ArticleThe Journal of biological chemistry2012
Propeptide of aminopeptidase 1 protein mediates aggregation and vesicle formation in cytoplasm-to-vacuole targeting pathway.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Recent Advances in Single-Particle Electron Microscopic Analysis of Autophagy Degradation Machinery.International journal of molecular sciences · 2020Review
- Autophagy in cancers including brain tumors: role of MicroRNAs.Cell communication and signaling : CCS · 2020Review
- Proteomic response ofFood science and biotechnology · 2019Article
- Autophagy Protects the Blood-Brain Barrier Through Regulating the Dynamic of Claudin-5 in Short-Term Starvation.Frontiers in physiology · 2019Article
- Higher-order assemblies of oligomeric cargo receptor complexes form the membrane scaffold of the Cvt vesicle.EMBO reports · 2016Article
- Mechanisms of Selective Autophagy.Journal of molecular biology · 2016Review
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- Article
- The contribution of Candida albicans vacuolar ATPase subunit V₁B, encoded by VMA2, to stress response, autophagy, and virulence is independent of environmental pH.Eukaryotic cell · 2014Article
- The proteolytic landscape of the yeast vacuole.Cellular logistics · 2014Review
- Selective autophagy in budding yeast.Cell death and differentiation · 2013Review
- Autophagy: more than a nonselective pathway.International journal of cell biology · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Misfolded protein aggregation causes disease and aging; autophagy counteracts this by eliminating damaged components, enabling cells to survive starvation. The cytoplasm-to-vacuole targeting pathway in yeast encompasses the aggregation of the premature form of aminopeptidase 1 (prApe1) in cytosol and its sequestration by autophagic proteins into a vesicle for vacuolar transport. We show that the propeptide of Ape1 is important for aggregation and vesicle formation and that it is sufficient for binding to prApe1 and Atg19. Defective aggregation disrupts vacuolar transport, suggesting that aggregate shape is important in vesicle formation, whereas Atg19 binding is not sufficient for vacuolar transport. Aggregation involves hydrophobicity, whereas Atg19 binding requires additional electrostatic interactions. Ape1 dodecamerization may cluster propeptides into trimeric structures, with sufficient affinity to form propeptide hexamers by binding to other dodecamers, causing aggregation. We show that Ape1 aggregates bind Atg19 and Atg8 in vitro; this could be used as a scaffold for an in vitro assay of autophagosome formation to elucidate the mechanisms of autophagy.
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Registered trials
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