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A Human Corneal Organ Culture Model of Descemet's Stripping Only with Accelerated Healing Stimulated by Engineered Fibroblast Growth Factor 1
Published on: July 22, 2022
Differential regulation of fibroblast growth factor receptor 1 trafficking and function by extracellular galectins
Marika Kucińska1, Natalia Porębska1, Agata Lampart1
1Faculty of Biotechnology, Department of Protein Engineering, University of Wroclaw, Joliot-Curie 14a, 50-383, Wroclaw, Poland.
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.
Insights
Galectins bind to Fibroblast Growth Factor Receptors (FGFR1), influencing cell signaling. Galectin-1 promotes cell proliferation, while galectin-3 inhibits receptor internalization, impacting cell fate.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Fibroblast Growth Factor Receptors (FGFRs) are crucial for cell signaling, and their dysregulation is linked to cancer and metabolic diseases.
- FGFRs' localization, trafficking, and function depend on multiprotein complex formation.
- Galectins are implicated in cancer development and progression.
Purpose of the Study:
- To identify novel binding partners of FGFR1.
- To investigate the interaction between galectins and FGFR1.
- To elucidate the functional consequences of galectin binding on FGFR1 signaling and trafficking.
Main Methods:
- Co-immunoprecipitation assays to detect FGFR1-galectin interactions.
- Surface plasmon resonance to confirm direct binding kinetics.
- Cell-based assays to assess FGFR1 activation, signaling, proliferation, and internalization.
Main Results:
- Galectin-1 and galectin-3 were identified as novel binding proteins for FGFR1.
- Both galectins bind to the glycosylated extracellular domain of FGFR1 and compete for the same sites.
- Galectin-1 activates FGFR1 signaling, promoting cell proliferation and survival.
- Galectin-3 induces FGFR1 clustering, inhibiting its internalization and constitutive signaling.
Conclusions:
- Extracellular galectins interact with FGFR1, modulating its function.
- Galectin-1 and galectin-3 exert opposing effects on FGFR1 activity and trafficking.
- This interplay highlights a novel regulatory mechanism for FGFRs in controlling cell fate.
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