EphB1 interaction with caveolin-1 in endothelial cells modulates caveolae biogenesis.
Journal
Molecular biology of the cell
ISSN: 1939-4586
Titre abrégé: Mol Biol Cell
Pays: United States
ID NLM: 9201390
Informations de publication
Date de publication:
15 05 2020
15 05 2020
Historique:
pubmed:
3
4
2020
medline:
14
5
2021
entrez:
3
4
2020
Statut:
ppublish
Résumé
Caveolae, the cave-like structures abundant in endothelial cells (ECs), are important for multiple signaling processes such as production of nitric oxide and caveolae-mediated intracellular trafficking. Using superresolution microscopy, fluorescence resonance energy transfer, and biochemical analysis, we observed that the EphB1 receptor tyrosine kinase constitutively interacts with caveolin-1 (Cav-1), the key structural protein of caveolae. Activation of EphB1 with its ligand Ephrin B1 induced EphB1 phosphorylation and the uncoupling EphB1 from Cav-1 and thereby promoted phosphorylation of Cav-1 by
Identifiants
pubmed: 32238105
doi: 10.1091/mbc.E19-12-0713
pmc: PMC7353165
doi:
Substances chimiques
Caveolin 1
0
Efnb1 protein, mouse
0
Ephrin-B1
0
Nitric Oxide
31C4KY9ESH
Receptor Protein-Tyrosine Kinases
EC 2.7.10.1
Receptor, EphB1
EC 2.7.10.1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
1167-1182Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM117028
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL142636
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL128359
Pays : United States
Organisme : NHLBI NIH HHS
ID : P01 HL060678
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL122157
Pays : United States
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