Evidence map›Paper›PMID 23387437›Full record

ArticleTraffic (Copenhagen, Denmark)2013

Antagonistic control of lysosomal fusion by Rab14 and the Lyst-related protein LvsB.

Elena Kypri, Kristin Falkenstein, Arturo De Lozanne

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Lysosomal size matters.Traffic (Copenhagen, Denmark) · 2020
    Review
  6. Review
  7. Article
  8. Observational
  9. Article
  10. Cellular logistics · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
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 3 institutions in 2 countries.

Elena KypriSection of Molecular Cell & Developmental Biology and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.
Kristin Falkenstein
Arturo De Lozanne
Institut de Biologie Moléculaire et Cellulaire · FRMedicover Genetics (Cyprus)The University of Texas at Austin · US

Funding

MOLECULAR ANALYSIS OF CYTOKINESIS IN DICTYOSTELIUMR01GM048745 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI DE LOZANNE, ARTURO · 1998 to 2006
$1.9M
Interaction between Vibrio cholerae and Dictylostelium discoideumR21AI078136 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI DE LOZANNE, ARTURO, PAYNE, SHELLEY M. · 2009 to 2010
$411k
MOLECULAR ANALYSIS OF CYTOKINESIS IN DICTYOSTELIUMR29GM048745 · NIGMS · DUKE UNIVERSITY · PI DE LOZANNE, ARTURO · 1993 to 1997
–
NIAID NIH HHS AI078136NIAID NIH HHS R21 AI078136NIGMS NIH HHS GM48745NIGMS NIH HHS R01 GM048745
6 · The paper itself

Abstract

While loss of the protein Lyst causes abnormal lysosomes in patients with Chediak-Higashi syndrome, the contribution of Lyst to lysosome biology is not known. Previously we found that the Dictyostelium ortholog of Lyst, LvsB, is a cytosolic protein that associates with lysosomes and post-lysosomes to prevent their inappropriate fusion. Here we provide three lines of evidence that indicate that LvsB contributes to lysosome function by antagonizing the function of DdRab14, a protein that promotes homotypic fusion among lysosomes. (1) Instead of restricting DdRab14 to lysosomes, cells that lack LvsB expand DdRab14 localization to include post-lysosomes. (2) Expression of activated DdRab14 phenocopies the loss of LvsB, causing inappropriate heterotypic fusion between lysosomes and post-lysosomes and their subsequent enlargement. (3) Conversely, expression of inactivated DdRab14 suppresses the phenotype of LvsB null cells and restores their lysosomal size and segregation from post-lysosomes. Our data suggest a scenario where LvsB binds to late lysosomes and promotes the inactivation of DdRab14. This inactivation allows the lysosomes to mature into post-lysosomes for eventual secretion. We propose that human Lyst may function similarly to regulate Rab-dependent fusion of lysosomal compartments.

Indexed as

Biological TransportDictyosteliumEndosomesGreen Fluorescent ProteinsHeterocyclic Compounds, 4 or More RingsHumansLysosomesPhenotypePlasmidsProtozoan Proteinsrab GTP-Binding ProteinsVesicular Transport ProteinsGreen Fluorescent ProteinsHeterocyclic Compounds, 4 or More RingsLYST protein, humanProtozoan ProteinsRab14 protein, humanrab GTP-Binding Proteinsvacuolin-1Vesicular Transport Proteins

Identifiers

PMID23387437
PMCPMC3622840
OpenAlexW1508490324

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.