Evidence map›Paper›PMID 21525240›Full record

ArticleMolecular biology of the cell2011

Role of AP1 and Gadkin in the traffic of secretory endo-lysosomes.

Karine Laulagnier, Nicole L Schieber, Tanja Maritzen, Volker Haucke, Robert G Parton, Jean Gruenberg

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Protein sorting from endosomes to the TGN.Frontiers in cell and developmental biology · 2023
    Review
  8. Loss of Christianson Syndrome NaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Mutant Huntingtin Is Secreted via a Late Endosomal/Lysosomal Unconventional Secretory Pathway.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  16. Article
  17. Protective responses to sublytic complement in the retinal pigment epithelium.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. Article
  19. Article
  20. 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

6 authors at 3 institutions in 3 countries.

Karine LaulagnierDepartment of Biochemistry, University of Geneva, Switzerland.
Nicole L Schieber
Tanja Maritzen
Volker Haucke
Robert G Parton
Jean Gruenberg
Freie Universität Berlin · DEThe University of Queensland · AUUniversity of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Whereas lysosome-related organelles (LRO) of specialized cells display both exocytic and endocytic features, lysosomes in nonspecialized cells can also acquire the property to fuse with the plasma membrane upon an acute rise in cytosolic calcium. Here, we characterize this unconventional secretory pathway in fibroblast-like cells, by monitoring the appearance of Lamp1 on the plasma membrane and the release of lysosomal enzymes into the medium. After sequential ablation of endocytic compartments in living cells, we find that donor membranes primarily derive from a late compartment, but that an early compartment is also involved. Strikingly, this endo-secretory process is not affected by treatments that inhibit endosome dynamics (microtubule depolymerization, cholesterol accumulation, overexpression of Rab7 or its effector Rab-interacting lysosomal protein [RILP], overexpression of Rab5 mutants), but depends on Rab27a, a GTPase involved in LRO secretion, and is controlled by F-actin. Moreover, we find that this unconventional endo-secretory pathway requires the adaptor protein complexes AP1, Gadkin (which recruits AP1 by binding to the γ1 subunit), and AP2, but not AP3. We conclude that a specific fraction of the AP2-derived endocytic pathway is dedicated to secretory purposes under the control of AP1 and Gadkin.

Indexed as

ActinsAdaptor Protein Complex 1AnimalsBiological TransportCricetinaeCytosolEndocytosisEndosomesExocytosisFibroblastsHexosaminidasesHumansLysosomal-Associated Membrane Protein 1Lysosomal Membrane ProteinsLysosomesMembrane ProteinsActinsAdaptor Protein Complex 1AP1AR protein, humanHexosaminidasesLAMP1 protein, humanLysosomal-Associated Membrane Protein 1Lysosomal Membrane ProteinsMembrane ProteinsRAB27A protein, humanrab27 GTP-Binding Proteinsrab GTP-Binding Proteins

Identifiers

PMID21525240
PMCPMC3113771
OpenAlexW2051056059

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.