Structure of Human ATG9A, the Only Transmembrane Protein of the Core Autophagy Machinery
Open accessAbstract
Autophagy is a catabolic process involving capture of cytoplasmic materials into double-membraned autophagosomes that subsequently fuse with lysosomes for degradation of the materials by lysosomal hydrolases. One of the least understood components of the autophagy machinery is the transmembrane protein ATG9. Here, we report a cryoelectron microscopy structure of the human ATG9A isoform at 2.9-Å resolution. The structure reveals a fold with a homotrimeric domain-swapped architecture, multiple membrane spans, and a network of branched cavities, consistent with ATG9A being a membrane transporter. Mutational analyses support a role for the cavities in the function of ATG9A. In addition, structure-guided molecular simulations predict that ATG9A causes membrane bending, explaining the localization of this protein to small vesicles and highly curved edges of growing autophagosomes.
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Inactive ATG9A with mutations in the core part of the protein increased LC3 puncta size in ATG9A KO and wildtype HeLa cells, suggesting a dominant-negative effect.
“a recent study found that inactive ATG9A with mutations in the core part of the protein increased LC3 puncta size not only in ATG9A KO but also in wildtype HeLa cells, suggesting a dominant-negative effect [65].”
From miRNA family miR-29 inhibits PINK1-PRKN signaling via ATG9A (2026) · cites this paper as [65]
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- Authors
- Guardia, C. M., Tan, X.-F., Lian, T., Rana, M. S., Zhou, W., Christenson, E. T., Lowry, A. J., Faraldo-Gómez, J. D., Bonifacino, J. S., Jiang, J., & Banerjee, A.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Bonifacino, Juan S.
- Jiang, Jiansen
- Banerjee, Anirban
- ORCID
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2020-06
- Volume
- 31
- Issue
- 13
- Pages
- 107837
- ISSN
- 2211-1247 (ISSN-L)
- PMC
- PMC7388177
- OpenAlex
- W3038998766
- Cited by
- 163
- References
- 38
- Citations by year
- 2026: 18 · 2025: 19 · 2024: 30 · 2023: 28 · 2022: 30 · 2021: 29 · 2020: 9
- FWCI
- 17.75
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (ZIA HD001607, ZIA HD008928)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Keywords
- ATG9A, autophagy, membrane transporters, transmembrane protein structure, membrane bending, protein localization, cryo-EM structure
- MeSH terms
- Autophagy-Related Proteins, Protein Domains, Amino Acid Sequence, Autophagy, HeLa Cells, Humans, Lipid Bilayers, Membrane Proteins, Phosphatidylcholines, Mutagenesis, Protein Structure, Secondary, Cryoelectron Microscopy, Protein Subunits, Vesicular Transport Proteins, Protein Multimerization, Molecular Dynamics Simulation, HEK293 Cells, Hydrophobic and Hydrophilic Interactions
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