ArticleJournal of molecular biology2021
Membrane Binding and Homodimerization of Atg16 Via Two Distinct Protein Regions is Essential for Autophagy in Yeast.
Article in Journal of molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 22 citations in OpenAlex.
- Autophagy and metabolic homeostasis: Exploration in obesity‑related metabolic diseases (Review).International journal of molecular medicine · 2026Review
- Reconstitution of autophagic-like membrane tethering reveals that Atg11 can bind and cluster vesicles on cargo mimetics.Autophagy · 2026Article
- The nonsense-mediated mRNA decay factor Upf3 negatively regulates bulk autophagy progression inAutophagy reports · 2026Article
- The CgATG16 Was Involved in Growth, Development and Virulence Through Autophagy Modulation in the Rubber Tree Anthracnose FungusJournal of fungi (Basel, Switzerland) · 2025Article
- Pharmacological mechanism of natural products to treat osteoporosis: a focus on the autophagy.Frontiers in pharmacology · 2025Review
- When an underdog becomes a major player: the role of protein structural disorder in the Atg8 conjugation system.Autophagy · 2024Review
- Autophagy: Are Amino Acid Signals Dependent on the mTORC1 Pathway or Independent?Current issues in molecular biology · 2024Review
- Complete set of the Atg8-E1-E2-E3 conjugation machinery forms an interaction web that mediates membrane shaping.Nature structural & molecular biology · 2024Article
- The pivotal role of dysregulated autophagy in the progression of non-alcoholic fatty liver disease.Frontiers in endocrinology · 2024Review
- Coiled-coil-mediated dimerization of Atg16 is required for binding to the PROPPIN Atg21.Open biology · 2023Article
- Autophagy in hepatic ischemia-reperfusion injury.Cell death discovery · 2023Review
- Effect of ATG12-ATG5-ATG16L1 autophagy E3-like complex on the ability of LC3/GABARAP proteins to induce vesicle tethering and fusion.Cellular and molecular life sciences : CMLS · 2023Article
- Evolutionary diversification of the autophagy-related ubiquitin-like conjugation systems.Autophagy · 2022Article
- Atg8-PE protein-basedAutophagy · 2022Review
- Review
- Theater in the Self-Cleaning Cell: Intrinsically Disordered Proteins or Protein Regions Acting with Membranes in Autophagy.Membranes · 2022Review
- The critical role of dysregulated autophagy in the progression of diabetic kidney disease.Frontiers in pharmacology · 2022Review
- Multiple structural rearrangements mediated by high-plasticity regions in Atg3 are key for efficient conjugation of Atg8 to PE during autophagy.Autophagy · 2021Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
Macroautophagy is a bulk degradation mechanism in eukaryotic cells. Efficiency of an essential step of this process in yeast, Atg8 lipidation, relies on the presence of Atg16, a subunit of the Atg12-Atg5-Atg16 complex acting as the E3-like enzyme in the ubiquitination-like reaction. A current view on the functional structure of Atg16 in the yeast S. cerevisiae comes from the two crystal structures that reveal the Atg5-interacting α-helix linked via a flexible linker to another α-helix of Atg16, which then assembles into a homodimer. This view does not explain the results of previous in vitro studies revealing Atg16-dependent deformations of membranes and liposome-binding of the Atg12-Atg5 conjugate upon addition of Atg16. Here we show that Atg16 acts as both a homodimerizing and peripheral membrane-binding polypeptide. These two characteristics are imposed by the two distinct regions that are disordered in the nascent protein. Atg16 binds to membranes in vivo via the amphipathic α-helix (amino acid residues 113-131) that has a coiled-coil-like propensity and a strong hydrophobic face for insertion into the membrane. The other protein region (residues 64-99) possesses a coiled-coil propensity, but not amphipathicity, and is dispensable for membrane anchoring of Atg16. This region acts as a Leu-zipper essential for formation of the Atg16 homodimer. Mutagenic disruption in either of these two distinct domains renders Atg16 proteins that, in contrast to wild type, completely fail to rescue the autophagy-defective phenotype of atg16Δ cells. Together, the results of this study yield a model for the molecular mechanism of Atg16 function in macroautophagy.
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