ArticleInternational journal of molecular sciences2019
Crosstalk between p38 and Erk 1/2 in Downregulation of FGF1-Induced Signaling.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 19 citations in OpenAlex.
- Control-guided refinement of partially specified Boolean networks: applications to RTK signaling.Bioinformatics (Oxford, England) · 2026Article
- Chinese Expert Consensus for the Application of rh-aFGF for Chronic Refractory Wounds.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Targeting p38 MAPK signaling pathway: Quercetin as a novel therapy for TMJ synovitis.International journal of molecular medicine · 2026Article
- Hippo Signaling Dysregulation in Breast Cancer: Subtype-Independent Gene and miRNA Signatures.Biomedicines · 2025Article
- Role of signaling pathways in age-related orthopedic diseases: focus on the fibroblast growth factor family.Military Medical Research · 2024Review
- TGFβ overcomes FGF-induced transinhibition of EGFR in lens cells to enable fibrotic secondary cataract.Molecular biology of the cell · 2024Article
- Isoform-specific optical activation of kinase function reveals p38-ERK signaling crosstalk.RSC chemical biology · 2023Article
- MiRNA 24-3p-rich exosomes functionalized DEGMA-modified hyaluronic acid hydrogels for corneal epithelial healing.Bioactive materials · 2023Article
- Evolutionary analysis of p38 stress-activated kinases in unicellular relatives of animals suggests an ancestral function in osmotic stress.Open biology · 2023Article
- [Research advances on the role of acid fibroblast growth factor in promotion of wound healing].Zhonghua shao shang yu chuang mian xiu fu za zhi · 2022Article
- New developments in the biology of fibroblast growth factors.WIREs mechanisms of disease · 2022Review
- p38-MAPK-mediated translation regulation during early blastocyst development is required for primitive endoderm differentiation in mice.Communications biology · 2021Article
- Fibroblast Growth Factor Receptors (FGFRs) and Noncanonical Partners in Cancer Signaling.Cells · 2021Review
- Title: p38δ Regulates IL6 Expression Modulating ERK Phosphorylation in Preadipocytes.Frontiers in cell and developmental biology · 2021Article
- miR-188-3p Inhibits Vascular Smooth Muscle Cell Proliferation and Migration by Targeting Fibroblast Growth Factor 1 (FGF1).Medical science monitor : international medical journal of experimental and clinical research · 2020Article
- An overview of mammalian p38 mitogen-activated protein kinases, central regulators of cell stress and receptor signaling.F1000Research · 2020Review
- Both Hypoxia-Inducible Factor 1 and MAPK Signaling Pathway Attenuate PI3K/AKT via Suppression of Reactive Oxygen Species in Human Pluripotent Stem Cells.Frontiers in cell and developmental biology · 2020Article
- Fibroblast Growth Factor Receptor 4 Deficiency Mediates Airway Inflammation in the Adult Healthy Lung?Frontiers in medicine · 2020Article
- Mitogen-Activated Protein Kinases: Functions in Signal Transduction and Human Diseases.International journal of molecular sciences · 2019Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Mitogen-activated protein kinases (MAPK): Erk1 and Erk2 are key players in negative-feedback regulation of fibroblast growth factor (FGF) signaling. Upon activation, Erk1 and Erk2 directly phosphorylate FGF receptor 1 (FGFR1) at a specific serine residue in the C-terminal part of the receptor, substantially reducing the tyrosine phosphorylation in the receptor kinase domain and its signaling. Similarly, active Erks can also phosphorylate multiple threonine residues in the docking protein FGF receptor substrate 2 (FRS2), a major mediator of FGFR signaling. Here, we demonstrate that in NIH3T3 mouse fibroblasts and human osteosarcoma U2OS cells stably expressing FGFR1, in addition to Erk1 and Erk2, p38 kinase is able to phosphorylate FRS2. Simultaneous inhibition of Erk1/2 and p38 kinase led to a significant change in the phosphorylation pattern of FRS2 that in turn resulted in prolonged tyrosine phosphorylation of FGFR1 and FRS2 and in sustained signaling, as compared to the selective inhibition of Erks. Furthermore, excessive activation of p38 with anisomycin partially compensated the lack of Erks activity. These experiments reveal a novel crosstalk between p38 and Erk1/2 in downregulation of FGF-induced signaling.
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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.