Evidence map›Paper›PMID 31399562›Full record

ArticleNature communications2019

A switch element in the autophagy E2 Atg3 mediates allosteric regulation across the lipidation cascade.

Yumei Zheng, Yu Qiu, Christy R R Grace, Xu Liu, Daniel J Klionsky, Brenda A Schulman

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

28 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
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  3. EnterohemorrhagicAIMS microbiology · 2025
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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

6 authors at 3 institutions in 2 countries.

Yumei ZhengDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.ORCID http://orcid.org/0000-0002-4033-2670
Yu QiuDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.ORCID http://orcid.org/0000-0002-2078-0513
Christy R R GraceDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.ORCID http://orcid.org/0000-0002-1600-5610
Xu LiuLife Sciences Institute, University of Michigan, Ann Arbor, MI, USA.ORCID http://orcid.org/0000-0002-3314-6511
Daniel J KlionskyLife Sciences Institute, University of Michigan, Ann Arbor, MI, USA.ORCID http://orcid.org/0000-0002-7828-8118
Brenda A SchulmanDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA. schulman@biochem.mpg.de.ORCID http://orcid.org/0000-0002-3083-1126
St. Jude Children's Research Hospital · USBrigham and Women's Hospital · USUniversity of Michigan · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI MALCOLM S. CAPEL · 2018 to 2026
$34.2M
ALTERNATIVE VACUOLAR TARGETING MECHANISMS IN YEASTR01GM053396 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KLIONSKY, DANIEL J. · 1995 to 2018
$12.1M
The mechanism and regulation of autophagyR35GM131919 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DANIEL J. KLIONSKY · 2019 to 2026
$6.4M
Ubiquitin-like Protein Transfer CascadesR01GM069530 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHULMAN, BRENDA A · 2003 to 2013
$3.4M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
NCI NIH HHS P30 CA021765NCRR NIH HHS S10 RR029205NIGMS NIH HHS P30 GM124165NIGMS NIH HHS R01 GM053396NIGMS NIH HHS R01 GM069530NIGMS NIH HHS R35 GM131919NIH HHS S10 OD021527
6 · The paper itself

Abstract

Autophagy depends on the E2 enzyme, Atg3, functioning in a conserved E1-E2-E3 trienzyme cascade that catalyzes lipidation of Atg8-family ubiquitin-like proteins (UBLs). Molecular mechanisms underlying Atg8 lipidation remain poorly understood despite association of Atg3, the E1 Atg7, and the composite E3 Atg12-Atg5-Atg16 with pathologies including cancers, infections and neurodegeneration. Here, studying yeast enzymes, we report that an Atg3 element we term E123IR (E1, E2, and E3-interacting region) is an allosteric switch. NMR, biochemical, crystallographic and genetic data collectively indicate that in the absence of the enzymatic cascade, the Atg3

Indexed as

Allosteric RegulationAutophagyAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsCatalytic DomainCrystallography, X-RayLigasesModels, MolecularMutationProtein ConformationProtein Processing, Post-TranslationalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesUbiquitinsATG3 protein, S cerevisiaeATG8 protein, S cerevisiaeAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsLigasesSaccharomyces cerevisiae ProteinsUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesUbiquitins

Identifiers

PMID31399562
PMCPMC6689050
OpenAlexW2967262750

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.