Authors: MacDonald, E., Forrester, A., Valades-Cruz, C.A. et al.
Source: Nat Cell Biol 27, 449–463 (2025).
We are delighted to share insights from a recent study entitled "Growth factor-triggered de-sialylation controls glycolipid-lectin-driven endocytosis" published in Nature Cell Biology by Ewan MacDonald et al:
"Glycolipid-lectin-driven endocytosis controls the formation of clathrin-independent carriers and the internalization of various cargos such as β1 integrin. Whether this process is regulated in a dynamic manner remained unexplored. Here we demonstrate that, within minutes, the epidermal growth factor triggers the galectin-driven endocytosis of cell-surface glycoproteins, such as integrins, that are key regulators of cell adhesion and migration. The onset of this process—mediated by the Na+/H+ antiporter NHE1 as well as the neuraminidases Neu1 and Neu3—requires the pH-triggered enzymatic removal of sialic acids whose presence otherwise prevents galectin binding. De-sialylated glycoproteins are then retrogradely transported to the Golgi apparatus where their glycan make-up is reset to regulate EGF-dependent invasive-cell migration. Further evidence is provided for a role of neuraminidases and galectin-3 in acidification-dependent bone resorption. Glycosylation at the cell surface thereby emerges as a dynamic and reversible regulatory post-translational modification that controls a highly adaptable trafficking pathway."
Congratulations to all authors for this great article.
Our Lullaby Transfection Reagent was used for gene silencing in HeLa cells with siRNA.
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