ArticleCell communication and signaling : CCS2019
Differential regulation of fibroblast growth factor receptor 1 trafficking and function by extracellular galectins.
Article in Cell communication and signaling : CCS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 48 citations in OpenAlex.
- Synthetic Heparan Sulfate-like Oligosaccharides as Tools to Decipher Growth Factor Recognition.Journal of medicinal chemistry · 2026Article
- The role of fibroblast growth factors in cell and cancer metabolism.FEBS letters · 2026Review
- STEAP3 promotes triple-negative breast cancer growth through the FGFR1-mediated activation of PI3K/AKT/mTOR signaling.iScience · 2025Article
- Reprogramming FGF1 from the natural growth factor to the engineered heparan sulphate biosensor.Cell communication and signaling : CCS · 2025Article
- GPNMB is a novel binding partner of FGFR1 that affects tumorigenic potential through AKT phosphorylation in TNBC.Cancer science · 2025Article
- Targeting FGFR for cancer therapy.Journal of hematology & oncology · 2024Review
- The diverse dependence of galectin-1 and -8 on multivalency for the modulation of FGFR1 endocytosis.Cell communication and signaling : CCS · 2024Article
- The intracellular interplay between galectin-1 and FGF12 in the assembly of ribosome biogenesis complex.Cell communication and signaling : CCS · 2024Article
- N-glycosylation acts as a switch for FGFR1 trafficking between the plasma membrane and nuclear envelope.Cell communication and signaling : CCS · 2023Article
- Receptor clustering by a precise set of extracellular galectins initiates FGFR signaling.Cellular and molecular life sciences : CMLS · 2023Article
- The FGF/FGFR system in the microglial neuroinflammation with Borrelia burgdorferi: likely intersectionality with other neurological conditions.Journal of neuroinflammation · 2023Article
- Functional selectivity of Receptor Tyrosine Kinases regulates distinct cellular outputs.Frontiers in cell and developmental biology · 2023Review
- Galectin‑1 binds GRP78 to promote the proliferation and metastasis of gastric cancer.International journal of oncology · 2022Article
- FGFR3-TACCs3 Fusions and Their Clinical Relevance in Human Glioblastoma.International journal of molecular sciences · 2022Review
- The Significance of Cell Surface N-Glycosylation for Internalization and Potency of Cytotoxic Conjugates Targeting Receptor Tyrosine Kinases.International journal of molecular sciences · 2022Article
- New developments in the biology of fibroblast growth factors.WIREs mechanisms of disease · 2022Review
- The microdissected gene expression landscape of nasopharyngeal cancer reveals vulnerabilities in FGF and noncanonical NF-κB signaling.Science advances · 2022Article
- Exploring the FGF/FGFR System in Ocular Tumors: New Insights and Perspectives.International journal of molecular sciences · 2022Review
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fibroblast growth factor receptors (FGFRs) are integral membrane proteins that transmit signals through the plasma membrane. FGFRs signaling needs to be precisely adjusted as aberrant FGFRs function is associated with development of human cancers or severe metabolic diseases. The subcellular localization, trafficking and function of FGFRs rely on the formation of multiprotein complexes. In this study we revealed galectins, lectin family members implicated in cancer development and progression, as novel FGFR1 binding proteins. We demonstrated that galectin-1 and galectin-3 directly bind to the sugar chains of the glycosylated extracellular part of FGFR1. Although both galectins compete for the same binding sites on FGFR1, these proteins elicit different impact on FGFR1 function and cellular trafficking. Galectin-1 mimics fibroblast growth factor as it efficiently activates FGFR1 and receptor-downstream signaling pathways that result in cell proliferation and apoptotic evasion. In contrast, galectin-3 induces extensive clustering of FGFR1 on the cell surface that inhibits constitutive internalization of FGFR1. Our data point on the interplay between extracellular galectins and FGFRs in the regulation of cell fate.
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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.