ArticleBiochemical and biophysical research communications2015
Identification and characterization of the linear region of ATG3 that interacts with ATG7 in higher eukaryotes.
Article in Biochemical and biophysical research communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Structural Insights into the GABARAP-ATG3 Backside Interaction and Apo ATG3 Conformation.Biochemistry · 2025Article
- Structural Analyses of a GABARAP~ATG3 Conjugate Uncover a Novel Non-covalent Ubl-E2 Backside Interaction.bioRxiv : the preprint server for biology · 2024Article
- Semisynthetic LC3 Probes for Autophagy Pathways Reveal a Noncanonical LC3 Interacting Region Motif Crucial for the Enzymatic Activity of Human ATG3.ACS central science · 2023Article
- An N-terminal conserved region in human Atg3 couples membrane curvature sensitivity to conjugase activity during autophagy.Nature communications · 2021Article
- Binding Features and Functions of ATG3.Frontiers in cell and developmental biology · 2021Review
- Review
- A switch element in the autophagy E2 Atg3 mediates allosteric regulation across the lipidation cascade.Nature communications · 2019Article
- Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.Chemical reviews · 2018Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Transfer of GABARAP thioester from the E1 ATG7 to the E2 ATG3 requires the interaction between the N-terminal domain of ATG7 and the flexible region (FR) of ATG3. This interaction has been visualized in the yeast Atg7-Atg3 complex crystal structure, but remains to be defined in higher eukaryotes. Here, our NMR data precisely define the region of the FR of human ATG3 that interacts with ATG7 (RIA7) and demonstrate RIA7 partially overlaps with the E3-interacting region, explaining how the E1-E2 and E2-E3 interactions are mutually exclusive. Mutational analyses identify critical residues of the RIA7 for the E1 interaction and GABARAP transfer, advancing our understanding of a molecular mechanism of the autophagic conjugation cascade in higher eukaryotes.
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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.