Evidence map›Paper›PMID 26450213›Full record

ArticleScience (New York, N.Y.)2015

Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes.

Ksenia Rostislavleva, Nicolas Soler, Yohei Ohashi, Lufei Zhang, Els Pardon, John E Burke, Glenn R Masson, Chris Johnson, Jan Steyaert, Nicholas T Ktistakis and 1 more

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
152citing papers in PubMed, 1 pooled it
13.1field-weighted citation impact, top 1% 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

152 citing papers in PubMed, 1 synthesis or guideline pooled it, 235 citations in OpenAlex.

  1. Guideline
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. The ATG14: multi-layer autophagy control and an emerging therapeutic target in cancer.Apoptosis : an international journal on programmed cell death · 2026
    Review
  10. Article
  11. Article
  12. The Biological Role and Clinical Significance of BECLIN-1 in Cancer.International journal of molecular sciences · 2025
    Review
  13. The human autophagy-initiating complexes ULK1C and PI3KC3-C1.The Journal of biological chemistry · 2025
    Review
  14. Article
  15. Making PI3K superfamily enzymes run faster.Advances in biological regulation · 2025
    Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Review

92 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

11 authors at 4 institutions in 2 countries.

Ksenia Rostislavleva *MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Nicolas Soler *MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Yohei OhashiMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Lufei ZhangMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Els PardonStructural Biology Research Center, VIB, B-1050 Brussels, Belgium.
John E BurkeMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Glenn R MassonMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Chris JohnsonMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Jan SteyaertStructural Biology Research Center, VIB, B-1050 Brussels, Belgium.
Nicholas T KtistakisThe Babraham Institute, Cambridge UK.
Roger L WilliamsMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Medical Research Council · GBMRC Laboratory of Molecular Biology · GBVrije Universiteit Brussel · BEBabraham Institute · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K019155/1Biotechnology and Biological Sciences Research Council BBS/E/B/00001221British Heart Foundation PG/11/109/29247British Heart Foundation PG11/109/29247Medical Research Council MC_U105184308Medical Research Council U105184308
6 · The paper itself

Abstract

Phosphatidylinositol 3-kinase Vps34 complexes regulate intracellular membrane trafficking in endocytic sorting, cytokinesis, and autophagy. We present the 4.4 angstrom crystal structure of the 385-kilodalton endosomal complex II (PIK3C3-CII), consisting of Vps34, Vps15 (p150), Vps30/Atg6 (Beclin 1), and Vps38 (UVRAG). The subunits form a Y-shaped complex, centered on the Vps34 C2 domain. Vps34 and Vps15 intertwine in one arm, where the Vps15 kinase domain engages the Vps34 activation loop to regulate its activity. Vps30 and Vps38 form the other arm that brackets the Vps15/Vps34 heterodimer, suggesting a path for complex assembly. We used hydrogen-deuterium exchange mass spectrometry (HDX-MS) to reveal conformational changes accompanying membrane binding and identify a Vps30 loop that is critical for the ability of complex II to phosphorylate giant liposomes on which complex I is inactive.

Indexed as

Cell MembraneClass III Phosphatidylinositol 3-KinasesCrystallography, X-RayEndosomesProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiarySaccharomyces cerevisiaeVacuolar Sorting Protein VPS15Class III Phosphatidylinositol 3-KinasesVacuolar Sorting Protein VPS15

Identifiers

PMID26450213
PMCPMC4601532
OpenAlexW2214645750

What OpenQuestion holds

Textmetadata
LicenceTDM
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.