Imperial College London


Faculty of MedicineDepartment of Metabolism, Digestion and Reproduction

Reader in Cell Biology



+44 (0)20 7594 2128a.hanyaloglu Website




Miss Kiran Dosanjh +44 (0)20 7594 2176




2009Institute of Reproductive and Developmental BiologyHammersmith Campus






BibTex format

author = {Hanyaloglu, AC and Fanelli, F and Jonas, KC},
booktitle = {Receptors},
doi = {10.1007/978-3-319-60174-8_8},
pages = {207--231},
title = {Class A GPCR: Di/oligomerization of glycoprotein hormone receptors},
url = {},
year = {2017}

RIS format (EndNote, RefMan)

AB - © Springer International Publishing AG 2017. G protein-coupled receptor (GPCR) dimerization and oligomerization was first described over 2 decades ago, contributing to the recent paradigm shift in GPCR signaling of a simplistic, archetypal view involving single receptors activating specific heterotrimeric G proteins at the cell surface, to one of an increasing complex receptor signaling system. However, our understanding of how dimerization and oligomerization, particularly homomerization, generates functional diversity in GPCR signaling is poorly understood. For the Class A/rhodopsin subfamily of glycoprotein hormone receptors (GpHRs), di/oligomerization has been demonstrated to play a significant role in regulating its signal activity at a cellular and physiological level and even pathophysiologically. Here we will describe and discuss the developments in our understanding of GPCR oligomerization, primarily the role of homomeric receptor complexes, in both health and disease, from the study of this unique and complex subfamily of GPCRs.
AU - Hanyaloglu,AC
AU - Fanelli,F
AU - Jonas,KC
DO - 10.1007/978-3-319-60174-8_8
EP - 231
PY - 2017///
SP - 207
TI - Class A GPCR: Di/oligomerization of glycoprotein hormone receptors
T1 - Receptors
UR -
ER -