Ubiquitin ligase CHFR mediated degradation of VE-cadherin through ubiquitylation disrupts endothelial adherens junctions.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
18 10 2023
18 10 2023
Historique:
received:
15
09
2022
accepted:
04
10
2023
medline:
23
10
2023
pubmed:
19
10
2023
entrez:
18
10
2023
Statut:
epublish
Résumé
Vascular endothelial cadherin (VE-cadherin) expressed at endothelial adherens junctions (AJs) is vital for vascular integrity and endothelial homeostasis. Here we identify the requirement of the ubiquitin E3-ligase CHFR as a key mechanism of ubiquitylation-dependent degradation of VE-cadherin. CHFR was essential for disrupting the endothelium through control of the VE-cadherin protein expression at AJs. We observe augmented expression of VE-cadherin in endothelial cell (EC)-restricted Chfr knockout (Chfr
Identifiants
pubmed: 37852964
doi: 10.1038/s41467-023-42225-2
pii: 10.1038/s41467-023-42225-2
pmc: PMC10584835
doi:
Substances chimiques
cadherin 5
0
Ubiquitin
0
Ligases
EC 6.-
Lipopolysaccharides
0
Cadherins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
6582Subventions
Organisme : NHLBI NIH HHS
ID : R01 HL156965
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM138499
Pays : United States
Organisme : NHLBI NIH HHS
ID : P01 HL160469
Pays : United States
Informations de copyright
© 2023. Springer Nature Limited.
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