Evidence map›Paper›PMID 28327644›Full record

ArticleNature communications2017

A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation.

Yi-Tong Li, Cong Yi, Chen-Chen Chen, Huan Lan, Man Pan, Shao-Jin Zhang, Yi-Chao Huang, Chao-Jian Guan, Yi-Ming Li, Li Yu and 1 more

Abstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Atg8-PE protein-basedAutophagy · 2022
    Review
  10. Review
  11. All-Frontiers in oncology · 2022
    Article
  12. Article
  13. Binding Features and Functions of ATG3.Frontiers in cell and developmental biology · 2021
    Review
  14. Article
  15. Review
  16. Atg3 promotes Atg8 lipidation via altering lipid diffusion and rearrangement.Protein science : a publication of the Protein Society · 2020
    Article
  17. Article
  18. Review
  19. Review
  20. Review
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

11 authors.

Yi-Tong LiSchool of Biological and Medical Engineering, Hefei University of Technology, Anhui, Hefei 230009, China.
Cong YiTsinghua-Peking Center for Life Sciences, Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Chen-Chen ChenSchool of Biological and Medical Engineering, Hefei University of Technology, Anhui, Hefei 230009, China.
Huan LanTsinghua-Peking Center for Life Sciences, Key Laboratory of Bioorganic Phosphorus Chemistry &Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China.
Man PanTsinghua-Peking Center for Life Sciences, Key Laboratory of Bioorganic Phosphorus Chemistry &Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China.
Shao-Jin ZhangTsinghua-Peking Center for Life Sciences, Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Yi-Chao HuangTsinghua-Peking Center for Life Sciences, Key Laboratory of Bioorganic Phosphorus Chemistry &Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China.
Chao-Jian GuanSchool of Biological and Medical Engineering, Hefei University of Technology, Anhui, Hefei 230009, China.
Yi-Ming LiSchool of Biological and Medical Engineering, Hefei University of Technology, Anhui, Hefei 230009, China.
Li YuTsinghua-Peking Center for Life Sciences, Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Lei LiuTsinghua-Peking Center for Life Sciences, Key Laboratory of Bioorganic Phosphorus Chemistry &Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetylation of Atg3 regulates the lipidation of the protein Atg8 in autophagy. The molecular mechanism behind this important biochemical event remains to be elucidated. We describe the first semi-synthesis of homogeneous K19/K48-diacetylated Atg3 through sequential hydrazide-based native chemical ligation. In vitro reconstitution experiments with the semi-synthetic proteins confirm that Atg3 acetylation can promote the lipidation of Atg8. We find that acetylation of Atg3 enhances its binding to phosphatidylethanolamine-containing liposomes and to endoplasmic reticulum, through which it promotes the lipidation process.

Indexed as

AcetylationAmino Acid SequenceAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsEndoplasmic ReticulumEstersIntracellular MembranesLipidsLiposomesLysineModels, BiologicalProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating EnzymesATG3 protein, S cerevisiaeATG8 protein, S cerevisiaeAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsEstersLipidsLiposomesLysineSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating Enzymes

Identifiers

PMID28327644
PMCPMC5473643

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Registered trials

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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.