Evidence map›Paper›PMID 25694446›Full record

ArticleMolecular biology of the cell2015

PKCι interacts with Rab14 and modulates epithelial barrier function through regulation of claudin-2 levels.

Ruifeng Lu, Dogukan Dalgalan, Edward K Mandell, Sara S Parker, Sourav Ghosh, Jean M Wilson

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Rab14 promotes Parkin-mediated mitophagy.Molecular biology of the cell · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Claudin-2: Roles beyond Permeability Functions.International journal of molecular sciences · 2019
    Review
  8. Review
  9. The Endosomal Protein Endotubin Is Required for Enterocyte Differentiation.Cellular and molecular gastroenterology and hepatology · 2018
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. 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

6 authors at 2 institutions in 1 country.

Ruifeng LuDepartment of Cellular and Molecular Medicine, University of Arizona College of Medicine, Tucson, AZ 85724.
Dogukan DalgalanDepartment of Cellular and Molecular Medicine, University of Arizona College of Medicine, Tucson, AZ 85724.
Edward K MandellDepartment of Neurology, Yale University School of Medicine, New Haven, CT 06511.
Sara S ParkerDepartment of Cellular and Molecular Medicine, University of Arizona College of Medicine, Tucson, AZ 85724.
Sourav GhoshDepartment of Neurology, Yale University School of Medicine, New Haven, CT 06511.
Jean M WilsonDepartment of Cellular and Molecular Medicine, University of Arizona College of Medicine, Tucson, AZ 85724 jeanw@email.arizona.edu.
University of Arizona · USYale University · US

Funding

Regulation of Intestinal Tight Junction Structure by Membrane TrafficR01DK084047 · NIDDK · UNIVERSITY OF ARIZONA · PI WILSON, JEAN M · 2011 to 2015
$1.7M
Regulation of Intestinal Tight Junction Structure by Membrane TrafficR56DK084047 · NIDDK · UNIVERSITY OF ARIZONA · PI WILSON, JEAN M · 2010 to 2010
$379k
NIDDK NIH HHS DK084047NIDDK NIH HHS R01 DK084047NIDDK NIH HHS R56 DK084047
6 · The paper itself

Abstract

PKCι is essential for the establishment of epithelial polarity and the normal assembly of tight junctions. We find that PKCι knockdown does not compromise the steady-state distribution of most tight junction proteins but results in increased transepithelial resistance (TER) and decreased paracellular permeability. Analysis of the levels of tight junction components demonstrates that claudin-2 protein levels are decreased. However, other tight junction proteins, such as claudin-1, ZO-1, and occludin, are unchanged. Incubation with an aPKC pseudosubstrate recapitulates the phenotype of PKCι knockdown, including increased TER and decreased levels of claudin-2. In addition, overexpression of PKCι results in increased claudin-2 levels. ELISA and coimmunoprecipitation show that the TGN/endosomal small GTPase Rab14 and PKCι interact directly. Immunolabeling shows that PKCι and Rab14 colocalize in both intracellular puncta and at the plasma membrane and that Rab14 expression is required for normal PKCι distribution in cysts in 3D culture. We showed previously that knockdown of Rab14 results in increased TER and decreased claudin-2. Our results suggest that Rab14 and aPKC interact to regulate trafficking of claudin-2 out of the lysosome-directed pathway.

Indexed as

AnimalsClaudin-2DogsEpithelial CellsGene Expression RegulationGene Knockdown TechniquesHumansIsoenzymesLysosomesMadin Darby Canine Kidney CellsPermeabilityProtein Kinase CProtein Kinase C-lambdaProtein Transportrab GTP-Binding ProteinsTight JunctionsClaudin-2IsoenzymesProtein Kinase CProtein Kinase C-lambdaRab14 protein, humanrab GTP-Binding Proteins

Identifiers

PMID25694446
PMCPMC4395131
OpenAlexW2159449385

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.