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Metamorphic proteins at the basis of human autophagy initiation and lipid transfer
Open accessPreprint — published as 10.1016/j.molcel.2023.04.026
Abstract
Autophagy is a conserved intracellular degradation pathway that uses de novo doublemembrane vesicle (autophagosome) formation to target a wide range of cytoplasmic material for lysosomal degradation. In multicellular organisms, autophagy initiation requires the timely assembly of a contact site between the ER and the nascent autophagosome. Here, we report the in vitro reconstitution of a full-length sevensubunit human autophagy initiation supercomplex and found at its core ATG13-101 and transmembrane protein ATG9. Assembly of this core complex requires the rare ability of ATG13 and ATG101 to adopt topologically distinct folds. The slow spontaneous conversion between folds creates a rate-limiting step to regulate selfassembly of the super-complex. The interaction of the core complex with ATG2-WIPI4 enhances tethering of membrane vesicles and accelerates lipid transfer of ATG2 by both ATG9 and ATG13-101. Our work uncovers the molecular basis of the contact site and its assembly mechanisms imposed by the metamorphosis of ATG13-101 to regulate autophagosome biogenesis in space and time.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Nguyen, A., Lugarini, F., David, C., Hosnani, P., Knotkova, B., Patel, A., Parfentev, I., Friedrich, A., Urlaub, H., Meinecke, M., Stork, B., & Faesen, A. C.
- Affiliations
- Max Planck Institute for Multidisciplinary Sciences (DE)
- Düsseldorf University Hospital (DE)
- Heidelberg University (DE)
- Universitätsmedizin Göttingen (DE)
- Corresponding author
- Faesen, Alex C.
- Venue
- Molecular Cell
- Publisher
- openRxiv
- Published
- 2022-09-21
- Volume
- 83
- Issue
- 12
- Pages
- 2077-2090.e12
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W4377092158
- Cited by
- 47
- References
- 1
- Citations by year
- 2026: 10 · 2025: 16 · 2024: 11 · 2023: 9 · 2022: 1
- FWCI
- 9.17
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- Molecular Cell (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
- PubMed (publishedVersion)
- GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (submittedVersion, cc-by)
- Funders
- Boehringer Ingelheim Fonds (DFG-INST 208/746-1 FUGG)
- Deutsche Forschungsgemeinschaft (SFB 1190, DFG SFB1190)
- Max-Planck-Gesellschaft (SFB1190, GRK2158, STO864/4-3, GRK2578, STO864/6-1)
- University of Tokyo (FIP200)
- Center for Advanced Brain Imaging
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › 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 › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- autophagy initiation, Atg9, in vitro reconstitution, lipid transfer, autophagosome formation, membrane tethering
- MeSH terms
- Autophagosomes, Autophagy-Related Proteins, Autophagy, Humans, Lipids, Membrane Proteins
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