ArticleCell reports2022
Dimerization-dependent membrane tethering by Atg23 is essential for yeast autophagy.
Article in Cell reports, 2022. 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.
- Atg23 prevents aberrant fusion of Atg9 vesicles during delivery to autophagosome formation sites.The EMBO journal · 2026Article
- Membrane-Associated Biomolecules for Synthetic Cell Signalling.Chembiochem : a European journal of chemical biology · 2026Review
- A GUV-based assay to reconstitute membrane tethering in vitro.Molecular biology of the cell · 2026Article
- Review
- Reconstitution of autophagic-like membrane tethering reveals that Atg11 can bind and cluster vesicles on cargo mimetics.Autophagy · 2026Article
- Atg23 Interacts With Both the N- and C-termini of Atg9 Via a Hydrophobic Binding Pocket.bioRxiv : the preprint server for biology · 2025Article
- Amino Acid Substitutions in Bacteriocin Lactolisterin BU Reveal Functional Domains Involved in Biological Activity AgainstMolecules (Basel, Switzerland) · 2025Article
- ATG9A vesicles are a subtype of intracellular nanovesicle.Journal of cell science · 2025Article
- Huntingtin contains an ubiquitin-binding domain and regulates lysosomal targeting of mitochondrial and RNA-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- TOR-mediated Ypt1 phosphorylation regulates autophagy initiation complex assembly.The EMBO journal · 2023Article
- Osmotic Pressure Enables High-Yield Assembly of Giant Vesicles in Solutions of Physiological Ionic Strengths.Langmuir : the ACS journal of surfaces and colloids · 2023Article
- Atg23 is a vesicle-tethering protein.Autophagy · 2022Article
- Article
- Review
- Theater in the Self-Cleaning Cell: Intrinsically Disordered Proteins or Protein Regions Acting with Membranes in Autophagy.Membranes · 2022Review
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6 authors.
Funding
Abstract
Eukaryotes maintain cellular health through the engulfment and subsequent degradation of intracellular cargo using macroautophagy. The function of Atg23, despite being critical to the efficiency of this process, is unclear due to a lack of biochemical investigations and an absence of any structural information. In this study, we use a combination of in vitro and in vivo methods to show that Atg23 exists primarily as a homodimer, a conformation facilitated by a putative amphipathic helix. We utilize small-angle X-ray scattering to monitor the overall shape of Atg23, revealing that it contains an extended rod-like structure spanning approximately 320 Å. We also demonstrate that Atg23 interacts with membranes directly, primarily through electrostatic interactions, and that these interactions lead to vesicle tethering. Finally, mutation of the hydrophobic face of the putative amphipathic helix completely precludes dimer formation, leading to severely impaired subcellular localization, vesicle tethering, Atg9 binding, and autophagic efficiency.
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