Unknown

Dataset Information

0

GPCRs and Signal Transducers: Interaction Stoichiometry.


ABSTRACT: Until the late 1990s, class A G protein-coupled receptors (GPCRs) were believed to function as monomers. Indirect evidence that they might internalize or even signal as dimers has emerged, along with proof that class C GPCRs are obligatory dimers. Crystal structures of GPCRs and their much larger binding partners were consistent with the idea that two receptors might engage a single G protein, GRK, or arrestin. However, recent biophysical, biochemical, and structural evidence invariably suggests that a single GPCR binds G proteins, GRKs, and arrestins. Here we review existing evidence of the stoichiometry of GPCR interactions with signal transducers and discuss potential biological roles of class A GPCR oligomers, including proposed homo- and heterodimers.

SUBMITTER: Gurevich VV 

PROVIDER: S-EPMC6005764 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

GPCRs and Signal Transducers: Interaction Stoichiometry.

Gurevich Vsevolod V VV   Gurevich Eugenia V EV  

Trends in pharmacological sciences 20180505 7


Until the late 1990s, class A G protein-coupled receptors (GPCRs) were believed to function as monomers. Indirect evidence that they might internalize or even signal as dimers has emerged, along with proof that class C GPCRs are obligatory dimers. Crystal structures of GPCRs and their much larger binding partners were consistent with the idea that two receptors might engage a single G protein, GRK, or arrestin. However, recent biophysical, biochemical, and structural evidence invariably suggests  ...[more]

Similar Datasets

| S-EPMC3458427 | biostudies-literature
| S-EPMC3264485 | biostudies-literature
| S-EPMC244915 | biostudies-literature
| S-EPMC6488950 | biostudies-literature
| S-EPMC3274258 | biostudies-literature
| S-EPMC3985647 | biostudies-literature
| S-EPMC9189013 | biostudies-literature
| S-EPMC5371730 | biostudies-literature
| S-EPMC2359764 | biostudies-literature
| S-EPMC3322882 | biostudies-literature