ArticleThe EMBO journal2024
Receptor-mediated cargo hitchhiking on bulk autophagy.
Article in The EMBO journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Nucleophagy is promoted by two autophagy receptors and inhibited by chromatin-nuclear envelope tethering in fission yeast.Nature communications · 2026Article
- Core principles of autophagy initiation mechanisms.Nature structural & molecular biology · 2026Review
- Review
- Reconsidering the selectivity of bulk autophagy: cargo hitchhiking specifies cargo for degradation.Autophagy · 2025Article
- Review
- A plasmid module for PCR-based gene modification for the accurate measurement of vacuolar delivery of specific proteins in yeastAutophagy reports · 2025Article
- Med13 is required for efficient P-body recruitment and autophagic degradation of Edc3 following nitrogen starvation.Molecular biology of the cell · 2024Article
- A hitchhiker's guide to autophagy.The EMBO journal · 2024Article
- Atg45 is an autophagy receptor for glycogen, a non-preferred cargo of bulk autophagy in yeast.iScience · 2024Article
Corrections and comments
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Authors and funding
7 authors.
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Abstract
While the molecular mechanism of autophagy is well studied, the cargoes delivered by autophagy remain incompletely characterized. To examine the selectivity of autophagy cargo, we conducted proteomics on isolated yeast autophagic bodies, which are intermediate structures in the autophagy process. We identify a protein, Hab1, that is highly preferentially delivered to vacuoles. The N-terminal 42 amino acid region of Hab1 contains an amphipathic helix and an Atg8-family interacting motif, both of which are necessary and sufficient for the preferential delivery of Hab1 by autophagy. We find that fusion of this region with a cytosolic protein results in preferential delivery of this protein to the vacuole. Furthermore, attachment of this region to an organelle allows for autophagic delivery in a manner independent of canonical autophagy receptor or scaffold proteins. We propose a novel mode of selective autophagy in which a receptor, in this case Hab1, binds directly to forming isolation membranes during bulk autophagy.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.