Evidence map›Paper›PMID 32602837›Full record

ArticleeLife2020

Membrane characteristics tune activities of endosomal and autophagic human VPS34 complexes.

Yohei Ohashi, Shirley Tremel, Glenn Robert Masson, Lauren McGinney, Jerome Boulanger, Ksenia Rostislavleva, Christopher M Johnson, Izabella Niewczas, Jonathan Clark, Roger L Williams

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  5. The human autophagy-initiating complexes ULK1C and PI3KC3-C1.The Journal of biological chemistry · 2025
    Review
  6. Making PI3K superfamily enzymes run faster.Advances in biological regulation · 2025
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Yohei Ohashi *MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom.ORCID 0000-0002-2288-130X
Shirley Tremel *MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom.ORCID 0000-0002-4077-0021
Glenn Robert MassonMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom.ORCID 0000-0002-1386-4719
Lauren McGinneyMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom.
Jerome BoulangerMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom.
Ksenia RostislavlevaMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom.
Christopher M JohnsonMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom.
Izabella NiewczasBabraham Institute, Cambridge, United Kingdom.
Jonathan ClarkBabraham Institute, Cambridge, United Kingdom.
Roger L WilliamsMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, United Kingdom.ORCID 0000-0001-7754-4207
MRC Laboratory of Molecular Biology · GBBabraham Institute · GB

Funding

Cancer Research UK C14801/A21211Medical Research Council MC-A024-5PF9LMedical Research Council MC_U105184308Medical Research Council MC_U105184326MRF_ MRF-113-0001-F-BOULA
6 · The paper itself

Abstract

The lipid kinase VPS34 orchestrates diverse processes, including autophagy, endocytic sorting, phagocytosis, anabolic responses and cell division. VPS34 forms various complexes that help adapt it to specific pathways, with complexes I and II being the most prominent ones. We found that physicochemical properties of membranes strongly modulate VPS34 activity. Greater unsaturation of both substrate and non-substrate lipids, negative charge and curvature activate VPS34 complexes, adapting them to their cellular compartments. Hydrogen/deuterium exchange mass spectrometry (HDX-MS) of complexes I and II on membranes elucidated structural determinants that enable them to bind membranes. Among these are the Barkor/ATG14L autophagosome targeting sequence (BATS), which makes autophagy-specific complex I more active than the endocytic complex II, and the Beclin1 BARA domain. Interestingly, even though Beclin1 BARA is common to both complexes, its membrane-interacting loops are critical for complex II, but have only a minor role for complex I.

Indexed as

AutophagyEndosomesCell MembraneClass III Phosphatidylinositol 3-KinasesHumansClass III Phosphatidylinositol 3-Kinasesautophagybiochemistrychemical biologyendocytosishumanmembrane defectsmolecular biophysicsphosphoinositide 3-kinasephospholipidssortingstructural biology

Identifiers

PMID32602837
PMCPMC7326497
OpenAlexW3039246668

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.