Evidence map›Paper›PMID 23924897›Full record

ArticleMolecular biology of the cell2013

Occludin OCEL-domain interactions are required for maintenance and regulation of the tight junction barrier to macromolecular flux.

Mary M Buschmann, Le Shen, Harsha Rajapakse, David R Raleigh, Yitang Wang, Yingmin Wang, Amulya Lingaraju, Juanmin Zha, Elliot Abbott, Erin M McAuley and 5 more

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed, 1 pooled it
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

114 citing papers in PubMed, 1 synthesis or guideline pooled it, 184 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. NontoxigenicMicroorganisms · 2026
    Review
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  20. Prednisolone Targets Claudins in Mouse Brain Blood Vessels.International journal of molecular sciences · 2023
    Article

54 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

15 authors at 1 institution in 1 country.

Mary M BuschmannDepartment of Pathology, The University of Chicago, Chicago, IL 60637.
Le Shen
Harsha Rajapakse
David R Raleigh
Yitang Wang
Yingmin Wang
Amulya Lingaraju
Juanmin Zha
Elliot Abbott
Erin M McAuley
Lydia A Breskin
Licheng Wu
Kenneth Anderson
Jerrold R Turner
Christopher R Weber
University of Chicago · US

Funding

VIRAL ONCOLOGY CORE FACILITYP30CA014599 · NCI · UNIVERSITY OF CHICAGO · PI MARK W. LINGEN · 1985 to 2026
$122.1M
ULTRASTRUCTURE AND CYTOMORPHOLOGY COREP30DK042086 · NIDDK · UNIVERSITY OF CHICAGO · PI LIU, CAMBRIAN YANGSHAO · 1990 to 2025
$29.8M
TRANSLATIONAL RESEARCH UNIVERSITY OF CHICAGO: CLINICAL TRIALSUL1RR024999 · NCRR · UNIVERSITY OF CHICAGO · PI SOLWAY, JULIAN · 2007 to 2011
$25.3M
ZO-1-MEDIATED PROTEIN INTERACTIONS: REGULATORS AND INTEGRATORS OF DIVERSE EPITHELIAL FUNCTIONS IN HEALTH AND DISEASER01DK061931 · NIDDK · UNIVERSITY OF CHICAGO · PI JERROLD R. TURNER · 2001 to 2026
$15.0M
Therapeutic targeting of protein interactions to reverse MLCK1-mediated intestinal barrier loss and ameliorate disease.R01DK068271 · NIDDK · UNIVERSITY OF CHICAGO · PI JERROLD R. TURNER · 2005 to 2026
$11.3M
Transcriptional Regulation of NHE-3 Isoform in Human IntestineP01DK067887 · NIDDK · UNIVERSITY OF ILLINOIS AT CHICAGO · PI HECHT, GAIL A · 2006 to 2011
$4.9M
Contribution of occludin to intestinal homeostasis and diseaseK01DK092381 · NIDDK · UNIVERSITY OF CHICAGO · PI SHEN, LE · 2012 to 2016
$751k
Mechanisms and pathways of trans-tight junction conductanceK08DK088953 · NIDDK · UNIVERSITY OF CHICAGO · PI WEBER, CHRISTOPHER · 2010 to 2014
$733k
HTS ASSAYS FOR INHIBITORS OF PROTEIN INTERACTIONS INCLUDING MLCK1-FKBP8R56DK094954 · NIDDK · UNIVERSITY OF ILLINOIS AT CHICAGO · PI MILLER, LAWRENCE, TURNER, JERROLD R. · 2012 to 2012
$157k
ZO-1 domain interactions in tight junction structure and barrier functionF32DK094550 · NIDDK · UNIVERSITY OF CHICAGO · PI BUSCHMANN, MARY MCVEY · 2011 to 2013
$147k
NCI NIH HHS P30 CA014599NCI NIH HHS P30CA14599NCRR NIH HHS UL1 RR024999NCRR NIH HHS UL1RR024999NIDDK NIH HHS F32 DK094550NIDDK NIH HHS F32DK094550NIDDK NIH HHS K01 DK092381NIDDK NIH HHS K01DK092381NIDDK NIH HHS K08 DK088953NIDDK NIH HHS K08DK088953NIDDK NIH HHS P01 DK067887NIDDK NIH HHS P30 DK042086NIDDK NIH HHS P30DK042086NIDDK NIH HHS R01 DK061931NIDDK NIH HHS R01 DK068271NIDDK NIH HHS R01DK61931NIDDK NIH HHS R01DK68271
6 · The paper itself

Abstract

In vitro and in vivo studies implicate occludin in the regulation of paracellular macromolecular flux at steady state and in response to tumor necrosis factor (TNF). To define the roles of occludin in these processes, we established intestinal epithelia with stable occludin knockdown. Knockdown monolayers had markedly enhanced tight junction permeability to large molecules that could be modeled by size-selective channels with radii of ~62.5 Å. TNF increased paracellular flux of large molecules in occludin-sufficient, but not occludin-deficient, monolayers. Complementation using full-length or C-terminal coiled-coil occludin/ELL domain (OCEL)-deficient enhanced green fluorescent protein (EGFP)-occludin showed that TNF-induced occludin endocytosis and barrier regulation both required the OCEL domain. Either TNF treatment or OCEL deletion accelerated EGFP-occludin fluorescence recovery after photobleaching, but TNF treatment did not affect behavior of EGFP-occludin(ΔOCEL). Further, the free OCEL domain prevented TNF-induced acceleration of occludin fluorescence recovery, occludin endocytosis, and barrier loss. OCEL mutated within a recently proposed ZO-1-binding domain (K433) could not inhibit TNF effects, but OCEL mutated within the ZO-1 SH3-GuK-binding region (K485/K488) remained functional. We conclude that OCEL-mediated occludin interactions are essential for limiting paracellular macromolecular flux. Moreover, our data implicate interactions mediated by the OCEL K433 region as an effector of TNF-induced barrier regulation.

Indexed as

Caco-2 CellsEndocytosisGene Knockdown TechniquesHumansIntestinal MucosaOccludinPermeabilityProtein BindingProtein Structure, TertiarySequence DeletionSignal TransductionTight JunctionsTumor Necrosis Factor-alphaOccludinTumor Necrosis Factor-alpha

Identifiers

PMID23924897
PMCPMC3784380
OpenAlexW2063638556

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.