Role of post-translational modifications on structure, function and pharmacology of class C G protein-coupled receptors

TY - JOUR

T1 - Role of post-translational modifications on structure, function and pharmacology of class C G protein-coupled receptors

AU - Nørskov-Lauritsen, Lenea

AU - Bräuner-Osborne, Hans

N1 - Copyright © 2015. Published by Elsevier B.V.

PY - 2015/9/15

Y1 - 2015/9/15

N2 - G protein-coupled receptors are divided into three classes (A, B and C) based on homology of their seven transmembrane domains. Class C is the smallest class with 22 human receptor subtypes including eight metabotropic glutamate (mGlu1-8) receptors, two GABAB receptors (GABAB1 and GABAB2), three taste receptors (T1R1-3), one calcium-sensing (CaS) receptor, one GPCR, class C, group 6, subtype A (GPRC6) receptor, and seven orphan receptors. G protein-coupled receptors undergo a number of post-translational modifications, which regulate their structure, function and/or pharmacology. Here, we review the existence of post-translational modifications in class C G protein-coupled receptors and their regulatory roles, with particular focus on glycosylation, phosphorylation, ubiquitination, SUMOylation, disulphide bonding and lipidation.

AB - G protein-coupled receptors are divided into three classes (A, B and C) based on homology of their seven transmembrane domains. Class C is the smallest class with 22 human receptor subtypes including eight metabotropic glutamate (mGlu1-8) receptors, two GABAB receptors (GABAB1 and GABAB2), three taste receptors (T1R1-3), one calcium-sensing (CaS) receptor, one GPCR, class C, group 6, subtype A (GPRC6) receptor, and seven orphan receptors. G protein-coupled receptors undergo a number of post-translational modifications, which regulate their structure, function and/or pharmacology. Here, we review the existence of post-translational modifications in class C G protein-coupled receptors and their regulatory roles, with particular focus on glycosylation, phosphorylation, ubiquitination, SUMOylation, disulphide bonding and lipidation.

U2 - 10.1016/j.ejphar.2015.05.015

DO - 10.1016/j.ejphar.2015.05.015

M3 - Journal article

C2 - 25981296

SN - 0014-2999

VL - 763

SP - 233

EP - 240

JO - European Journal of Pharmacology

JF - European Journal of Pharmacology

ER -