Evidence map›Paper›PMID 25783203›Full record

ArticleTraffic (Copenhagen, Denmark)2015

Recruitment of VPS33A to HOPS by VPS16 Is Required for Lysosome Fusion with Endosomes and Autophagosomes.

Lena Wartosch, Ufuk Günesdogan, Stephen C Graham, J Paul Luzio

Open access · hybridAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

94 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
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  5. Review
  6. Late Endosome Transport by RILP-RAB7A Promotes Dendrite Arborization Independently of Degradation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
    Article
  7. Review
  8. Review
  9. Article
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  11. Late endosome transport by RILP-RAB7A promotes dendrite arborization.bioRxiv : the preprint server for biology · 2025
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
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34 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

4 authors at 2 institutions in 1 country.

Lena WartoschCambridge Institute for Medical Research and Department of Clinical Biochemistry, Wellcome Trust/MRC Building, University of Cambridge, Cambridge, CB2 0XY, UK.
Ufuk GünesdoganWellcome Trust/Cancer Research UK Gurdon Institute, University of Cambridge, Cambridge, CB2 1QN, UK.
Stephen C GrahamDepartment of Pathology, University of Cambridge, Cambridge, CB2 1QP, UK.
J Paul LuzioCambridge Institute for Medical Research and Department of Clinical Biochemistry, Wellcome Trust/MRC Building, University of Cambridge, Cambridge, CB2 0XY, UK.
University of Cambridge · GBWellcome/Cancer Research UK Gurdon Institute · GB

Funding

Medical Research Council G0900113Wellcome Trust 079919Wellcome Trust 093026Wellcome Trust 098406Wellcome Trust 098406/Z/12/ZWellcome Trust 100140
6 · The paper itself

Abstract

The mammalian homotypic fusion and vacuole protein sorting (HOPS) complex is comprised of six subunits: VPS11, VPS16, VPS18, VPS39, VPS41 and the Sec1/Munc18 (SM) family member VPS33A. Human HOPS has been predicted to be a tethering complex required for fusion of intracellular compartments with lysosomes, but it remains unclear whether all HOPS subunits are required. We showed that the whole HOPS complex is required for fusion of endosomes with lysosomes by monitoring the delivery of endocytosed fluorescent dextran to lysosomes in cells depleted of individual HOPS proteins. We used the crystal structure of the VPS16/VPS33A complex to design VPS16 and VPS33A mutants that no longer bind each other and showed that, unlike the wild-type proteins, these mutants no longer rescue lysosome fusion with endosomes or autophagosomes in cells depleted of the endogenous proteins. There was no effect of depleting either VIPAR or VPS33B, paralogs of VPS16 and VPS33A, on fusion of lysosomes with either endosomes or autophagosomes and immunoprecipitation showed that they form a complex distinct from HOPS. Our data demonstrate the necessity of recruiting the SM protein VPS33A to HOPS via its interaction with VPS16 and that HOPS proteins, but not VIPAR or VPS33B, are essential for fusion of endosomes or autophagosomes with lysosomes.

Indexed as

Amino Acid SequenceAutophagyEndosomesHeLa CellsHumansLysosomesMolecular Sequence DataPhagosomesProtein BindingProtein TransportVesicular Transport ProteinsVesicular Transport ProteinsVPS16 protein, humanVPS33A protein, humanautophagyCORVETendocytosisHOPSlysosomesSM proteintethering factorVPS16VPS33A

Identifiers

PMID25783203
PMCPMC4510706
OpenAlexW1534198965

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.