Evidence map›Paper›PMID 28301741›Full record

ReviewAnnual review of biochemistry2017

Mechanisms of Autophagy Initiation.

James H Hurley, Lindsey N Young

Abstract readReview
In one paragraph

Review in Annual review of biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 398 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
398citing papers in PubMed, 3 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

398 citing papers in PubMed, 3 syntheses or guidelines pooled it.

  1. Pooled it
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  20. The Roles of SQSTM1/p62 in Selective Autophagy and Oncogenic Signaling.International journal of molecular sciences · 2026
    Review

338 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.

James H HurleyDepartment of Molecular and Cell Biology and California Institute of Quantitative Biosciences, University of California, Berkeley, California, and Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California, 94720; email: jimhurley@berkeley.edu.
Lindsey N YoungDepartment of Molecular and Cell Biology and California Institute of Quantitative Biosciences, University of California, Berkeley, California, and Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California, 94720; email: jimhurley@berkeley.edu.

Funding

TUBULIN STRUCTURE BY ELECTRON CRYSTALLOGRAPHYP01GM051487 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI CATE, JAMIE H · 1994 to 2018
$27.6M
The Autophagy Initiation ComplexesR01GM111730 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HURLEY, JAMES H · 2014 to 2021
$2.2M
NIGMS NIH HHS P01 GM051487NIGMS NIH HHS R01 GM111730
6 · The paper itself

Abstract

Autophagy is the process of cellular self-eating by a double-membrane organelle, the autophagosome. A range of signaling processes converge on two protein complexes to initiate autophagy: the ULK1 (unc51-like autophagy activating kinase 1) protein kinase complex and the PI3KC3-C1 (class III phosphatidylinositol 3-kinase complex I) lipid kinase complex. Some 90% of the mass of these large protein complexes consists of noncatalytic domains and subunits, and the ULK1 complex has essential noncatalytic activities. Structural studies of these complexes have shed increasing light on the regulation of their catalytic and noncatalytic activities in autophagy initiation. The autophagosome is thought to nucleate from vesicles containing the integral membrane protein Atg9 (autophagy-related 9), COPII (coat protein complex II) vesicles, and possibly other sources. In the wake of reconstitution and super-resolution imaging studies, we are beginning to understand how the ULK1 and PI3KC3-C1 complexes might coordinate the nucleation and fusion of Atg9 and COPII vesicles at the start of autophagosome biogenesis.

Indexed as

AutophagyAutophagy-Related Protein-1 HomologCell MembraneClass III Phosphatidylinositol 3-KinasesCOP-Coated VesiclesEukaryotic CellsGene ExpressionGene Expression RegulationHumansIntracellular Signaling Peptides and ProteinsPhagosomesPhosphatidylinositol 3-KinaseProtein BindingProtein MultimerizationSignal TransductionAutophagy-Related Protein-1 HomologClass III Phosphatidylinositol 3-KinasesIntracellular Signaling Peptides and ProteinsPhosphatidylinositol 3-KinaseULK1 protein, humanAtg1COPIImembrane fusionmembrane remodelingnanoscale biologyphosphatidylinositol 3-kinasetethering complexULK1vesicleVps34

Identifiers

PMID28301741
PMCPMC5604869

What OpenQuestion holds

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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.