Evidence map›Paper›PMID 19538289›Full record

ArticleAnnals of the New York Academy of Sciences2009

Occludin phosphorylation in regulation of epithelial tight junctions.

Radhakrishna Rao

Open access · greenAbstract read
In one paragraph

Article in Annals of the New York Academy of Sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing 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

121 citing papers in PubMed, 219 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Integrated 'Shield-Spear' Biological Patch for Fibrosis-Free Bladder Reconstruction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  5. Review
  6. Macronutrients as Regulators of Intestinal Epithelial Permeability: Where Do We Stand?Comprehensive reviews in food science and food safety · 2025
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
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  19. Article
  20. Article

61 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Radhakrishna RaoDepartment of Physiology, University of Tennessee Health Science Center, Memphis, Tennessee 38163, USA. rkrao@physio1.utmem.edu
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
Intestinal Mucosal Protection by Epidermal Growth FactorR56DK055532 · NIDDK · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI RAO, RADHAKRISHNA · 2009 to 2009
$345k
NIAAA NIH HHS AA12307NIAAA NIH HHS R01 AA012307NIDDK NIH HHS DK55532NIDDK NIH HHS R01 DK055532
6 · The paper itself

Abstract

Occludin is the first transmembrane protein of the tight junction to be discovered. While numerous studies emphasized the important role of occludin in assembly and maintenance of tight junctions, occludin knockout studies indicated that it was not required for tight junction assembly in different epithelia. However, a detailed characterization of the occludin knockout mouse concluded that the occludin gene is indispensable, and plays a complex role in regulation of epithelial tight junctions in different organs. This article describes the role of occludin phosphorylation in the regulation of its assembly into the tight junctions. Occludin is highly phosphorylated on Ser and Thr residues, while Tyr-phosphorylation is kept at minimum in the intact epithelium. During the disruption of tight junctions by various factors, occludin undergoes dephosphorylation on Ser/Thr residues and elevated phosphorylation on Tyr residues. The phosphorylation of occludin on Tyr, Ser, and Thr residues appears to be regulated by the balance between protein kinases such as c-Src, PKCzeta, and PKClambda/iota, and protein phosphatases such as PP2A, PP1, and PTP1B. The precise mechanism of regulation of the tight junction by occludin phosphorylation is unclear at this time. However, an in vitro study indicated that Tyr-phosphorylation of occludin C-terminal domain attenuates its interaction with ZO-1. Therefore, phosphorylation of specific Ser/Thr/Tyr residues in occludin may regulate its interactions with ZO-1 and possibly other tight junction proteins. It is likely that occludin plays a regulatory role in tight junctions rather than a role in the de novo assembly of tight junctions.

Indexed as

AnimalsBinding SitesEpitheliumHumansMembrane ProteinsMiceMice, KnockoutOccludinPhosphorylationSerineThreonineTight JunctionsTyrosineMembrane ProteinsOccludinOCLN protein, humanOcln protein, mouseSerineThreonineTyrosine

Identifiers

PMID19538289
PMCPMC6202026
OpenAlexW2109758577

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.