Evidence map›Paper›PMID 32686895›Full record

ArticleChembiochem : a European journal of chemical biology2020

Distinct Mechanisms for Processing Autophagy Protein LC3-PE by RavZ and ATG4B.

Aimin Yang, Supansa Pantoom, Yao-Wen Wu

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.3field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Mechanisms and roles of membrane-anchored ATG8s.Frontiers in cell and developmental biology · 2025
    Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Atg8-PE protein-basedAutophagy · 2022
    Review
  10. Chemische Synthese und Semisynthese von lipidierten Proteinen.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022
    Review
  11. Chemical Synthesis and Semisynthesis of Lipidated Proteins.Angewandte Chemie (International ed. in English) · 2022
    Review
  12. Review
  13. Article
  14. Distinct Mechanisms for Processing Autophagy Protein LC3-PE by RavZ and ATG4B.Chembiochem : a European journal of chemical biology · 2020
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 3 institutions in 3 countries.

Aimin YangSchool of Life Sciences, Chongqing University, 401331, Chongqing, P. R. China.
Supansa PantoomTranslational Neurodegeneration Section "Albrecht-Kossel" Department of Neurology, University Medical Center Rostock, 18147, Rostock, Germany.
Yao-Wen WuDepartment of Chemistry Umeå Centre for Microbial Research, Umeå University, 90187, Umeå, Sweden.ORCID 0000-0002-2573-8736
Chongqing University · CNMax Planck Society · DEUniversity of Rostock · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is a conserved catabolic process involved in the elimination of proteins, organelles and pathogens in eukaryotic cells. Lipidated LC3 proteins that are conjugated to phosphatidylethanolamine (PE) play a key role in autophagosome biogenesis. Endogenous ATG4-mediated deconjugation of LC3-PE is required for LC3 recycling. However, the Legionella effector RavZ irreversibly deconjugates LC3-PE to inhibit autophagy. It is not clear how ATG4 and RavZ process LC3-PE with distinct modes. Herein, a series of semisynthetic LC3-PE proteins containing C-terminal mutations or insertions were used to investigate the relationship of the C-terminal structure of LC3-PE with ATG4/RavZ-mediated deconjugation. Using a combination of molecular docking and biochemical assays, we found that Gln116, Phe119 and Gly120 of LC3-PE are required for cleavage by both RavZ and ATG4B, whereas Glu117(LC3) is specific to cleavage by RavZ. The molecular ruler mechanism exists in the active site of ATG4B, but not in RavZ. Met63 and Gln64 at the active site of RavZ are involved in accommodating LC3 C-terminal motif. Our findings show that the distinct binding modes of the LC3 C-terminal motif (116-120) with ATG4 and RavZ might determine the specificity of cleavage site.

Indexed as

AutophagyAutophagy-Related ProteinsBacterial ProteinsCysteine EndopeptidasesHumansLegionella pneumophilaMicrotubule-Associated ProteinsMolecular Docking SimulationPhosphatidylethanolaminesATG4B protein, humanAutophagy-Related ProteinsBacterial ProteinsCysteine EndopeptidasesMAP1LC3A protein, humanMicrotubule-Associated ProteinsphosphatidylethanolaminePhosphatidylethanolaminesautophagycysteine proteasesexpressed protein ligationLegionella pneumophilapeptide synthesis

Identifiers

PMID32686895
PMCPMC7754449
OpenAlexW3042474626

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.