Evidence map›Paper›PMID 26023235›Full record

ArticleThe Journal of biological chemistry2015

Structural Basis of a Key Factor Regulating the Affinity between the Zonula Occludens First PDZ Domain and Claudins.

Julian Nomme, Aleksandar Antanasijevic, Michael Caffrey, Christina M Van Itallie, James M Anderson, Alan S Fanning, Arnon Lavie

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
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

33 citing papers in PubMed.

  1. Review
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  7. Review
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  11. Article
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  15. Article
  16. Article
  17. The Epithelial Cell Leak Pathway.International journal of molecular sciences · 2021
    Review
  18. Article
  19. Article
  20. Claudin-2 inhibits renal clear cell carcinoma progression by inhibiting YAP-activation.Journal of experimental & clinical cancer research : CR · 2021
    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

7 authors.

Julian NommeFrom the Department of Biochemistry and Molecular Genetics, University of Illinois, Chicago, Illinois 60607.
Aleksandar AntanasijevicFrom the Department of Biochemistry and Molecular Genetics, University of Illinois, Chicago, Illinois 60607.
Michael CaffreyFrom the Department of Biochemistry and Molecular Genetics, University of Illinois, Chicago, Illinois 60607.
Christina M Van ItallieLaboratory of Tight Junction Structure and Function, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, and.
James M AndersonLaboratory of Tight Junction Structure and Function, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, and.
Alan S FanningDepartment of Cell Biology and Physiology, University of North Carolina, Chapel Hill, North Carolina 27599.
Arnon LavieFrom the Department of Biochemistry and Molecular Genetics, University of Illinois, Chicago, Illinois 60607, lavie@uic.edu.

Funding

ZO-1 & Cytoplasmic Scaffolding of the Tight JunctionR01DK061397 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI FANNING, ALAN SCOTT · 2003 to 2012
$3.4M
Novel approaches to study dynamic coupling of the tight junction barrier to the actin cytoskeletonZIAHL006207 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ANDERSON, JAMES · 2016 to 2016
$461k
NMR-based discovery of influenza hemagglutinin probesR21AI101676 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI CAFFREY, MICHAEL S. · 2012 to 2013
$427k
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 HHSNIAID NIH HHS AI101676NIAID NIH HHS R21 AI101676NIDDK NIH HHS DK61397NIDDK NIH HHS R01 DK061397NIDDK NIH HHS R56 DK061397
6 · The paper itself

Abstract

The molecular seal between epithelial cells, called the tight junction (TJ), is built by several membrane proteins, with claudins playing the most prominent role. The scaffold proteins of the zonula occludens family are required for the correct localization of claudins and hence formation of the TJ. The intracellular C terminus of claudins binds to the N-terminal PDZ domain of zonula occludens proteins (PDZ1). Of the 23 identified human claudin proteins, nine possess a tyrosine at the -6 position. Here we show that the claudin affinity for PDZ1 is dependent on the presence or absence of this tyrosine and that the affinity is reduced if the tyrosine is modified by phosphorylation. The PDZ1 β2-β3 loop undergoes a significant conformational change to accommodate this tyrosine. Cell culture experiments support a regulatory role for this tyrosine. Plasticity has been recognized as a critical property of TJs that allow cell remodeling and migration. Our work provides a molecular framework for how TJ plasticity may be regulated.

Indexed as

Amino Acid MotifsAmino Acid SequenceClaudin-1Claudin-2HumansMolecular Sequence DataPDZ DomainsPhosphorylationProtein BindingProtein Structure, SecondarySequence AlignmentTight JunctionsTyrosineZonula Occludens-1 ProteinClaudin-1Claudin-2TyrosineZonula Occludens-1 Proteinclaudinphosphorylationphosphotyrosinescaffold proteinstructural biologytight junctionZO-1

Identifiers

PMID26023235
PMCPMC4505413

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.