ArticleCellular and molecular life sciences : CMLS2021
The crystal structure of Atg18 reveals a new binding site for Atg2 in Saccharomyces cerevisiae.
Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- PfATG18 links V-ATPase assembly to endocytic membrane dynamics in malaria parasites.PLoS pathogens · 2026Article
- Atg18 oligomer organization in assembled tubes and on lipid membrane scaffolds.Nature communications · 2023Article
- In Vitro Transcriptional Response ofInternational journal of molecular sciences · 2023Article
- Article
- CROP: a retromer-PROPPIN complex mediating membrane fission in the endo-lysosomal system.The EMBO journal · 2022Article
- A conserved ATG2 binding site in WIPI4 and yeast Hsv2 is disrupted by mutations causing β-propeller protein-associated neurodegeneration.Human molecular genetics · 2021Article
- Review
- TheFrontiers in cell and developmental biology · 2021Review
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Authors and funding
16 authors at 4 institutions in 1 country.
Funding
Abstract
Macroautophagy (hereafter referred to as autophagy) is a highly conserved catabolic eukaryotic pathway that is critical for stress responses and homeostasis. Atg18, one of the core proteins involved in autophagy, belongs to the PROPPIN family and is composed of seven WD40 repeats. Together with Atg2, Atg18 participates in the elongation of phagophores and the recycling of Atg9 in yeast. Despite extensive studies on the PROPPIN family, the structure of Atg18 from Saccharomyces cerevisiae has not been determined. Here, we report the structure of ScAtg18 at a resolution of 2.8 Å. Based on bioinformatics and structural analysis, we found that the 7AB loop of ScAtg18 is extended in Atg18, in comparison to other members of the PROPPIN family. Genetic analysis revealed that the 7AB loop of ScAtg18 is required for autophagy. Biochemical and biophysical experiments indicated that the 7AB loop of ScAtg18 is critical for interaction with ScAtg2 and the recruitment of ScAtg2 to the autophagy-initiating site. Collectively, our results show that the 7AB loop of ScAtg18 is a new binding site for Atg2 and is of functional importance to autophagy.
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