Evidence map›Paper›PMID 28829038›Full record

ArticleeLife2017

Dual control of pcdh8l/PCNS expression and function in

Vikram Khedgikar, Genevieve Abbruzzese, Ketan Mathavan, Hannah Szydlo, Helene Cousin, Dominique Alfandari

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

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  7. Development (Cambridge, England) · 2018
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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

6 authors at 2 institutions in 1 country.

Vikram KhedgikarDepartment of Veterinary and Animal Sciences, University of Massachusetts, Amherst, United States.
Genevieve AbbruzzeseDavid H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, United States.
Ketan MathavanDepartment of Veterinary and Animal Sciences, University of Massachusetts, Amherst, United States.
Hannah SzydloDepartment of Veterinary and Animal Sciences, University of Massachusetts, Amherst, United States.
Helene CousinDepartment of Veterinary and Animal Sciences, University of Massachusetts, Amherst, United States.
Dominique AlfandariDepartment of Veterinary and Animal Sciences, University of Massachusetts, Amherst, United States.ORCID http://orcid.org/0000-0002-0557-1246
University of Massachusetts Amherst · USMassachusetts Institute of Technology · US

Funding

Mechanism of Xenopus Cranial Neural Crest Cell MigrationR01DE016289 · NIDCR · UNIVERSITY OF MASSACHUSETTS AMHERST · PI ALFANDARI, DOMINIQUE R · 2006 to 2022
$5.4M
CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
Production and characterization of monoclonal antibodies to Xenopus ProteinsR24OD021485 · OD · UNIVERSITY OF MASSACHUSETTS AMHERST · PI ALFANDARI, DOMINIQUE R · 2017 to 2020
$1.2M
Role of Lbh during craniofacial development of vertebratesR03DE025692 · NIDCR · UNIVERSITY OF MASSACHUSETTS AMHERST · PI COUSIN, HELENE · 2016 to 2017
$227k
Regulation of ADAM13 function during cranial neural crest migrationF31DE023275 · NIDCR · UNIVERSITY OF MASSACHUSETTS AMHERST · PI ABBRUZZESE, GENEVIEVE · 2012 to 2014
$84k
NIDCR NIH HHS F31 DE023275NIDCR NIH HHS R01 DE016289NIDCR NIH HHS R03 DE025692NIGMS NIH HHS T32 GM008515NIH HHS R24 OD021485
6 · The paper itself

Abstract

Adam13/33 is a cell surface metalloprotease critical for cranial neural crest (CNC) cell migration. It can cleave multiple substrates including itself, fibronectin, ephrinB, cadherin-11, pcdh8 and pcdh8l (this work). Cleavage of cadherin-11 produces an extracellular fragment that promotes CNC migration. In addition, the adam13 cytoplasmic domain is cleaved by gamma secretase, translocates into the nucleus and regulates multiple genes. Here, we show that adam13 interacts with the arid3a/dril1/Bright transcription factor. This interaction promotes a proteolytic cleavage of arid3a and its translocation to the nucleus where it regulates another transcription factor: tfap2α. Tfap2α in turn activates multiple genes including the protocadherin pcdh8l (PCNS). The proteolytic activity of adam13 is critical for the release of arid3a from the plasma membrane while the cytoplasmic domain appears critical for the cleavage of arid3a. In addition to this transcriptional control of pcdh8l, adam13 cleaves pcdh8l generating an extracellular fragment that also regulates cell migration.

Indexed as

Gene Expression RegulationADAM ProteinsAnimalsCadherinsDNA-Binding ProteinsMembrane ProteinsNeural CrestProtocadherinsTranscription Factor AP-2Transcription FactorsTranscription, GeneticXenopus laevisXenopus ProteinsADAM33 protein, XenopusADAM ProteinsArid3a protein, XenopusCadherinsDNA-Binding ProteinsMembrane Proteinspcdh8l protein, XenopusProtocadherinstfap2a protein, XenopusTranscription Factor AP-2Transcription FactorsXenopus ProteinsADAMcell migrationdevelopmental biologyembryometalloproteaseneural crestprotocadherinstem cellsxenopus

Identifiers

PMID28829038
PMCPMC5601995
OpenAlexW2750260156

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.