Glycosylation and raft endocytosis in cancer.

Abstract

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.

• Authors: Ludger Johannes, Anne Billet
• Journal: Cancer metastasis reviews (Cancer Metastasis Rev) Vol. 39 Issue 2 Pg. 375-396 (06 2020) ISSN: 1573-7233 [Electronic] Netherlands
• PMID: 32388640 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)

Chemical References

• Galectins
• Glycolipids
• Glycoproteins
• Shiga Toxin

Topics

• Animals
• Endocytosis
• Galectins (metabolism)
• Glycolipids (metabolism)
• Glycoproteins (metabolism)
• Glycosylation
• Humans
• Membrane Microdomains (metabolism)
• Neoplasms (metabolism, pathology)
• Shiga Toxin (metabolism)