Exploration into Galectin-3 Driven Endocytosis and Lattices.
clathrin
endocytosis
galectin-3
gl-lect hypothesis
glycosphingolipids
lattices
α5β1 integrin
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
18 Sep 2024
18 Sep 2024
Historique:
received:
19
03
2024
revised:
05
09
2024
accepted:
14
09
2024
medline:
28
9
2024
pubmed:
28
9
2024
entrez:
28
9
2024
Statut:
epublish
Résumé
Essentially all plasma membrane proteins are glycosylated, and their activity is regulated by tuning their cell surface dynamics. This is achieved by glycan-binding proteins of the galectin family that either retain glycoproteins within lattices or drive their endocytic uptake via the clathrin-independent glycolipid-lectin (GL-Lect) mechanism. Here, we have used immunofluorescence-based assays to analyze how lattice and GL-Lect mechanisms affect the internalization of the cell adhesion and migration glycoprotein α
Identifiants
pubmed: 39334935
pii: biom14091169
doi: 10.3390/biom14091169
pii:
doi:
Substances chimiques
Galectin 3
0
Integrin alpha5beta1
0
LGALS3 protein, human
0
Galectins
0
Blood Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Mizutani Foundation for Glycoscience
ID : 200014
Organisme : Agence Nationale de la Recherche
ID : ANR-19-CE13-0001-01
Organisme : Agence Nationale de la Recherche
ID : ANR-20-CE15-0009-01
Organisme : Agence Nationale de la Recherche
ID : ANR-22-CE11-0030-03
Organisme : Fondation pour la Recherche Médicale
ID : EQU202103012926
Organisme : European Research Council
ID : 101062030
Pays : International