Evidence map›Paper›PMID 29233870›Full record

ReviewEssays in biochemistry2017

The mammalian ULK1 complex and autophagy initiation.

Maria Zachari, Ian G Ganley

Abstract readReview
In one paragraph

Review in Essays in biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 494 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
494citing papers in PubMed, 1 pooled it
–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

494 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  14. The Human Autophagy Core Complexes.Annual review of biochemistry · 2026
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434 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

2 authors.

Maria ZachariMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
Ian G GanleyMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K. i.ganley@dundee.ac.uk.

Funding

Medical Research Council MC_UU_12016/4
6 · The paper itself

Abstract

Autophagy is a vital lysosomal degradation pathway that serves as a quality control mechanism. It rids the cell of damaged, toxic or excess cellular components, which if left to persist could be detrimental to the cell. It also serves as a recycling pathway to maintain protein synthesis under starvation conditions. A key initial event in autophagy is formation of the autophagosome, a unique double-membrane organelle that engulfs the cytosolic cargo destined for degradation. This step is mediated by the serine/threonine protein kinase ULK1 (unc-51-like kinase 1), which functions in a complex with at least three protein partners: FIP200 (focal adhesion kinase family interacting protein of 200 kDa), ATG (autophagy-related protein) 13 (ATG13), and ATG101. In this artcile, we focus on the regulation of the ULK1 complex during autophagy initiation. The complex pattern of upstream pathways that converge on ULK1 suggests that this complex acts as a node, converting multiple signals into autophagosome formation. Here, we review our current understanding of this regulation and in turn discuss what happens downstream, once the ULK1 complex becomes activated.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsAutophagyAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsHumansProtein-Tyrosine KinasesVesicular Transport ProteinsAdaptor Proteins, Signal TransducingAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsProtein-Tyrosine KinasesVesicular Transport ProteinsautophagykinaseULK1

Identifiers

PMID29233870
PMCPMC5869855

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.