Evidence map›Paper›PMID 26975849›Full record

ArticleThe Journal of cell biology2016

The position of lysosomes within the cell determines their luminal pH.

Danielle E Johnson, Philip Ostrowski, Valentin Jaumouillé, Sergio Grinstein

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 344 papers.

0numbers the graph read from it
0cells of the map it votes in
344citing papers in PubMed
41.0field-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

344 citing papers in PubMed, 593 citations in OpenAlex.

  1. Article
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  4. Ion transport as a determinant of membrane fusion and fission.Nature structural & molecular biology · 2026
    Review
  5. The molecular and functional interplay between the osteopetrosis-associated proteins SNX10, OSTM1, and CLC-7 during mouse osteoclastogenesis.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2026
    Article
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284 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Danielle E JohnsonProgram in Cell Biology, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada.
Philip OstrowskiProgram in Cell Biology, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada.
Valentin JaumouilléProgram in Cell Biology, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada.
Sergio GrinsteinProgram in Cell Biology, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada sergio.grinstein@sickkids.ca.
Hospital for Sick Children · CA

Funding

Canadian Institutes of Health Research FDN-143202
6 · The paper itself

Abstract

We examined the luminal pH of individual lysosomes using quantitative ratiometric fluorescence microscopy and report an unappreciated heterogeneity: peripheral lysosomes are less acidic than juxtanuclear ones despite their comparable buffering capacity. An increased passive (leak) permeability to protons, together with reduced vacuolar H(+)-adenosine triphosphatase (V-ATPase) activity, accounts for the reduced acidifying ability of peripheral lysosomes. The altered composition of peripheral lysosomes is due, at least in part, to more limited access to material exported by the biosynthetic pathway. The balance between Rab7 and Arl8b determines the subcellular localization of lysosomes; more peripheral lysosomes have reduced Rab7 density. This in turn results in decreased recruitment of Rab-interacting lysosomal protein (RILP), an effector that regulates the recruitment and stability of the V1G1 component of the lysosomal V-ATPase. Deliberate margination of lysosomes is associated with reduced acidification and impaired proteolytic activity. The heterogeneity in lysosomal pH may be an indication of a broader functional versatility.

Indexed as

Adaptor Proteins, Signal TransducingADP-Ribosylation FactorsBiosynthetic PathwaysCell Line, TumorHeLa CellsHumansHydrogen-Ion ConcentrationLysosomesrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsVacuolar Proton-Translocating ATPasesVacuolesAdaptor Proteins, Signal TransducingADP-Ribosylation FactorsARL8B protein, humanATP6V1G1 protein, humanrab7 GTP-Binding Proteinsrab7 GTP-binding proteins, humanrab GTP-Binding ProteinsRILP protein, humanVacuolar Proton-Translocating ATPases

Identifiers

PMID26975849
PMCPMC4792074
OpenAlexW2322556561

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.