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Article Dans Une Revue Communications Biology Année : 2021

Glycolipid-dependent and lectin-driven transcytosis in mouse enterocytes

Valerie Chambon
  • Fonction : Auteur
Roger Sandhoff
Richard Jennemann
  • Fonction : Auteur
Estelle Dransart
  • Fonction : Auteur
Katrina Podsypanina
  • Fonction : Auteur
Bérangère Lombard
Damarys Loew
Christophe Lamaze
Francoise Poirier
  • Fonction : Auteur
Hermann-Josef Gröne
  • Fonction : Auteur
Ludger Johannes
Massiullah Shafaq-Zadah

Résumé

Abstract Glycoproteins and glycolipids at the plasma membrane contribute to a range of functions from growth factor signaling to cell adhesion and migration. Glycoconjugates undergo endocytic trafficking. According to the glycolipid-lectin (GL-Lect) hypothesis, the construction of tubular endocytic pits is driven in a glycosphingolipid-dependent manner by sugar-binding proteins of the galectin family. Here, we provide evidence for a function of the GL-Lect mechanism in transcytosis across enterocytes in the mouse intestine. We show that galectin-3 (Gal3) and its newly identified binding partner lactotransferrin are transported in a glycosphingolipid-dependent manner from the apical to the basolateral membrane. Transcytosis of lactotransferrin is perturbed in Gal3 knockout mice and can be rescued by exogenous Gal3. Inside enterocytes, Gal3 is localized to hallmark structures of the GL-Lect mechanism, termed clathrin-independent carriers. These data pioneer the existence of GL-Lect endocytosis in vivo and strongly suggest that polarized trafficking across the intestinal barrier relies on this mechanism.

Dates et versions

hal-03969596 , version 1 (02-02-2023)

Identifiants

Citer

Alena Ivashenka, Christian Wunder, Valerie Chambon, Roger Sandhoff, Richard Jennemann, et al.. Glycolipid-dependent and lectin-driven transcytosis in mouse enterocytes. Communications Biology, 2021, 4 (1), pp.173. ⟨10.1038/s42003-021-01693-2⟩. ⟨hal-03969596⟩
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