Back to Search
Start Over
Subnanometer resolution cryo-EM structure of Arabidopsis thaliana ATG9.
- Source :
-
Autophagy [Autophagy] 2020 Mar; Vol. 16 (3), pp. 575-583. Date of Electronic Publication: 2019 Jul 16. - Publication Year :
- 2020
-
Abstract
- Macroautophagy/autophagy is an essential process for the maintenance of cellular homeostasis by recycling macromolecules under normal and stress conditions. ATG9 (autophagy related 9) is the only integral membrane protein in the autophagy core machinery and has a central role in mediating autophagosome formation. In cells, ATG9 exists on mobile vesicles that traffic to the growing phagophore, providing an essential membrane source for the formation of autophagosomes. Here we report the three-dimensional structure of ATG9 from Arabidopsis thaliana at 7.8 Å resolution, determined by single particle cryo-electron microscopy. ATG9 organizes into a homotrimer, with each protomer contributing at least six transmembrane α-helices. At the center of the trimer, the protomers interact via their membrane-embedded and C-terminal cytoplasmic regions. Combined with prediction of protein contacts using sequence co-evolutionary information, the structure provides molecular insights into the ATG9 architecture and testable hypotheses for the molecular mechanism of autophagy progression regulated by ATG9. Abbreviations: 2D: 2-dimensional; 3D: 3-dimensional; AtATG9: Arabidopsis ATG9; Atg: autophagy-related; ATG9: autophagy-related protein 9; cryo-EM: cryo-electron microscopy; DDM: dodecyl maltoside; GraDeR: gradient-based detergent removal; LMNG: lauryl maltose-neopentyl glycol; PAS: phagophore assembly site; PtdIns3K: phosphatidylinositol 3-kinase.
- Subjects :
- Arabidopsis Proteins ultrastructure
Autophagy-Related Proteins ultrastructure
Membrane Proteins ultrastructure
Models, Molecular
Protein Multimerization
Protein Structure, Secondary
Structural Homology, Protein
Arabidopsis metabolism
Arabidopsis ultrastructure
Arabidopsis Proteins metabolism
Autophagy-Related Proteins metabolism
Cryoelectron Microscopy
Membrane Proteins metabolism
Nanotechnology
Subjects
Details
- Language :
- English
- ISSN :
- 1554-8635
- Volume :
- 16
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Autophagy
- Publication Type :
- Academic Journal
- Accession number :
- 31276439
- Full Text :
- https://doi.org/10.1080/15548627.2019.1639300