Evidence map›Paper›PMID 23418357›Full record

ArticleJournal of cell science2013

Epithelial barrier assembly requires coordinated activity of multiple domains of the tight junction protein ZO-1.

Laurel S Rodgers, M Tanner Beam, James M Anderson, Alan S Fanning

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
7.6field-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

93 citing papers in PubMed, 153 citations in OpenAlex.

  1. Article
  2. Tight junction structure, assembly and (dys)function.Nature reviews. Molecular cell biology · 2026
    Review
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33 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

4 authors at 1 institution in 1 country.

Laurel S RodgersDepartment of Cell Biology and Physiology, University of North Carolina at Chapel Hill, CB7545, Chapel Hill, NC 27599-7545, USA.
M Tanner Beam
James M Anderson
Alan S Fanning
University of North Carolina at Chapel Hill · US

Funding

SEEDING POSTDOCTORAL INNOVATORS IN RESEARCH &EDUCATIONK12GM000678 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DONALD T LYSLE, Kathryn Joanna Reissner · 1999 to 2026
$30.9M
ZO-1 & Cytoplasmic Scaffolding of the Tight JunctionR01DK061397 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI FANNING, ALAN SCOTT · 2003 to 2012
$3.4M
Expanding the tight junction inventory through proteomicsZIAHL006176 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ANDERSON, JAMES · 2014 to 2014
$601k
ZO-1 & Cytoplasmic Scaffolding of the Tight JunctionR56DK061397 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ANDERSON, JAMES M. · 2008 to 2008
$327k
Intramural NIH HHSNIDDK NIH HHS DK061397NIDDK NIH HHS R01 DK061397NIDDK NIH HHS R56 DK061397NIGMS NIH HHS GM000678NIGMS NIH HHS K12 GM000678
6 · The paper itself

Abstract

Tight junctions (TJs) regulate the paracellular movement of ions, macromolecules and immune cells across epithelia. Zonula occludens (ZO)-1 is a multi-domain polypeptide required for the assembly of TJs. MDCK II cells lacking ZO-1, and its homolog ZO-2, have three distinct phenotypes: reduced localization of occludin and some claudins to the TJs, increased epithelial permeability, and expansion of the apical actomyosin contractile array found at the apical junction complex (AJC). However, it is unclear exactly which ZO-1 binding domains are required to coordinate these activities. We addressed this question by examining the ability of ZO-1 domain-deletion transgenes to reverse the effects of ZO depletion. We found that the SH3 domain and the U5 motif are required to recruit ZO-1 to the AJC and that localization is a prerequisite for normal TJ and cytoskeletal organization. The PDZ2 domain is not required for localization of ZO-1 to the AJC, but is necessary to establish the characteristic continuous circumferential band of ZO-1, occludin and claudin-2. PDZ2 is also required to establish normal permeability, but is not required for normal cytoskeletal organization. Finally, our results demonstrate that PDZ1 is crucial for the normal organization of both the TJ and the AJC cytoskeleton. Our results establish that ZO-1 acts as a true scaffolding protein and that the coordinated activity of multiple domains is required for normal TJ structure and function.

Indexed as

Actin CytoskeletonAnimalsBlotting, WesternCell LineCell Membrane PermeabilityClaudin-2DogsHumansImmunohistochemistryImmunoprecipitationProtein BindingTight JunctionsZonula Occludens-1 ProteinClaudin-2Zonula Occludens-1 ProteinActin cytoskeletonMAGUKParacellular permeabilityPDZTight junctionZonula occludens

Identifiers

PMID23418357
PMCPMC3647435
OpenAlexW2103943414

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.