Fusion of the <scp> β <sub>2</sub> ‐adrenergic </scp> receptor with either Gαs or βarrestin‐2 produces constitutive signaling by each pathway and induces <scp>gain‐of‐function</scp> in <scp>BEAS‐2B</scp> cells-Reference-Cited by-同舟云学术

Fusion of the β ₂ ‐adrenergic receptor with either Gαs or βarrestin‐2 produces constitutive signaling by each pathway and induces gain‐of‐function in BEAS‐2B cells

Published:2022-09-24 Issue:12 Volume:4 Page:758-774
ISSN:2573-9832
Container-title:FASEB BioAdvances
language:en
Short-container-title:FASEB BioAdvances

Author:

Lucero‐Garcia Rojas Emilio Y.¹^ORCID,Reyes‐Alcaraz Arfaxad¹,Ruan Kehe¹,McConnell Bradley K.¹^ORCID,Bond Richard A.¹^ORCID

Affiliation:

1. Department of Pharmacology and Pharmaceutical Sciences, College of Pharmacy University of Houston Houston Texas USA

Funder

American Heart Association

National Heart, Lung, and Blood Institute

National Institutes of Health

Publisher

Wiley

Subject

Cancer Research,Biochemistry, Genetics and Molecular Biology (miscellaneous),Molecular Medicine,Physiology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fba.2022-00038

Reference41 articles.

1. Mechanisms of signalling and biased agonism in G protein-coupled receptors

2. Phosphorylation of the mammalian beta‐adrenergic receptor by cyclic AMP‐dependent protein kinase. Regulation of the rate of receptor phosphorylation and dephosphorylation by agonist occupancy and effects on coupling of the receptor to the stimulatory guanine nucleotide regulatory protein;Benovic JL;J Biol Chem,1985

3. Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor.

4. β-Arrestin-Dependent Formation of β 2 Adrenergic Receptor-Src Protein Kinase Complexes

5. Biased Receptor Signaling in Drug Discovery

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