ACKR3 Proximity Labeling Identifies Novel G protein- and ß-arrestin-independent GPCR Interacting Proteins.
bioRxiv
; 2024 Jan 28.
Article
em En
| MEDLINE
| ID: mdl-38410489
ABSTRACT
The canonical paradigm of GPCR signaling recognizes G proteins and ß-arrestins as the two primary transducers that promote GPCR signaling. Recent evidence suggests the atypical chemokine receptor 3 (ACKR3) does not couple to G proteins, and ß-arrestins are dispensable for some of its functions. Here, we employed proximity labeling to identify proteins that interact with ACKR3 in cells devoid of ß-arrestin. We identified proteins involved in the endocytic machinery and evaluated a subset of proteins conserved across several GPCR-based proximity labeling experiments. We discovered that the bone morphogenic protein 2-inducible kinase (BMP2K) interacts with many different GPCRs with varying dependency on ß-arrestin. Together, our work highlights the existence of modulators that can act independently of G proteins and ß-arrestins to regulate GPCR signaling and provides important evidence for other targets that may regulate GPCR signaling.
G protein; G protein-coupled receptor; G protein-coupled receptor kinase; GPCR interacting proteins; GPCR trafficking; ascorbate peroxidase enzyme 2; atypical chemokine receptor 3; biased agonism; bone morphogenic protein 2-inducible kinase; noncanonical GPCR signaling; proximity labeling; ß-arrestin
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Idioma:
En
Revista:
BioRxiv
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
Estados Unidos