Evidence map›Paper›PMID 26565778›Full record

ArticleAutophagy2015

Atg41/Icy2 regulates autophagosome formation.

Zhiyuan Yao, Elizabeth Delorme-Axford, Steven K Backues, Daniel J Klionsky

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed, 2 pooled it
6.1field-weighted citation impact, top 3% 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

56 citing papers in PubMed, 2 syntheses or guidelines pooled it, 88 citations in OpenAlex.

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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

4 authors at 3 institutions in 1 country.

Zhiyuan Yaoa Life Sciences Institute and Department of Molecular, Cellular and Developmental Biology ; University of Michigan ; Ann Arbor , MI USA.
Elizabeth Delorme-Axforda Life Sciences Institute and Department of Molecular, Cellular and Developmental Biology ; University of Michigan ; Ann Arbor , MI USA.
Steven K Backuesb Department of Chemistry ; Eastern Michigan University ; Ypsilanti , MI USA.
Daniel J Klionskya Life Sciences Institute and Department of Molecular, Cellular and Developmental Biology ; University of Michigan ; Ann Arbor , MI USA.
Ann Arbor Center for Independent Living · USEastern Michigan University · USUniversity of Michigan–Ann Arbor · US

Funding

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 GM053396NIGMS NIH HHS R01 GM053396
6 · The paper itself

Abstract

Macroautophagy (hereafter autophagy) is one of the major degradation systems in eukaryotic cells, and its dysfunction may result in diseases ranging from neurodegeneration to cancer. Although most of the autophagy-related (Atg) proteins that function in this pathway were first identified in yeast, many were subsequently shown to have homologs in higher eukaryotes including humans, and the overall mechanism of autophagy is highly conserved. The most prominent feature of autophagy is the formation of a double-membrane sequestering compartment, the phagophore; this transient organelle surrounds part of the cytoplasm and matures into an autophagosome, which subsequently fuses with the vacuole or lysosome to allow degradation of the cargo. Much attention has focused on the process involved in phagophore nucleation and expansion, but many questions remain. Here, we identified the yeast protein Icy2, which we now name Atg41, as playing a role in autophagosome formation. Atg41 interacts with the transmembrane protein Atg9, a key component involved in autophagosome biogenesis, and both proteins display a similar localization profile. Under autophagy-inducing conditions the expression level of Atg41 increases dramatically and is regulated by the transcription factor Gcn4. This work provides further insight into the mechanism of Atg9 function and the dynamics of sequestering membrane formation during autophagy.

Indexed as

AutophagyCarrier ProteinsLysosomesPhagosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesCarrier ProteinsIcy2 protein, S cerevisiaeSaccharomyces cerevisiae Proteinsautophagylysosomestressvacuoleyeast

Identifiers

PMID26565778
PMCPMC4835205
OpenAlexW2173437641

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.