Evidence map›Paper›PMID 27113757›Full record

ArticleEMBO reports2016

Folliculin directs the formation of a Rab34-RILP complex to control the nutrient-dependent dynamic distribution of lysosomes.

Georgina P Starling, Yan Y Yip, Anneri Sanger, Penny E Morton, Emily R Eden, Mark P Dodding

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

60 citing papers in PubMed, 99 citations in OpenAlex.

  1. 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
  2. Review
  3. Late endosome transport by RILP-RAB7A promotes dendrite arborization.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
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  6. Review
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  12. Article
  13. Membrane trafficking alterations in breast cancer progression.Frontiers in cell and developmental biology · 2024
    Review
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  15. Article
  16. Article
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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

6 authors at 2 institutions in 1 country.

Georgina P StarlingRandall Division of Cell and Molecular Biophysics, King's College London, London, UK.
Yan Y YipRandall Division of Cell and Molecular Biophysics, King's College London, London, UK.
Anneri SangerRandall Division of Cell and Molecular Biophysics, King's College London, London, UK.
Penny E MortonRandall Division of Cell and Molecular Biophysics, King's College London, London, UK.
Emily R EdenInstitute of Ophthalmology, University College London, London, UK.
Mark P DoddingRandall Division of Cell and Molecular Biophysics, King's College London, London, UK mark.dodding@kcl.ac.uk.
King's College London · GBUniversity College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L006774/1Medical Research Council MR/M010767/1Wellcome Trust 097316
6 · The paper itself

Abstract

The spatial distribution of lysosomes is important for their function and is, in part, controlled by cellular nutrient status. Here, we show that the lysosome associated Birt-Hoge-Dubé (BHD) syndrome renal tumour suppressor folliculin (FLCN) regulates this process. FLCN promotes the peri-nuclear clustering of lysosomes following serum and amino acid withdrawal and is supported by the predominantly Golgi-associated small GTPase Rab34. Rab34-positive peri-nuclear membranes contact lysosomes and cause a reduction in lysosome motility and knockdown of FLCN inhibits Rab34-induced peri-nuclear lysosome clustering. FLCN interacts directly via its C-terminal DENN domain with the Rab34 effector RILP Using purified recombinant proteins, we show that the FLCN-DENN domain does not act as a GEF for Rab34, but rather, loads active Rab34 onto RILP We propose a model whereby starvation-induced FLCN association with lysosomes drives the formation of contact sites between lysosomes and Rab34-positive peri-nuclear membranes that restrict lysosome motility and thus promote their retention in this region of the cell.

Indexed as

Adaptor Proteins, Signal TransducingCarrier ProteinsCell LineEstroneGene ExpressionGolgi ApparatusHumansIntracellular MembranesLysosomesNuclear ProteinsProtein BindingProtein TransportProto-Oncogene Proteinsrab GTP-Binding ProteinsRecombinant ProteinsSignal TransductionAdaptor Proteins, Signal TransducingCarrier ProteinsEstroneFLCN protein, humanNuclear ProteinsProto-Oncogene ProteinsRAB34 protein, humanrab GTP-Binding ProteinsRecombinant ProteinsRILP protein, humanTumor Suppressor ProteinsBHD syndromefolliculinlysosomeRab34RILP

Identifiers

PMID27113757
PMCPMC4893818
OpenAlexW2340271424

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.