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Glycosylation and raft endocytosis in cancer

Changes in glycosylation on proteins or lipids are one of the hallmarks of tumorigenesis. In many cases, it is still not understood how glycan information is translated into biological function. In this review, we discuss at the example of specific cancer-related glycoproteins how their endocytic up...

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Autores principales: Johannes, Ludger, Billet, Anne
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7311491/
https://www.ncbi.nlm.nih.gov/pubmed/32388640
http://dx.doi.org/10.1007/s10555-020-09880-z
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author Johannes, Ludger
Billet, Anne
author_facet Johannes, Ludger
Billet, Anne
author_sort Johannes, Ludger
collection PubMed
description Changes in glycosylation on proteins or lipids are one of the hallmarks of tumorigenesis. In many cases, it is still not understood how glycan information is translated into biological function. In this review, we discuss at the example of specific cancer-related glycoproteins how their endocytic uptake into eukaryotic cells is tuned by carbohydrate modifications. For this, we not only focus on overall uptake rates, but also illustrate how different uptake processes—dependent or not on the conventional clathrin machinery—are used under given glycosylation conditions. Furthermore, we discuss the role of certain sugar-binding proteins, termed galectins, to tune glycoprotein uptake by inducing their crosslinking into lattices, or by co-clustering them with glycolipids into raft-type membrane nanodomains from which the so-called clathrin-independent carriers (CLICs) are formed for glycoprotein internalization into cells. The latter process has been termed glycolipid–lectin (GL-Lect) hypothesis, which operates in a complementary manner to the clathrin pathway and galectin lattices.
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spelling pubmed-73114912020-06-26 Glycosylation and raft endocytosis in cancer Johannes, Ludger Billet, Anne Cancer Metastasis Rev Article Changes in glycosylation on proteins or lipids are one of the hallmarks of tumorigenesis. In many cases, it is still not understood how glycan information is translated into biological function. In this review, we discuss at the example of specific cancer-related glycoproteins how their endocytic uptake into eukaryotic cells is tuned by carbohydrate modifications. For this, we not only focus on overall uptake rates, but also illustrate how different uptake processes—dependent or not on the conventional clathrin machinery—are used under given glycosylation conditions. Furthermore, we discuss the role of certain sugar-binding proteins, termed galectins, to tune glycoprotein uptake by inducing their crosslinking into lattices, or by co-clustering them with glycolipids into raft-type membrane nanodomains from which the so-called clathrin-independent carriers (CLICs) are formed for glycoprotein internalization into cells. The latter process has been termed glycolipid–lectin (GL-Lect) hypothesis, which operates in a complementary manner to the clathrin pathway and galectin lattices. Springer US 2020-05-09 2020 /pmc/articles/PMC7311491/ /pubmed/32388640 http://dx.doi.org/10.1007/s10555-020-09880-z Text en © The Author(s) 2020 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Johannes, Ludger
Billet, Anne
Glycosylation and raft endocytosis in cancer
title Glycosylation and raft endocytosis in cancer
title_full Glycosylation and raft endocytosis in cancer
title_fullStr Glycosylation and raft endocytosis in cancer
title_full_unstemmed Glycosylation and raft endocytosis in cancer
title_short Glycosylation and raft endocytosis in cancer
title_sort glycosylation and raft endocytosis in cancer
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7311491/
https://www.ncbi.nlm.nih.gov/pubmed/32388640
http://dx.doi.org/10.1007/s10555-020-09880-z
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