Exploration into Galectin-3 Driven Endocytosis and Lattices.


Journal

Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414

Informations de publication

Date de publication:
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

Auteurs

Massiullah Shafaq-Zadah (M)

Cellular and Chemical Biology Unit, Institut Curie, Paris Sciences & Lettres Research University, U1143 INSERM, UMR3666 CNRS, 75248 Paris, France.

Estelle Dransart (E)

Cellular and Chemical Biology Unit, Institut Curie, Paris Sciences & Lettres Research University, U1143 INSERM, UMR3666 CNRS, 75248 Paris, France.

Satish Kailasam Mani (SK)

Cellular and Chemical Biology Unit, Institut Curie, Paris Sciences & Lettres Research University, U1143 INSERM, UMR3666 CNRS, 75248 Paris, France.

Julio Lopes Sampaio (JL)

CurieCoreTech-Metabolomics and Lipidomics Platform, Institute Curie, 75248 Paris, France.

Lydia Bouidghaghen (L)

CurieCoreTech-Metabolomics and Lipidomics Platform, Institute Curie, 75248 Paris, France.

Ulf J Nilsson (UJ)

Department of Chemistry, Lund University, 221 00 Lund, Sweden.

Hakon Leffler (H)

Section MIG (Microbiology, Immunology, Glycobiology), Department of Laboratory Medicine, Lund University, 221 00 Lund, Sweden.

Ludger Johannes (L)

Cellular and Chemical Biology Unit, Institut Curie, Paris Sciences & Lettres Research University, U1143 INSERM, UMR3666 CNRS, 75248 Paris, France.

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Classifications MeSH