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Glycolipid-dependent and lectin-driven transcytosis in mouse enterocytes
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 d...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7873212/ https://www.ncbi.nlm.nih.gov/pubmed/33564097 http://dx.doi.org/10.1038/s42003-021-01693-2 |
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author | Ivashenka, Alena Wunder, Christian Chambon, Valerie Sandhoff, Roger Jennemann, Richard Dransart, Estelle Podsypanina, Katrina Lombard, Bérangère Loew, Damarys Lamaze, Christophe Poirier, Francoise Gröne, Hermann-Josef Johannes, Ludger Shafaq-Zadah, Massiullah |
author_facet | Ivashenka, Alena Wunder, Christian Chambon, Valerie Sandhoff, Roger Jennemann, Richard Dransart, Estelle Podsypanina, Katrina Lombard, Bérangère Loew, Damarys Lamaze, Christophe Poirier, Francoise Gröne, Hermann-Josef Johannes, Ludger Shafaq-Zadah, Massiullah |
author_sort | Ivashenka, Alena |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7873212 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-78732122021-02-16 Glycolipid-dependent and lectin-driven transcytosis in mouse enterocytes Ivashenka, Alena Wunder, Christian Chambon, Valerie Sandhoff, Roger Jennemann, Richard Dransart, Estelle Podsypanina, Katrina Lombard, Bérangère Loew, Damarys Lamaze, Christophe Poirier, Francoise Gröne, Hermann-Josef Johannes, Ludger Shafaq-Zadah, Massiullah Commun Biol Article 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. Nature Publishing Group UK 2021-02-09 /pmc/articles/PMC7873212/ /pubmed/33564097 http://dx.doi.org/10.1038/s42003-021-01693-2 Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Ivashenka, Alena Wunder, Christian Chambon, Valerie Sandhoff, Roger Jennemann, Richard Dransart, Estelle Podsypanina, Katrina Lombard, Bérangère Loew, Damarys Lamaze, Christophe Poirier, Francoise Gröne, Hermann-Josef Johannes, Ludger Shafaq-Zadah, Massiullah Glycolipid-dependent and lectin-driven transcytosis in mouse enterocytes |
title | Glycolipid-dependent and lectin-driven transcytosis in mouse enterocytes |
title_full | Glycolipid-dependent and lectin-driven transcytosis in mouse enterocytes |
title_fullStr | Glycolipid-dependent and lectin-driven transcytosis in mouse enterocytes |
title_full_unstemmed | Glycolipid-dependent and lectin-driven transcytosis in mouse enterocytes |
title_short | Glycolipid-dependent and lectin-driven transcytosis in mouse enterocytes |
title_sort | glycolipid-dependent and lectin-driven transcytosis in mouse enterocytes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7873212/ https://www.ncbi.nlm.nih.gov/pubmed/33564097 http://dx.doi.org/10.1038/s42003-021-01693-2 |
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