Evidence map›Paper›PMID 27050455›Full record

ArticleAutophagy2016

Phosphorylation of Atg9 regulates movement to the phagophore assembly site and the rate of autophagosome formation.

Yuchen Feng, Steven K Backues, Misuzu Baba, Jin-mi Heo, J Wade Harper, Daniel J Klionsky

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed, 1 pooled it
7.9field-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

50 citing papers in PubMed, 1 synthesis or guideline pooled it, 80 citations in OpenAlex.

  1. The multiple roles of autophagy in uveal melanoma and the microenvironment.Journal of cancer research and clinical oncology · 2024
    Pooled it
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  4. Mec1-mediated Atg9 phosphorylation regulates the PAS recruitment of Atg9 vesicles upon energy stress.Proceedings of the National Academy of Sciences of the United States of America · 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.

Yuchen Fenga Life Sciences Institute and the Department of Molecular, Cellular and Developmental Biology, University of Michigan , Ann Arbor , MI , USA.
Steven K Backuesa Life Sciences Institute and the Department of Molecular, Cellular and Developmental Biology, University of Michigan , Ann Arbor , MI , USA.
Misuzu Babab Research Institute for Science and Technology, Kogakuin University , Tokyo , Japan.
Jin-mi Heoc Department of Cell Biology , Harvard Medical School , Boston , MA USA.
J Wade Harperc Department of Cell Biology , Harvard Medical School , Boston , MA USA.
Daniel J Klionskya Life Sciences Institute and the Department of Molecular, Cellular and Developmental Biology, University of Michigan , Ann Arbor , MI , USA.
University of Michigan · USHarvard University · USKogakuin University · JP

Funding

ALTERNATIVE VACUOLAR TARGETING MECHANISMS IN YEASTR01GM053396 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KLIONSKY, DANIEL J. · 1995 to 2018
$12.1M
Network organization of the human autophagy systemR01GM095567 · NIGMS · HARVARD MEDICAL SCHOOL · PI HARPER, JEFFREY W, KIMMELMAN, ALEC · 2011 to 2018
$3.0M
NIGMS NIH HHS GM053396NIGMS NIH HHS GM095567NIGMS NIH HHS R01 GM053396NIGMS NIH HHS R01 GM095567
6 · The paper itself

Abstract

Macroautophagy is primarily a degradative process that cells use to break down their own components to recycle macromolecules and provide energy under stress conditions, and defects in macroautophagy lead to a wide range of diseases. Atg9, conserved from yeast to mammals, is the only identified transmembrane protein in the yeast core macroautophagy machinery required for formation of the sequestering compartment termed the autophagosome. This protein undergoes dynamic movement between the phagophore assembly site (PAS), where the autophagosome precursor is nucleated, and peripheral sites that may provide donor membrane for expansion of the phagophore. Atg9 is a phosphoprotein that is regulated by the Atg1 kinase. We used stable isotope labeling by amino acids in cell culture (SILAC) to identify phosphorylation sites on this protein and identified an Atg1-independent phosphorylation site at serine 122. A nonphosphorylatable Atg9 mutant showed decreased autophagy activity, whereas the phosphomimetic mutant enhanced activity. Electron microscopy analysis suggests that the different levels of autophagy activity reflect differences in autophagosome formation, correlating with the delivery of Atg9 to the PAS. Finally, this phosphorylation regulates Atg9 interaction with Atg23 and Atg27.

Indexed as

AutophagyAmino Acid SequenceAutophagosomesAutophagy-Related ProteinsMembrane ProteinsPhosphorylationPhosphoserineProtein BindingProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsATG9 protein, S cerevisiaeAutophagy-Related ProteinsMembrane ProteinsPhosphoserineSaccharomyces cerevisiae Proteinsautophagylysosomestressvacuoleyeast

Identifiers

PMID27050455
PMCPMC4835963
OpenAlexW2318418872

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.