ArticleScientific reports2019
Solution structure of the autophagy-related protein LC3C reveals a polyproline II motif on a mobile tether with phosphorylation site.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Transcriptomic Analysis of Bovine Oocytes at GV and MII Stages and Dynamic Changes in Key Gene Expression Patterns.Biology · 2026Article
- When an underdog becomes a major player: the role of protein structural disorder in the Atg8 conjugation system.Autophagy · 2024Review
- Article
- Highlighting the hidden: monitoring the avidity-driven association of a fluorescent GABARAP tandem with microtubules in living cells.Autophagy reports · 2024Article
- Atg8 family proteins, LIR/AIM motifs and other interaction modes.Autophagy reports · 2023Article
- AIE-enabled transfection-free identification and isolation of viable cell subpopulations differing in the level of autophagy.Autophagy · 2023Article
- LC3 subfamily in cardiolipin-mediated mitophagy: a comparison of the LC3A, LC3B and LC3C homologs.Autophagy · 2022Article
- Canonical and non-canonical roles for ATG8 proteins in autophagy and beyond.Frontiers in molecular biosciences · 2022Review
- Atg8-Family Proteins-Structural Features and Molecular Interactions in Autophagy and Beyond.Cells · 2020Review
- Structure and Dynamics in the ATG8 Family From Experimental to Computational Techniques.Frontiers in cell and developmental biology · 2020Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
(Macro-)autophagy is a compartmental degradation pathway conserved from yeast to mammals. The yeast protein Atg8 mediates membrane tethering/hemifusion and cargo recruitment and is essential for autophagy. The human MAP1LC3/GABARAP family proteins show high sequence identity with Atg8, but MAP1LC3C is distinguished by a conspicuous amino-terminal extension with unknown functional significance. We have determined the high-resolution three-dimensional structure and measured the backbone dynamics of MAP1LC3C by NMR spectroscopy. From Ser18 to Ala120, MAP1LC3C forms an α-helix followed by the ubiquitin-like tertiary fold with two hydrophobic binding pockets used by MAP1LC3/GABARAP proteins to recognize targets presenting LC3-interacting regions (LIRs). Unlike other MAP1LC3/GABARAP proteins, the amino-terminal region of MAP1LC3C does not form a stable helix α
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