Structure and Function of RhoBTB1 Required for Substrate Specificity and Cullin-3 Ubiquitination.
Cullin-3
RhoBTB1
co-immunoprecipitation
protein–protein interaction
proximity labeling
Journal
Function (Oxford, England)
ISSN: 2633-8823
Titre abrégé: Function (Oxf)
Pays: England
ID NLM: 101770668
Informations de publication
Date de publication:
2023
2023
Historique:
received:
15
05
2023
revised:
27
06
2023
accepted:
28
06
2023
medline:
15
8
2023
pubmed:
14
8
2023
entrez:
14
8
2023
Statut:
epublish
Résumé
We identified Rho-related BTB domain containing 1 (RhoBTB1) as a key regulator of phosphodiesterase 5 (PDE5) activity, and through PDE5, a regulator of vascular tone. We identified the binding interface for PDE5 on RhoBTB1 by truncating full-length RhoBTB1 into its component domains. Co-immunoprecipitation analyses revealed that the C-terminal half of RhoBTB1 containing its two BTB domains and the C-terminal domain (B1B2C) is the minimal region required for PDE5 recruitment and subsequent proteasomal degradation via Cullin-3 (CUL3). The C-terminal domain was essential in recruiting PDE5 as constructs lacking this region could not participate in PDE5 binding or proteasomal degradation. We also identified Pro
Identifiants
pubmed: 37575477
doi: 10.1093/function/zqad034
pii: zqad034
pmc: PMC10413933
doi:
Substances chimiques
Cullin Proteins
0
Proteasome Endopeptidase Complex
EC 3.4.25.1
RhoBTB1 protein, human
0
CUL3 protein, human
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
zqad034Subventions
Organisme : NHLBI NIH HHS
ID : P01 HL014388
Pays : United States
Organisme : NHLBI NIH HHS
ID : R35 HL144807
Pays : United States
Informations de copyright
© The Author(s) 2023. Published by Oxford University Press on behalf of American Physiological Society.
Déclaration de conflit d'intérêts
None.
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