ArticleThe Journal of biological chemistry2010
Selective transport of alpha-mannosidase by autophagic pathways: structural basis for cargo recognition by Atg19 and Atg34.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 2 of them syntheses that pooled it.
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Who cites it
33 citing papers in PubMed, 2 syntheses or guidelines pooled it, 52 citations in OpenAlex.
- Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)Autophagy · 2021Guideline
- Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).Autophagy · 2016Guideline
- NBR1: The archetypal selective autophagy receptor.The Journal of cell biology · 2022Review
- Structural mechanism of protein recognition by the FW domain of autophagy receptor Nbr1.Nature communications · 2022Article
- A lysosomal biogenesis map reveals the cargo spectrum of yeast vacuolar protein targeting pathways.The Journal of cell biology · 2022Article
- Spatial control of avidity regulates initiation and progression of selective autophagy.Nature communications · 2021Article
- Molecular and structural mechanisms of ZZ domain-mediated cargo selection by Nbr1.The EMBO journal · 2021Article
- Cryo-EM structure of fission yeast tetrameric α-mannosidase Ams1.FEBS open bio · 2020Article
- The Roles of Ubiquitin in Mediating Autophagy.Cells · 2020Review
- History of the Selective Autophagy Research: How Did It Begin and Where Does It Stand Today?Journal of molecular biology · 2020Review
- Vac8 spatially confines autophagosome formation at the vacuole inJournal of cell science · 2019Article
- Selective Autophagy of Mitochondria on a Ubiquitin-Endoplasmic-Reticulum Platform.Developmental cell · 2019Article
- Gyp1 has a dual function as Ypt1 GAP and interaction partner of Atg8 in selective autophagy.Autophagy · 2019Article
- Mechanistic insights into selective autophagy pathways: lessons from yeast.Nature reviews. Molecular cell biology · 2016Review
- An overview of macroautophagy in yeast.Journal of molecular biology · 2016Review
- Mechanisms of Selective Autophagy.Journal of molecular biology · 2016Review
- Post-translationally-modified structures in the autophagy machinery: an integrative perspective.The FEBS journal · 2015Review
- Generation and degradation of free asparagine-linked glycans.Cellular and molecular life sciences : CMLS · 2015Review
- The machinery of macroautophagy.Cell research · 2014Review
- Glycobiology of cell death: when glycans and lectins govern cell fate.Cell death and differentiation · 2013Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the yeast Saccharomyces cerevisiae, a precursor form of aminopeptidase I (prApe1) and α-mannosidase (Ams1) are selectively transported to the vacuole through the cytoplasm-to-vacuole targeting pathway under vegetative conditions and through autophagy under starvation conditions. Atg19 plays a central role in these processes by linking Ams1 and prApe1 to Atg8 and Atg11. However, little is known about the molecular mechanisms of cargo recognition by Atg19. Here, we report structural and functional analyses of Atg19 and its paralog, Atg34. A protease-resistant domain was identified in the C-terminal region of Atg19, which was also conserved in Atg34. In vitro pulldown assays showed that the C-terminal domains of both Atg19 and Atg34 are responsible for Ams1 binding; these domains are hereafter referred to as Ams1-binding domains (ABDs). The transport of Ams1, but not prApe1, was blocked in atg19Δatg34Δ cells expressing Atg19(ΔABD), indicating that ABD is specifically required for Ams1 transport. We then determined the solution structures of the ABDs of Atg19 and Atg34 using NMR spectroscopy. Both ABD structures have a canonical immunoglobulin fold consisting of eight β-strands with highly conserved loops clustered at one side of the fold. These facts, together with the results of a mutational analysis, suggest that ABD recognizes Ams1 using these conserved loops.
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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.