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<p>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<sup>+</sup>/H<sup>+</sup> 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.</p>

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Growth factor-triggered de-sialylation controls glycolipid-lectin-driven endocytosis

  • 期刊论文

  • 发表日期：

    2025年2月21日

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  • Ewan MacDonald,
  • Alison Forrester,
  • Cesar A. Valades-Cruz,
  • Thomas D. Madsen,
  • Joseph H. R. Hetmanski,
  • Estelle Dransart,
  • Yeap Ng,
  • Rashmi Godbole,
  • Ananthan Akhil Shp,
  • Ludovic Leconte,
  • Valérie Chambon,
  • Debarpan Ghosh,
  • Alexis Pinet,
  • Dhiraj Bhatia,
  • Bérangère Lombard,
  • Damarys Loew,
  • Martin R. Larsen,
  • Hakon Leffler,
  • Dirk J. Lefeber,
  • Henrik Clausen,
  • Anne Blangy,
  • Patrick Caswell,
  • Massiullah Shafaq-Zadah,
  • Satyajit Mayor,
  • Roberto Weigert,
  • Christian Wunder,
  • Ludger Johannes

摘要

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.