ArticleThe Biochemical journal2003
Ligand-induced recruitment of Na+/H+-exchanger regulatory factor to the PDGF (platelet-derived growth factor) receptor regulates actin cytoskeleton reorganization by PDGF.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 49 citations in OpenAlex.
- MDA-9/Syntenin in the tumor and microenvironment defines prostate cancer bone metastasis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Formin-dependent TGF-β signaling for epithelial to mesenchymal transition.Molecular biology of the cell · 2018Article
- Role of the PDZ-scaffold protein NHERF1/EBP50 in cancer biology: from signaling regulation to clinical relevance.Oncogene · 2017Review
- Article
- The roles of PDGF in development and during neurogenesis in the normal and diseased nervous system.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2014Review
- Structural and functional properties of platelet-derived growth factor and stem cell factor receptors.Cold Spring Harbor perspectives in biology · 2013Review
- EBP50 phosphorylation by Cdc2/Cyclin B kinase affects actin cytoskeleton reorganization and regulates functions of human breast cancer cell line MDA-MB-231.Molecules and cells · 2013Article
- Novel bioactivity of NHERF1 in corneal neovascularization.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2012Article
- Tyrosine kinase gene fusions in cancer: translating mechanisms into targeted therapies.Journal of cellular and molecular medicine · 2012Review
- Platelet-derived growth factors and their receptors in normal and malignant hematopoiesis.American journal of blood research · 2012Article
- Regulation of G protein-coupled receptor function by Na+/H+ exchange regulatory factors.Pharmacological reviews · 2011Review
- Multiple oligomerization domains of KANK1-PDGFRβ are required for JAK2-independent hematopoietic cell proliferation and signaling via STAT5 and ERK.Haematologica · 2011Article
- Article
- Transcription factor regulation can be accurately predicted from the presence of target gene signatures in microarray gene expression data.Nucleic acids research · 2010Article
- Critical role of the platelet-derived growth factor receptor (PDGFR) beta transmembrane domain in the TEL-PDGFRbeta cytosolic oncoprotein.The Journal of biological chemistry · 2010Article
- The fusion proteins TEL-PDGFRbeta and FIP1L1-PDGFRalpha escape ubiquitination and degradation.Haematologica · 2009Article
- The transcription of FOXO genes is stimulated by FOXO3 and repressed by growth factors.The Journal of biological chemistry · 2009Article
- Nck adapters are involved in the formation of dorsal ruffles, cell migration, and Rho signaling downstream of the platelet-derived growth factor beta receptor.The Journal of biological chemistry · 2008Article
- NHERF links the N-cadherin/catenin complex to the platelet-derived growth factor receptor to modulate the actin cytoskeleton and regulate cell motility.Molecular biology of the cell · 2007Article
- PTEN tumor suppressor associates with NHERF proteins to attenuate PDGF receptor signaling.The EMBO journal · 2006Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins interacting with the human PDGF (platelet-derived growth factor) beta-receptor were isolated using immobilized peptides derived from the receptor C-terminus as a bait. We identified two PDZ domain proteins, namely NHERF (Na(+)/H(+) exchanger regulatory factor, also called EBP50) and NHERF2 (E3KARP, SIP-1, TKA-1), which have been shown previously to associate with the murine PDGF receptor [Maudsley, Zamah, Rahman, Blitzer, Luttrell, Lefkowitz and Hall (2000) Mol. Cell. Biol. 20, 8352-8363]. In porcine aortic endothelial cells and in fibroblasts, NHERF recruitment was induced by PDGF treatment, but the receptor kinase activity was not required for the formation of the complex, suggesting that NHERF was not recruited in a phosphotyrosine-dependent manner. Instead, the interaction was abolished by mutation of the consensus C-terminal PDZ-interacting domain of the receptor (Leu-1106 to Ala), or truncation of the last 75 amino acid residues of the receptor. Disruption of NHERF binding to the receptor enhanced actin filament reorganization, but did not affect PDGF-induced mitogenicity and chemotaxis. Although NHERF was initially characterized as a factor required for intracellular pH regulation by beta2-adrenergic receptors, we observed that it was not involved in pH regulation by PDGF. Collectively, these results suggest that the ligand-induced association of NHERF PDZ domain with the PDGF receptor tyrosine kinase controls the extent of cytoskeleton reorganization in response to PDGF.
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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.