Endocytic Roles of Glycans on Proteins and Lipids
(2024) In Cold Spring Harbor perspectives in biology 16(1).- Abstract
Most cell surface proteins are decorated by glycans, and the plasma membrane is rich in glycosylated lipids. The mechanisms by which the enormous complexity of these glycan structures on proteins and lipids is exploited to control glycoprotein activity by setting their cell surface residence time and the ways by which they are taken up into cells are still under active investigation. Here, two mechanisms are presented, termed galectin lattices and gly-colipid-lectin (GL-Lect)-driven endocytosis, which are among the most prominent to establish a link between glycan information and endocytosis. Types of glycans on glycoproteins and glycolipids are reviewed from the angle of their interaction with glycan-binding proteins that are at the... (More)
Most cell surface proteins are decorated by glycans, and the plasma membrane is rich in glycosylated lipids. The mechanisms by which the enormous complexity of these glycan structures on proteins and lipids is exploited to control glycoprotein activity by setting their cell surface residence time and the ways by which they are taken up into cells are still under active investigation. Here, two mechanisms are presented, termed galectin lattices and gly-colipid-lectin (GL-Lect)-driven endocytosis, which are among the most prominent to establish a link between glycan information and endocytosis. Types of glycans on glycoproteins and glycolipids are reviewed from the angle of their interaction with glycan-binding proteins that are at the heart of galectin lattices and GL-Lect-driven endocytosis. Examples are given to show how these mechanisms affect cellular functions ranging from cell migration and signaling to vascularization and immune modulation. Finally, outstanding challenges on the link between glycosylation and endocytosis are discussed.
(Less)
- author
- Johannes, Ludger ; Shafaq-Zadah, Massiullah ; Dransart, Estelle ; Wunder, Christian and Leffler, Hakon LU
- organization
- publishing date
- 2024-01
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Cold Spring Harbor perspectives in biology
- volume
- 16
- issue
- 1
- article number
- a041398
- publisher
- Cold Spring Harbor Laboratory Press (CSHL)
- external identifiers
-
- pmid:37735065
- scopus:85181584789
- ISSN
- 1943-0264
- DOI
- 10.1101/cshperspect.a041398
- language
- English
- LU publication?
- yes
- id
- 51ef33ec-ebce-45e8-9ff2-f9f3594cc43d
- date added to LUP
- 2024-02-12 10:48:16
- date last changed
- 2024-04-14 02:18:44
@article{51ef33ec-ebce-45e8-9ff2-f9f3594cc43d,
abstract = {{<p>Most cell surface proteins are decorated by glycans, and the plasma membrane is rich in glycosylated lipids. The mechanisms by which the enormous complexity of these glycan structures on proteins and lipids is exploited to control glycoprotein activity by setting their cell surface residence time and the ways by which they are taken up into cells are still under active investigation. Here, two mechanisms are presented, termed galectin lattices and gly-colipid-lectin (GL-Lect)-driven endocytosis, which are among the most prominent to establish a link between glycan information and endocytosis. Types of glycans on glycoproteins and glycolipids are reviewed from the angle of their interaction with glycan-binding proteins that are at the heart of galectin lattices and GL-Lect-driven endocytosis. Examples are given to show how these mechanisms affect cellular functions ranging from cell migration and signaling to vascularization and immune modulation. Finally, outstanding challenges on the link between glycosylation and endocytosis are discussed.</p>}},
author = {{Johannes, Ludger and Shafaq-Zadah, Massiullah and Dransart, Estelle and Wunder, Christian and Leffler, Hakon}},
issn = {{1943-0264}},
language = {{eng}},
number = {{1}},
publisher = {{Cold Spring Harbor Laboratory Press (CSHL)}},
series = {{Cold Spring Harbor perspectives in biology}},
title = {{Endocytic Roles of Glycans on Proteins and Lipids}},
url = {{http://dx.doi.org/10.1101/cshperspect.a041398}},
doi = {{10.1101/cshperspect.a041398}},
volume = {{16}},
year = {{2024}},
}