Evidence map›Paper›PMID 26330529›Full record

ArticleJournal of cell science2015

Failure of lysosome clustering and positioning in the juxtanuclear region in cells deficient in rapsyn.

Mohamed Aittaleb, Po-Ju Chen, Mohammed Akaaboune

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

12 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Measurement of Lysosome Positioning by Shell Analysis and Line Scan.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. AChRs Are Essential for the Targeting of Rapsyn to the Postsynaptic Membrane of NMJs in Living Mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    Article
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 1 institution in 1 country.

Mohamed AittalebDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Po-Ju ChenDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Mohammed AkaabouneDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA Program in Neuroscience, University of Michigan, Ann Arbor, MI 48109, USA makaabou@umich.edu.
University of Michigan–Ann Arbor · US

Funding

The Dynamics of Synaptic Component at the Neuromuscular Junction of Living AnimalR01NS047332 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI AKAABOUNE, MOHAMMED · 2003 to 2013
$2.7M
Effect of Calmodulin Kinase II-Related Anchoring Protein on the Stability of AChRR21NS082615 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI AKAABOUNE, MOHAMMED · 2013 to 2014
$426k
NINDS NIH HHS NS-047332NINDS NIH HHS NS-082615NINDS NIH HHS R01 NS047332NINDS NIH HHS R21 NS082615
6 · The paper itself

Abstract

Rapsyn, a scaffold protein, is required for the clustering of acetylcholine receptors (AChRs) at contacts between motor neurons and differentiating muscle cells. Rapsyn is also expressed in cells that do not express AChRs. However, its function in these cells remains unknown. Here, we show that rapsyn plays an AChR-independent role in organizing the distribution and mobility of lysosomes. In cells devoid of AChRs, rapsyn selectively induces the clustering of lysosomes at high density in the juxtanuclear region without affecting the distribution of other intracellular organelles. However, when the same cells overexpress AChRs, rapsyn is recruited away from lysosomes to colocalize with AChR clusters on the cell surface. In rapsyn-deficient (Rapsn(-/-)) myoblasts or cells overexpressing rapsyn mutants, lysosomes are scattered within the cell and highly dynamic. The increased mobility of lysosomes in Rapsn(-/-) cells is associated with a significant increase in lysosomal exocytosis, as evidenced by increased release of lysosomal enzymes and plasma membrane damage when cells were challenged with the bacterial pore-forming toxin streptolysin-O. These findings uncover a new link between rapsyn, lysosome positioning, exocytosis and plasma membrane integrity.

Indexed as

Bacterial ProteinsCell LineCell MembraneCell NucleusExocytosisLysosomesMuscle ProteinsMyoblastsReceptors, CholinergicStreptolysinsBacterial ProteinsMuscle Proteinsperipheral membrane protein 43KReceptors, Cholinergicstreptolysin OStreptolysinsClusteringExocytosisLysosomesMobilityRapsyn

Identifiers

PMID26330529
PMCPMC4631781
OpenAlexW1798673368

What OpenQuestion holds

Textmetadata
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.