Evidence map›Paper›PMID 30397185›Full record

ReviewJournal of lipid research2019

VPS34 complexes from a structural perspective.

Yohei Ohashi, Shirley Tremel, Roger L Williams

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of lipid research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed, 1 pooled it
5.2field-weighted citation impact, top 4% 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

87 citing papers in PubMed, 1 synthesis or guideline pooled it, 131 citations in OpenAlex.

  1. Guideline
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Where and how do mammalian cells shape autophagosomes?The Journal of biological chemistry · 2026
    Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The human autophagy-initiating complexes ULK1C and PI3KC3-C1.The Journal of biological chemistry · 2025
    Review
  18. Article
  19. Article
  20. Review

27 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 at 1 institution in 1 country.

Yohei OhashiMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.ORCID 0000-0002-2288-130X
Shirley TremelMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.
Roger L WilliamsMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom rlw@mrc-lmb.cam.ac.uk.ORCID 0000-0001-7754-4207
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184308
6 · The paper itself

Abstract

VPS34 phosphorylates phosphatidylinositol to produce PtdIns3P and is the progenitor of the phosphoinositide 3-kinase (PI3K) family. VPS34 has a simpler domain organization than class I PI3Ks, which belies the complexity of its quaternary organization, with the enzyme always functioning within larger assemblies. PtdIns3P recruits specific recognition modules that are common in protein-sorting pathways, such as autophagy and endocytic sorting. It is best characterized in two heterotetramers, complexes I and II. Complex I is composed of VPS34, VPS15, Beclin 1, and autophagy-related gene (ATG)14L, whereas complex II replaces ATG14L with UVRAG. Because VPS34 can form a component of several distinct complexes, it enables independent regulation of various pathways that are controlled by PtdIns3P. Complexes I and II are critical for early events in autophagy and endocytic sorting, respectively. Autophagy has a complex association with cancer. In early stages, it inhibits tumorigenesis, but in later stages, it acts as a survival factor for tumors. Recently, various disease-associated somatic mutations were found in genes encoding complex I and II subunits. Lipid kinase activities of the complexes are also influenced by posttranslational modifications (PTMs). Mapping PTMs and somatic mutations on three-dimensional models of the complexes suggests mechanisms for how these affect VPS34 activity.

Indexed as

Class III Phosphatidylinositol 3-KinasesEndocytosisEnzyme InhibitorsHumansProtein Processing, Post-TranslationalClass III Phosphatidylinositol 3-KinasesEnzyme Inhibitorscryo-electron microscopyhydrogen-deuterium exchange mass-spectrometrylipidvacuolar protein sorting 34X-ray crystallography

Identifiers

PMID30397185
PMCPMC6358306
OpenAlexW2900435357

What Socratic 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 Socratic graph.