Evidence map›Paper›PMID 29114050›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Structure and function of yeast Atg20, a sorting nexin that facilitates autophagy induction.

Hana Popelka, Alejandro Damasio, Jenny E Hinshaw, Daniel J Klionsky, Michael J Ragusa

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
3.1field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.

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  17. Small but mighty: Atg8s and Rabs in membrane dynamics during autophagy.Biochimica et biophysica acta. Molecular cell research · 2021
    Review
  18. Article
  19. YPIBP: A repository for phosphoinositide-binding proteins in yeast.Computational and structural biotechnology journal · 2021
    Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Hana PopelkaLife Sciences Institute, University of Michigan, Ann Arbor, MI 48109.
Alejandro DamasioDepartment of Chemistry, Dartmouth College, Hanover, NH 03755.
Jenny E HinshawLaboratory of Cell and Molecular Biology, National Institutes of Health, Bethesda, MD 20892.
Daniel J KlionskyLife Sciences Institute, University of Michigan, Ann Arbor, MI 48109; klionsky@umich.edu michael.j.ragusa@dartmouth.edu.
Michael J RagusaDepartment of Chemistry, Dartmouth College, Hanover, NH 03755; klionsky@umich.edu michael.j.ragusa@dartmouth.edu.ORCID 0000-0002-0231-0876
Dartmouth College · USUniversity of Michigan · USNational Institutes of Health · US

Funding

Understanding the role of RNA-binding protein mutations in cancerP20GM113132 · NIGMS · DARTMOUTH COLLEGE · PI MADDEN, DEAN R · 2016 to 2025
$25.9M
Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
ALTERNATIVE VACUOLAR TARGETING MECHANISMS IN YEASTR01GM053396 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KLIONSKY, DANIEL J. · 1995 to 2018
$12.1M
NIGMS NIH HHS P20 GM113132NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R01 GM053396
6 · The paper itself

Abstract

The Atg20 and Snx4/Atg24 proteins have been identified in a screen for mutants defective in a type of selective macroautophagy/autophagy. Both proteins are connected to the Atg1 kinase complex, which is involved in autophagy initiation, and bind phosphatidylinositol-3-phosphate. Atg20 and Snx4 contain putative BAR domains, suggesting a possible role in membrane deformation, but they have been relatively uncharacterized. Here we demonstrate that, in addition to its function in selective autophagy, Atg20 plays a critical role in the efficient induction of nonselective autophagy. Atg20 is a dynamic posttranslationally modified protein that engages both structurally stable (PX and BAR) and intrinsically disordered domains for its function. In addition to its PX and BAR domains, Atg20 uses a third membrane-binding module, a membrane-inducible amphipathic helix present in a previously undescribed location in Atg20 within the putative BAR domain. Taken together, these findings yield insights into the molecular mechanism of the autophagy machinery.

Indexed as

Gene Expression Regulation, FungalAmino Acid MotifsAutophagyAutophagy-Related ProteinsBinding SitesCloning, MolecularEscherichia coliGene ExpressionGenetic VectorsKineticsModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsRecombinant ProteinsAtg20 protein, S cerevisiaeAutophagy-Related ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSorting Nexinsautophagyvacuoleyeast

Identifiers

PMID29114050
PMCPMC5703286
OpenAlexW2767676388

What OpenQuestion holds

Textmetadata
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.