg1 kinase complex that serves as a scaffold for PAS organization. While autophagy is partially defective without one of these mechanisms, cells lacking both completely lose the PAS localization of Atg12-Atg5-Atg16 and show no autophagic activity. As with the PI3P-dependent mechanism, Atg12-Atg5-Atg16 recruited via the Atg12-dependent mechanism stimulates Atg8 lipidation, but also has the specific function of facilitating PAS scaffold assembly. Thus, this study significantly advances our understanding of the nucleation step in autophagosome formation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.