ArticlePLoS biology2019
N-terminal β-strand underpins biochemical specialization of an ATG8 isoform.
Article in PLoS biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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Who cites it
27 citing papers in PubMed, 59 citations in OpenAlex.
- An A. thaliana mutant lacking all nine ATG8 isoforms provides genetic evidence for functional specialization of ATG8 in plants.Journal of cell science · 2025Article
- Interaction of Potato Autophagy-Related StATG8 Family Proteins with Pathogen Effector and WRKY Transcription Factor in the Nucleus.Microorganisms · 2025Article
- Autophagy restricts tomato fruit ripening via a general role in ethylene repression.The New phytologist · 2025Article
- ATG8 delipidation is not universally critical for autophagy in plants.Nature communications · 2025Article
- Atg8 family proteins, LIR/AIM motifs and other interaction modes.Autophagy reports · 2023Article
- Identification and Expression Analysis of the Solanum tuberosum StATG8 Family Associated with the WRKY Transcription FactorPlants (Basel, Switzerland) · 2022Article
- Regressive evolution of an effector following a host jump in the Irish potato famine pathogen lineage.PLoS pathogens · 2022Article
- Defects in autophagy lead to selective in vivo changes in turnover of cytosolic and organelle proteins in Arabidopsis.The Plant cell · 2022Article
- Selective autophagy: adding precision in plant immunity.Essays in biochemistry · 2022Article
- Autophagic degradation of the chloroplastic 2-phosphoglycolate phosphatase TaPGLP1 in wheat.Plant cell reports · 2022Article
- Molecular mechanisms of endomembrane trafficking in plants.The Plant cell · 2022Review
- Autophagy modulates the metabolism and growth of tomato fruit during development.Horticulture research · 2022Article
- A single amino acid polymorphism in a conserved effector of the multihost blast fungus pathogen expands host-target binding spectrum.PLoS pathogens · 2021Article
- Article
- Plant pathogens convergently evolved to counteract redundant nodes of an NLR immune receptor network.PLoS biology · 2021Article
- Small but mighty: Atg8s and Rabs in membrane dynamics during autophagy.Biochimica et biophysica acta. Molecular cell research · 2021Review
- Host-interactor screens of Phytophthora infestans RXLR proteins reveal vesicle trafficking as a major effector-targeted process.The Plant cell · 2021Article
- Phosphorylation of the LIR Domain of SCOC Modulates ATG8 Binding Affinity and Specificity.Journal of molecular biology · 2021Article
- A unique AtSar1D-AtRabD2a nexus modulates autophagosome biogenesis inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
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Authors and funding
17 authors at 5 institutions in 2 countries.
Funding
Abstract
Autophagy-related protein 8 (ATG8) is a highly conserved ubiquitin-like protein that modulates autophagy pathways by binding autophagic membranes and a number of proteins, including cargo receptors and core autophagy components. Throughout plant evolution, ATG8 has expanded from a single protein in algae to multiple isoforms in higher plants. However, the degree to which ATG8 isoforms have functionally specialized to bind distinct proteins remains unclear. Here, we describe a comprehensive protein-protein interaction resource, obtained using in planta immunoprecipitation (IP) followed by mass spectrometry (MS), to define the potato ATG8 interactome. We discovered that ATG8 isoforms bind distinct sets of plant proteins with varying degrees of overlap. This prompted us to define the biochemical basis of ATG8 specialization by comparing two potato ATG8 isoforms using both in vivo protein interaction assays and in vitro quantitative binding affinity analyses. These experiments revealed that the N-terminal β-strand-and, in particular, a single amino acid polymorphism-underpins binding specificity to the substrate PexRD54 by shaping the hydrophobic pocket that accommodates this protein's ATG8-interacting motif (AIM). Additional proteomics experiments indicated that the N-terminal β-strand shapes the broader ATG8 interactor profiles, defining interaction specificity with about 80 plant proteins. Our findings are consistent with the view that ATG8 isoforms comprise a layer of specificity in the regulation of selective autophagy pathways in plants.
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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 Socratic graph.