Evidence map›Paper›PMID 19889837›Full record

ArticleMolecular biology of the cell2010

Sec3-containing exocyst complex is required for desmosome assembly in mammalian epithelial cells.

Nicholas J Andersen, Charles Yeaman

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

24 citing papers in PubMed, 39 citations in OpenAlex.

  1. Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024
    Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Regulation of Cell Polarity by Exocyst-Mediated Trafficking.Cold Spring Harbor perspectives in biology · 2018
    Review
  7. Article
  8. The Exocyst Complex in Health and Disease.Frontiers in cell and developmental biology · 2016
    Review
  9. Article
  10. Article
  11. The Exocyst at a Glance.Journal of cell science · 2015
    Review
  12. Article
  13. Article
  14. Article
  15. Desmosome assembly and dynamics.Trends in cell biology · 2013
    Review
  16. Article
  17. Review
  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

2 authors at 1 institution in 1 country.

Nicholas J AndersenCarver College of Medicine, University of Iowa, Iowa City, IA 52242, USA.
Charles Yeaman
University of Iowa · US

Funding

Role of Cell Adhesion in Organizing Membrane GrowthR01GM067002 · NIGMS · UNIVERSITY OF IOWA · PI YEAMAN, CHARLES A · 2004 to 2014
$2.6M
NIGMS NIH HHS GM-067002NIGMS NIH HHS R01 GM067002
6 · The paper itself

Abstract

The Exocyst is a conserved multisubunit complex involved in the docking of post-Golgi transport vesicles to sites of membrane remodeling during cellular processes such as polarization, migration, and division. In mammalian epithelial cells, Exocyst complexes are recruited to nascent sites of cell-cell contact in response to E-cadherin-mediated adhesive interactions, and this event is an important early step in the assembly of intercellular junctions. Sec3 has been hypothesized to function as a spatial landmark for the development of polarity in budding yeast, but its role in epithelial cells has not been investigated. Here, we provide evidence in support of a function for a Sec3-containing Exocyst complex in the assembly or maintenance of desmosomes, adhesive junctions that link intermediate filament networks to sites of strong intercellular adhesion. We show that Sec3 associates with a subset of Exocyst complexes that are enriched at desmosomes. Moreover, we found that membrane recruitment of Sec3 is dependent on cadherin-mediated adhesion but occurs later than that of the known Exocyst components Sec6 and Sec8 that are recruited to adherens junctions. RNA interference-mediated suppression of Sec3 expression led to specific impairment of both the morphology and function of desmosomes, without noticeable effect on adherens junctions. These results suggest that two different exocyst complexes may function in basal-lateral membrane trafficking and will enable us to better understand how exocytosis is spatially organized during development of epithelial plasma membrane domains.

Indexed as

AnimalsAntibody SpecificityCadherinsCell AdhesionCell LineCell MembraneCell PolarityCentriolesDesmoglein 2DesmosomesDogsEpithelial CellsHumansMiceProtein BindingProtein TransportCadherinsDesmoglein 2DSG2 protein, humanEXOC1 protein, humanVesicular Transport Proteins

Identifiers

PMID19889837
PMCPMC2801709
OpenAlexW2102740909

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.