Podosome formation promotes plasma membrane invagination and integrin-β3 endocytosis on a viscous RGD-membrane.
Actins
/ metabolism
Adaptor Proteins, Signal Transducing
/ genetics
Adaptor Proteins, Vesicular Transport
/ genetics
Animals
Cell Adhesion
Cell Membrane
/ metabolism
Cells, Cultured
Clathrin
/ genetics
Dynamin II
/ genetics
Endocytosis
/ genetics
Fibroblasts
/ metabolism
Gene Knockdown Techniques
Humans
Integrin beta3
/ genetics
Ligands
Membranes, Artificial
Mice
Nerve Tissue Proteins
/ genetics
Oligopeptides
/ metabolism
Podosomes
/ metabolism
Polymerization
Rats
Transfection
Tumor Suppressor Proteins
/ genetics
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
13 03 2020
13 03 2020
Historique:
received:
26
05
2019
accepted:
21
02
2020
entrez:
15
3
2020
pubmed:
15
3
2020
medline:
10
2
2021
Statut:
epublish
Résumé
Integrin receptors orchestrate cell adhesion and cytoskeletal reorganization. The endocytic mechanism of integrin-β3 receptor at the podosome remains unclear. Using viscous RGD-membrane as the model system, here we show that the formation of podosome-like adhesion promotes Dab2/clathrin-mediated endocytosis of integrin-β3. Integrin-β3 and RGD ligand are endocytosed from the podosome and sorted into the endosomal compartment. Inhibitions of podosome formation and knockdowns of Dab2 and clathrin reduce RGD endocytosis. F-actin assembly at the podosome core exhibits protrusive contact towards the substrate and results in plasma membrane invaginations at the podosome ring. BIN1 specifically associates with the region of invaginated membrane and recruits DNM2. During the podosome formation, BIN1 and DNM2 synchronously enrich at the podosome ring and trigger clathrin dissociation and RGD endocytosis. Knockdowns of BIN1 and DNM2 suppress RGD endocytosis. Thus, plasma membrane invagination caused by F-actin polymerization promotes BIN1-dependent DNM2 recruitment and facilitate integrin-β3 endocytosis at the podosome.
Identifiants
pubmed: 32170110
doi: 10.1038/s42003-020-0843-2
pii: 10.1038/s42003-020-0843-2
pmc: PMC7070051
doi:
Substances chimiques
Actins
0
Adaptor Proteins, Signal Transducing
0
Adaptor Proteins, Vesicular Transport
0
Bin1 protein, rat
0
Clathrin
0
Dab2 protein, rat
0
Integrin beta3
0
Ligands
0
Membranes, Artificial
0
Nerve Tissue Proteins
0
Oligopeptides
0
Tumor Suppressor Proteins
0
arginyl-glycyl-aspartic acid
78VO7F77PN
Dynamin II
EC 3.6.5.5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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