ArticleMolecular biology of the cell2018
The dynamic Atg13-free conformation of the Atg1 EAT domain is required for phagophore expansion.
Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 17 citations in OpenAlex.
- Recruitment of Atg1 to the phagophore by Atg8 orchestrates autophagy machineries.Nature structural & molecular biology · 2025Article
- Temporal dissection of the roles of Atg4 and ESCRT in autophagosome formation in yeast.Cell death and differentiation · 2025Article
- Article
- Omic AI reveals new autophagy regulators from the Atg1 interactome inFrontiers in cell and developmental biology · 2025Article
- AI-based AlphaFold2 significantly expands the structural space of the autophagy pathway.Autophagy · 2023Article
- Kinase regulation by liquid-liquid phase separation.Trends in cell biology · 2023Review
- Article
- Phase Separation in Regulation of Autophagy.Frontiers in cell and developmental biology · 2022Article
- BioID reveals an ATG9A interaction with ATG13-ATG101 in the degradation of p62/SQSTM1-ubiquitin clusters.EMBO reports · 2021Article
- Small but mighty: Atg8s and Rabs in membrane dynamics during autophagy.Biochimica et biophysica acta. Molecular cell research · 2021Review
- Atg38-Atg8 interaction in fission yeast establishes a positive feedback loop to promote autophagy.Autophagy · 2020Article
- Article
- Mechanisms governing autophagosome biogenesis.Nature reviews. Molecular cell biology · 2020Review
- Recruitment and Activation of the ULK1/Atg1 Kinase Complex in Selective Autophagy.Journal of molecular biology · 2020Review
- Emerging roles of ATG proteins and membrane lipids in autophagosome formation.Cell discovery · 2020Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Yeast macroautophagy begins with the de novo formation of a double-membrane phagophore at the preautophagosomal structure/phagophore assembly site (PAS), followed by its expansion into the autophagosome responsible for cargo engulfment. The kinase Atg1 is recruited to the PAS by Atg13 through interactions between the EAT domain of the former and the tMIM motif of the latter. Mass-spectrometry data have shown that, in the absence of Atg13, the EAT domain structure is strikingly dynamic, but the function of this Atg13-free dynamic state has been unclear. We used structure-based mutational analysis and quantitative and superresolution microscopy to show that Atg1 is present on autophagic puncta at, on average, twice the stoichiometry of Atg13. Moreover, Atg1 colocalizes with the expanding autophagosome in a manner dependent on Atg8 but not Atg13. We used isothermal titration calorimetry and crystal structure information to design an EAT domain mutant allele ATG1
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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.