A Mutation in the Second Transmembrane Region of the CB1 Receptor Selectively Disrupts G Protein Signaling and Prevents Receptor Internalization

1999 ◽  
Vol 56 (3) ◽  
pp. 611-618 ◽  
Author(s):  
John P. Roche ◽  
Sid Bounds ◽  
Sean Brown ◽  
Ken Mackie
Keyword(s):  
G Protein ◽  
Cb1 Receptor ◽  
Receptor Internalization ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Transmembrane Region

Elevated levels of endocannabinoids and CB1 receptor-mediated G-protein signaling in the prefrontal cortex of alcoholic suicide victims

2005 ◽  
Vol 57 (5) ◽  
pp. 480-486 ◽  
Author(s):  
K. Yaragudri Vinod ◽  
Victoria Arango ◽  
Shan Xie ◽  
Suham A. Kassir ◽  
J. John Mann ◽  
...  
Keyword(s):  
Prefrontal Cortex ◽  
G Protein ◽  
Cb1 Receptor ◽  
G Protein Signaling ◽  
Protein Signaling

scholarly journals Antipsychotic-induced alterations in CB1 receptor-mediated G-protein signaling and in vivo pharmacology in rats

2008 ◽  
Vol 55 (7) ◽  
pp. 1183-1190 ◽  
Author(s):  
Jenny L. Wiley ◽  
Seth H. Kendler ◽  
James J. Burston ◽  
Daniel R. Howard ◽  
Dana E. Selley ◽  
...  
Keyword(s):  
G Protein ◽  
Cb1 Receptor ◽  
G Protein Signaling ◽  
Protein Signaling

scholarly journals Distinct conformations of GPCR–β-arrestin complexes mediate desensitization, signaling, and endocytosis

2017 ◽  
Vol 114 (10) ◽  
pp. 2562-2567 ◽  
Author(s):  
Thomas J. Cahill ◽  
Alex R. B. Thomsen ◽  
Jeffrey T. Tarrasch ◽  
Bianca Plouffe ◽  
Anthony H. Nguyen ◽  
...  
Keyword(s):  
G Protein ◽  
Receptor Internalization ◽  
G Protein Signaling ◽  
Mutant Form ◽  
Protein Signaling ◽  
The Core ◽  
Loop Region ◽  
Relationship Of ◽  
The Relationship ◽  
G Protein Coupled

β-Arrestins (βarrs) interact with G protein-coupled receptors (GPCRs) to desensitize G protein signaling, to initiate signaling on their own, and to mediate receptor endocytosis. Prior structural studies have revealed two unique conformations of GPCR–βarr complexes: the “tail” conformation, with βarr primarily coupled to the phosphorylated GPCR C-terminal tail, and the “core” conformation, where, in addition to the phosphorylated C-terminal tail, βarr is further engaged with the receptor transmembrane core. However, the relationship of these distinct conformations to the various functions of βarrs is unknown. Here, we created a mutant form of βarr lacking the “finger-loop” region, which is unable to form the core conformation but retains the ability to form the tail conformation. We find that the tail conformation preserves the ability to mediate receptor internalization and βarr signaling but not desensitization of G protein signaling. Thus, the two GPCR–βarr conformations can carry out distinct functions.

Sign in / Sign up

Export Citation Format

Share Document