Evidence map›Paper›PMID 35946433›Full record

ArticleJournal of cell science2022

PDGFR dimer-specific activation, trafficking and downstream signaling dynamics.

Madison A Rogers, Maria B Campaña, Robert Long, Katherine A Fantauzzo

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

10 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
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  10. [Role and mechanism of platelet-derived growth factor BB in thrombocytosis in Kawasaki disease].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2023
    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

4 authors at 1 institution in 1 country.

Madison A RogersDepartment of Craniofacial Biology, School of Dental Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.
Maria B CampañaDepartment of Craniofacial Biology, School of Dental Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.
Robert LongDepartment of Craniofacial Biology, School of Dental Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.
Katherine A FantauzzoDepartment of Craniofacial Biology, School of Dental Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.
University of Colorado Anschutz Medical Campus · US

Funding

University of Colorado Cancer Center Support Grant - Lung Cancer Patient-Derived Xenografts with Autologous Human Immune SystemsP30CA046934 · NCI · UNIVERSITY OF COLORADO DENVER · PI James V Degregori · 1988 to 2026
$117.0M
Characterization of PDGFR dimer-specific dynamics in the craniofacial mesenchymeR01DE027689 · NIDCR · UNIVERSITY OF COLORADO DENVER · PI FANTAUZZO, KATHERINE ANN · 2018 to 2022
$2.0M
Characterization of PDGFR dimer-specific dynamics in the craniofacial mesenchymeK02DE028572 · NIDCR · UNIVERSITY OF COLORADO DENVER · PI FANTAUZZO, KATHERINE ANN · 2019 to 2023
$627k
Examining PDGFR dimer-specific activation and internalization dynamicsF31DE029976 · NIDCR · UNIVERSITY OF COLORADO DENVER · PI ROGERS, MADISON A · 2020 to 2022
$86k
NCI NIH HHS P30 CA046934NIDCR NIH HHS F31 DE029976NIDCR NIH HHS K02 DE028572NIDCR NIH HHS R01 DE027689
6 · The paper itself

Abstract

Signaling through the platelet-derived growth factor receptors (PDGFRs) plays a critical role in multiple cellular processes during development. The two PDGFRs, PDGFRα and PDGFRβ, dimerize to form homodimers and/or heterodimers. Here, we overcome previous limitations in studying PDGFR dimer-specific dynamics by generating cell lines stably expressing C-terminal fusions of each PDGFR with bimolecular fluorescence complementation (BiFC) fragments corresponding to the N-terminal or C-terminal regions of the Venus fluorescent protein. We find that PDGFRβ receptors homodimerize more quickly than PDGFRα receptors in response to PDGF ligand, with increased levels of autophosphorylation. Furthermore, we demonstrate that PDGFRα homodimers are trafficked and degraded more quickly, whereas PDGFRβ homodimers are more likely to be recycled back to the cell membrane. We show that PDGFRβ homodimer activation results in a greater amplitude of phospho-ERK1/2 and phospho-AKT signaling, as well as increased proliferation and migration. Finally, we demonstrate that inhibition of clathrin-mediated endocytosis leads to changes in cellular trafficking and downstream signaling, particularly for PDGFRα homodimers. Collectively, our findings provide significant insight into how biological specificity is introduced to generate unique responses downstream of PDGFR engagement. This article has an associated First Person interview with the first author of the paper.

Indexed as

Receptor, Platelet-Derived Growth Factor alphaSignal TransductionHumansPhosphorylationProtein MultimerizationReceptor, Platelet-Derived Growth Factor betaReceptor, Platelet-Derived Growth Factor alphaReceptor, Platelet-Derived Growth Factor betaMigrationPDGFRαPDGFRβProliferationSignalingTrafficking

Identifiers

PMID35946433
PMCPMC9482349
OpenAlexW4294916304

What Socratic 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 Socratic graph.