Glycosylation and raft endocytosis in cancer.
Actin
Cholera toxin
Cholesterol
GPI-anchored protein
Glycosphingolipid
Shiga toxin
Journal
Cancer metastasis reviews
ISSN: 1573-7233
Titre abrégé: Cancer Metastasis Rev
Pays: Netherlands
ID NLM: 8605731
Informations de publication
Date de publication:
06 2020
06 2020
Historique:
pubmed:
11
5
2020
medline:
27
1
2021
entrez:
11
5
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 32388640
doi: 10.1007/s10555-020-09880-z
pii: 10.1007/s10555-020-09880-z
pmc: PMC7311491
doi:
Substances chimiques
Galectins
0
Glycolipids
0
Glycoproteins
0
Shiga Toxin
75757-64-1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
375-396Références
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