Evidence map›Paper›PMID 16874303›Full record

ArticleThe EMBO journal2006

Intersectin-1L nucleotide exchange factor regulates secretory granule exocytosis by activating Cdc42.

Magali Malacombe, Mara Ceridono, Valérie Calco, Sylvette Chasserot-Golaz, Peter S McPherson, Marie-France Bader, Stéphane Gasman

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.5field-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

45 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Review
  3. Phospholipid Scramblase 1 Controls Efficient Neurotransmission and Synaptic Vesicle Retrieval at Cerebellar Synapses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  4. Review
  5. MYO1F Regulates IgE and MRGPRX2-Dependent Mast Cell Exocytosis.Journal of immunology (Baltimore, Md. : 1950) · 2021
    Article
  6. Review
  7. Article
  8. Gene Expression Profiling of Type 2 Diabetes Mellitus by Bioinformatics Analysis.Computational and mathematical methods in medicine · 2020
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Intersectin scaffold proteins and their role in cell signaling and endocytosis.Biochimica et biophysica acta. Molecular cell research · 2017
    Review
  15. Review
  16. Article
  17. Review
  18. Review
  19. Review
  20. 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

7 authors at 3 institutions in 2 countries.

Magali MalacombeDépartement Neurotransmission & Sécrétion Neuroendocrine, Institut des Neurosciences Cellulaires et Intégratives (UMR 7168/LC2), Centre National de la Recherche Scientifique & Université Louis Pasteur, Strasbourg, France.
Mara Ceridono
Valérie Calco
Sylvette Chasserot-Golaz
Peter S McPherson
Marie-France Bader
Stéphane Gasman
Institut des Neurosciences Cellulaires et Intégratives · FRCentre National de la Recherche Scientifique · FRMontreal Neurological Institute and Hospital · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rho GTPases are key regulators of the actin cytoskeleton in membrane trafficking events. We previously reported that Cdc42 facilitates exocytosis in neuroendocrine cells by stimulating actin assembly at docking sites for secretory granules. These findings raise the question of the mechanism activating Cdc42 in exocytosis. The neuronal guanine nucleotide exchange factor, intersectin-1L, which specifically activates Cdc42 and is at an interface between membrane trafficking and actin dynamics, appears as an ideal candidate to fulfill this function. Using PC12 and chromaffin cells, we now show the presence of intersectin-1 at exocytotic sites. Moreover, through an RNA interference strategy coupled with expression of various constructs encoding the guanine nucleotide exchange domain, we demonstrate that intersectin-1L is an essential component of the exocytotic machinery. Silencing of intersectin-1 prevents secretagogue-induced activation of Cdc42 revealing intersectin-1L as the factor integrating Cdc42 activation to the exocytotic pathway. Our results extend the current role of intersectin-1L in endocytosis to a function in exocytosis and support the idea that intersectin-1L is an adaptor that coordinates exo-endocytotic membrane trafficking in secretory cells.

Indexed as

ExocytosisActinsAdaptor Proteins, Vesicular TransportAnimalsCalciumcdc42 GTP-Binding ProteinChromaffin CellsGuanine Nucleotide Exchange FactorsHumansMicroscopy, ConfocalPC12 CellsRatsSecretory VesiclesSignal TransductionTransfectionActinsAdaptor Proteins, Vesicular TransportCalciumcdc42 GTP-Binding ProteinGuanine Nucleotide Exchange FactorsITSN1 protein, human

Identifiers

PMID16874303
PMCPMC1538555
OpenAlexW2044637592

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.