Differential regulation of fibroblast growth factor receptor 1 trafficking and function by extracellular galectins.
Cell Commun Signal
; 17(1): 65, 2019 06 17.
Article
em En
| MEDLINE
| ID: mdl-31208421
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.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Galectinas
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Receptor Tipo 1 de Fator de Crescimento de Fibroblastos
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Espaço Extracelular
Limite:
Animals
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Humans
Idioma:
En
Revista:
Cell Commun Signal
Ano de publicação:
2019
Tipo de documento:
Article
País de afiliação:
Polônia