ArticleNature communications2025
PDGFRα/β heterodimer activation negatively affects downstream ERK1/2 signaling and cellular proliferation.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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.
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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.
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Who cites it
4 citing papers in PubMed.
- Platelet-Derived Growth Factor Receptor Alpha in Male Reproductive Health and Oxidative Stress: Stromal Homeostasis, Injury, and Research Perspectives.Antioxidants (Basel, Switzerland) · 2026Review
- PDGFRα is required for postnatal cerebral perivascular fibroblast development.Developmental biology · 2026Article
- A PDGFRB-CD44-MIF crosstalk promotes cancer-associated cellular phenotypes in ATRT-TYR/MYC cell lines.Frontiers in oncology · 2026Article
- Functional and clinical roles of stromal PDGF receptors in tumor biology.Cancer metastasis reviews · 2024Review
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Authors and funding
6 authors.
Funding
Abstract
The platelet-derived growth factor receptor (PDGFR) family of receptor tyrosine kinases consists of two receptors, PDGFRα and PDGFRβ, that homodimerize and heterodimerize upon ligand binding. Here, we tested the hypothesis that differential internalization and trafficking dynamics of the various PDGFR dimers underlie differences in downstream intracellular signaling and cellular behavior. Using a bimolecular fluorescence complementation approach, we demonstrated that PDGFRα/β heterodimers are rapidly internalized into early endosomes. We showed that PDGFRα/β heterodimer activation does not induce downstream phosphorylation of ERK1/2 and significantly inhibits cell proliferation. Further, we identified MYO1D as a protein that preferentially binds PDGFRα/β heterodimers and demonstrated that knockdown of MYO1D leads to retention of PDGFRα/β heterodimers at the plasma membrane, increased phosphorylation of ERK1/2 and increased cell proliferation. Collectively, our findings impart valuable insight into the molecular mechanisms by which specificity is introduced downstream of PDGFR activation to differentially propagate signaling and generate distinct cellular responses.
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Registered trials
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.