Evidence map›Paper›PMID 29799763›Full record

ArticleAutophagy2018

An atypical BAR domain protein in autophagy.

Hana Popelka, Daniel J Klionsky, Michael J Ragusa

Abstract readComment
PubMed Full text at PMC Publisher
In one paragraph

Article in Autophagy, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Hana Popelkaa Life Sciences Institute , University of Michigan , Ann Arbor , MI USA.
Daniel J Klionskya Life Sciences Institute , University of Michigan , Ann Arbor , MI USA.ORCID 0000-0002-7828-8118
Michael J Ragusac Department of Chemistry , Dartmouth College , Hanover , NH USA.ORCID 0000-0002-0231-0876

Funding

Understanding the role of RNA-binding protein mutations in cancerP20GM113132 · NIGMS · DARTMOUTH COLLEGE · PI MADDEN, DEAN R · 2016 to 2025
$25.9M
NIGMS NIH HHS P20 GM113132
6 · The paper itself

Abstract

The sorting nexin Atg20 interacts with the selective macroautophagy/autophagy scaffolding protein Atg11, suggesting an important role for Atg20 in the initiation of selective autophagy. To explore this possibility, we recently investigated the structure and function of Atg20 using a variety of biophysical and yeast genetic approaches. Our data demonstrate that the BAR domain of Atg20 interacts with Snx4/Atg24 to form an asymmetric heterodimeric BAR domain complex. Atg20 also contains a long intrinsically disordered N terminus that facilitates binding to Atg11 and a large 89-amino acid insertion in its BAR domain, which we have termed the BAR-GAP. This BAR-GAP region is a unique feature of Atg20 and has not been observed in other BAR domains. Furthermore, the BAR-GAP of Atg20 contains an amphipathic helix which is required for membrane binding, tubulation and autophagy. Our findings demonstrate the important role of this novel region in autophagy.

Indexed as

AutophagySaccharomyces cerevisiae ProteinsAutophagy-Related ProteinsSaccharomyces cerevisiaeSorting NexinsVesicular Transport ProteinsAtg11 protein, S cerevisiaeAutophagy-Related ProteinsSaccharomyces cerevisiae ProteinsSorting NexinsVesicular Transport Proteinsamphipathic helixelectron microscopySAXSstructurevacuoleyeast

Identifiers

PMID29799763
PMCPMC6103713

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.