Evidence map›Paper›PMID 24338363›Full record

ArticleJournal of cell science2014

Biotin ligase tagging identifies proteins proximal to E-cadherin, including lipoma preferred partner, a regulator of epithelial cell-cell and cell-substrate adhesion.

Christina M Van Itallie, Amber Jean Tietgens, Angel Aponte, Karin Fredriksson, Alan S Fanning, Marjan Gucek, James M Anderson

Abstract read
In one paragraph

Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

71 citing papers in PubMed, 101 citations in OpenAlex.

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  13. Cell-cell communication: new insights and clinical implications.Signal transduction and targeted therapy · 2024
    Review
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11 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

7 authors at 3 institutions in 1 country.

Christina M Van ItallieLaboratory of Tight Junction Structure and Function, NHLBI, National Institutes of Health, Bethesda, MD 20892, USA.
Amber Jean Tietgens
Angel Aponte
Karin Fredriksson
Alan S Fanning
Marjan Gucek
James M Anderson
National Heart Lung and Blood Institute · USNational Institutes of Health · USUniversity of North Carolina at Chapel Hill · US

Funding

Proteomics CoreZICHL005903 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI GUCEK, MARJAN · 2009 to 2022
$23.3M
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 DK061397
6 · The paper itself

Abstract

Known proteins associated with the cell-adhesion protein E-cadherin include catenins and proteins involved in signaling, trafficking and actin organization. However, the list of identified adherens junction proteins is likely to be incomplete, limiting investigation into this essential cell structure. To expand the inventory of potentially relevant proteins, we expressed E-cadherin fused to biotin ligase in MDCK epithelial cells, and identified by mass spectrometry neighboring proteins that were biotinylated. The most abundant of the 303 proteins identified were catenins and nearly 40 others that had been previously reported to influence cadherin function. Many others could be rationalized as novel candidates for regulating the adherens junction, cytoskeleton, trafficking or signaling. We further characterized lipoma preferred partner (LPP), which is present at both cell contacts and focal adhesions. Knockdown of LPP demonstrated its requirement for E-cadherin-dependent adhesion and suggested that it plays a role in coordination of the cell-cell and cell-substrate cytoskeletal interactions. The analysis of LPP function demonstrates proof of principle that the proteomic analysis of E-cadherin proximal proteins expands the inventory of components and tools for understanding the function of E-cadherin.

Indexed as

Actin CytoskeletonAdherens JunctionsAnimalsAntigens, CDCadherinsCarbon-Nitrogen LigasesCell AdhesionCell MovementDogsEpithelial CellsEscherichia coli ProteinsHumansLIM Domain ProteinsMadin Darby Canine Kidney CellsPermeabilityProtein Interaction Domains and MotifsAntigens, CDbirA protein, E coliCadherinsCarbon-Nitrogen LigasesCDH1 protein, humanEscherichia coli ProteinsLIM Domain ProteinsRecombinant Fusion ProteinsRepressor ProteinsAdherens junctionBiotin ligaseE-cadherinProteomics

Identifiers

PMID24338363
PMCPMC3924204
OpenAlexW2328192806

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.