Evidence map›Paper›PMID 21545357›Full record

ArticleThe Biochemical journal2011

Protein kinase Cζ phosphorylates occludin and promotes assembly of epithelial tight junctions.

Suneet Jain, Takuya Suzuki, Ankur Seth, Geetha Samak, Radhakrishna Rao

Abstract read
In one paragraph

Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

55 citing papers in PubMed, 96 citations in OpenAlex.

  1. Review
  2. Review
  3. Occludin acts as a dynein adaptor regulating permeability and collateral angiogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Occludin: a gatekeeper of brain Infection by HIV-1.Fluids and barriers of the CNS · 2023
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. The Epithelial Cell Leak Pathway.International journal of molecular sciences · 2021
    Review
  15. Review
  16. Article
  17. The Role ofGenetics · 2020
    Article
  18. Article
  19. Article
  20. EnteropathogenicInternational journal of molecular sciences · 2020
    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

5 authors at 1 institution in 1 country.

Suneet JainDepartment of Physiology, University of Tennessee Health Science Center, Memphis, TN 38163, USA.
Takuya Suzuki
Ankur Seth
Geetha Samak
Radhakrishna Rao
University of Tennessee Health Science Center · US

Funding

INTESTINAL MUCOSAL PROTECTION BY EPIDERMAL GROWTH FACTORR01DK055532 · NIDDK · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI RAO, RADHAKRISHNA · 1998 to 2020
$4.7M
MECHANISM OF ENDOTOXIN ABSORPTION IN ALCOHOLISMR01AA012307 · NIAAA · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI RAO, RADHAKRISHNA · 2000 to 2014
$3.9M
NIAAA NIH HHS R01 AA012307NIAAA NIH HHS R01-AA12307NIDDK NIH HHS R01 DK055532NIDDK NIH HHS R01-DK55532
6 · The paper itself

Abstract

Protein kinases play an important role in the regulation of epithelial tight junctions. In the present study, we investigated the role of PKCζ (protein kinase Cζ) in tight junction regulation in Caco-2 and MDCK (Madin-Darby canine kidney) cell monolayers. Inhibition of PKCζ by a specific PKCζ pseudosubstrate peptide results in redistribution of occludin and ZO-1 (zona occludens 1) from the intercellular junctions and disruption of barrier function without affecting cell viability. Reduced expression of PKCζ by antisense oligonucleotide or shRNA (short hairpin RNA) also results in compromised tight junction integrity. Inhibition or knockdown of PKCζ delays calcium-induced assembly of tight junctions. Tight junction disruption by PKCζ pseudosubstrate is associated with the dephosphorylation of occludin and ZO-1 on serine and threonine residues. PKCζ directly binds to the C-terminal domain of occludin and phosphorylates it on threonine residues. Thr403, Thr404, Thr424 and Thr438 in the occludin C-terminal domain are the predominant sites of PKCζ-dependent phosphorylation. A T424A or T438A mutation in full-length occludin delays its assembly into the tight junctions. Inhibition of PKCζ also induces redistribution of occludin and ZO-1 from the tight junctions and dissociates these proteins from the detergent-insoluble fractions in mouse ileum. The present study demonstrates that PKCζ phosphorylates occludin on specific threonine residues and promotes assembly of epithelial tight junctions.

Indexed as

AnimalsCaco-2 CellsDogsHumansIleumMembrane ProteinsMiceOccludinPhosphorylationProtein Kinase CProtein Kinase C zetaThreonineTight JunctionsMembrane ProteinsOccludinOCLN protein, humanOcln protein, mouseProtein Kinase CProtein Kinase C zetaThreonine

Identifiers

PMID21545357
PMCPMC3408004
OpenAlexW13749613

What OpenQuestion holds

Textmetadata
LicenceTDM
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.