ArticleProtein science : a publication of the Protein Society2026
Role of N-glycosylation as a determinant of ATG9A conformations and activity.
Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Distinct structural mechanisms drive gain-of-function activation of TMEM16E in gnathodiaphyseal dysplasia.Research square · 2026Article
- Role of N-glycosylation as a determinant of ATG9A conformations and activity.Protein science : a publication of the Protein Society · 2026Article
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Authors and funding
11 authors.
Funding
Abstract
Here, we investigate the effects of glycosylation at position N99 on the structural dynamics and lipid scrambling activity of ATG9A, a key autophagy protein, using microsecond all-atom molecular dynamics simulations. ATG9A is an integral membrane protein involved in autophagosome biogenesis, and glycosylation at N99 has previously been implicated in intracellular trafficking, although its precise role remains unclear. The simulations reveal that the hydrophilic central cavity of ATG9A supports lipid reorientation and partial trans-bilayer movements, consistent with experiments on its lipid scrambling activity. We propose that N-glycosylation at N99 enhances cooperative interactions between protomers, facilitating lipid insertion and translocation within the central cavity. These findings suggest a mechanism by which glycosylation may influence lipid redistribution across the phagophore membrane during autophagy. To test this hypothesis, we generate N99 variants (ATG9A
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