Evidence map›Paper›PMID 31351898›Full record

ReviewJournal of molecular biology2020

Recruitment and Activation of the ULK1/Atg1 Kinase Complex in Selective Autophagy.

Eleonora Turco, Dorotea Fracchiolla, Sascha Martens

Abstract readReview
In one paragraph

Review in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing 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

67 citing papers in PubMed.

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7 more citing papers are in PubMed but not listed here.

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

3 authors.

Eleonora TurcoDepartment of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9/5, 1030 Vienna, Austria. Electronic address: eleonora.turco@univie.ac.at.
Dorotea FracchiollaDepartment of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9/5, 1030 Vienna, Austria. Electronic address: dorotea.fracchiolla@univie.ac.at.
Sascha MartensDepartment of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9/5, 1030 Vienna, Austria. Electronic address: sascha.martens@univie.ac.at.

Funding

Austrian Science Fund FWF P 30401Austrian Science Fund FWF W 1261
6 · The paper itself

Abstract

Autophagy is a major cellular degradation pathway, which mediates the delivery of cytoplasmic cargo material into lysosomes. This is achieved by the specific sequestration of the cargo within double-membrane vesicles, the autophagosomes, which form de novo around this material. Autophagosome formation requires the action of a conserved set of factors, which act in hierarchical manner. The ULK1/Atg1 kinase complex is one of the most upstream acting components of the autophagy machinery. Here we discuss recent insights into the mechanisms of ULK1/Atg1 recruitment and activation at the cargo during selective autophagy. In particular, we will focus on the role of cargo receptors such as p62 and NDP52 during this process and discuss the emerging concept that cargo receptors act upstream of the autophagy machinery during cargo-induced selective autophagy.

Indexed as

AutophagyAnimalsAutophagosomesAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsEnzyme ActivationHumansLysosomesMacroautophagyPhosphorylationProtein KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsATG1 protein, S cerevisiaeAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsProtein KinasesSaccharomyces cerevisiae Proteinsautophagosomecargo receptorprotein kinasequality controlsignaling

Identifiers

PMID31351898
PMCPMC6971721

What OpenQuestion holds

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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.