Receptor oligomerization: from early evidence to current understanding in class B GPCRs

doi:10.3389/fendo.2012.00175

. 2013 Jan 4:3:175.

doi: 10.3389/fendo.2012.00175. eCollection 2012.

Receptor oligomerization: from early evidence to current understanding in class B GPCRs

Stephanie Y L Ng¹, Leo T O Lee, Billy K C Chow

Affiliations

PMID: 23316183
PMCID: PMC3539651
DOI: 10.3389/fendo.2012.00175

Receptor oligomerization: from early evidence to current understanding in class B GPCRs

Stephanie Y L Ng et al. Front Endocrinol (Lausanne). 2013.

. 2013 Jan 4:3:175.

doi: 10.3389/fendo.2012.00175. eCollection 2012.

Authors

Stephanie Y L Ng¹, Leo T O Lee, Billy K C Chow

Affiliation

¹ Endocrinology, School of Biological Sciences, The University of Hong Kong Hong Kong, China.

PMID: 23316183
PMCID: PMC3539651
DOI: 10.3389/fendo.2012.00175

Abstract

Dimerization or oligomerization of G protein-coupled receptors (GPCRs) are known to modulate receptor functions in terms of ontogeny, ligand-oriented regulation, pharmacological diversity, signal transduction, and internalization. Class B GPCRs are receptors to a family of hormones including secretin, growth hormone-releasing hormone, vasoactive intestinal polypeptide and parathyroid hormone, among others. The functional implications of receptor dimerization have extensively been studied in class A GPCRs, while less is known regarding its function in class B GPCRs. This article reviews receptor oligomerization in terms of the early evidence and current understanding particularly of class B GPCRs.

Keywords: BRET; GPCR; class B; oligomerization; secretin receptor.

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References

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1. Ayoub M. A., Levoye A., Delagrange P., Jockers R. (2004). Preferential formation of MT1/MT2 melatonin receptor heterodimers with distinct ligand interaction properties compared with MT2 homodimers. Mol. Pharmacol. 66 312–321 - PubMed
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1. Bayburt T. H., Vishnivetskiy S. A., Mclean M. A., Morizumi T., Huang C. C., Tesmer J. J., et al. (2011). Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding. J. Biol. Chem. 286 1420–1428 - PMC - PubMed

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[1] Albizu L., Balestre M. N., Breton C., Pin J. P., Manning M., Mouillac B., et al. (2006). Probing the existence of G protein-coupled receptor dimers by positive and negative ligand-dependent cooperative binding. Mol. Pharmacol. 70 1783–1791 - PubMed

[2] Albizu L., Balestre M. N., Breton C., Pin J. P., Manning M., Mouillac B., et al. (2006). Probing the existence of G protein-coupled receptor dimers by positive and negative ligand-dependent cooperative binding. Mol. Pharmacol. 70 1783–1791 - PubMed

[3] Avissar S., Amitai G., Sokolovsky M. (1983). Oligomeric structure of muscarinic receptors is shown by photoaffinity labeling: subunit assembly may explain high- and low-affinity agonist states. Proc. Natl. Acad. Sci. U.S.A. 80 156–159 - PMC - PubMed

[4] Avissar S., Amitai G., Sokolovsky M. (1983). Oligomeric structure of muscarinic receptors is shown by photoaffinity labeling: subunit assembly may explain high- and low-affinity agonist states. Proc. Natl. Acad. Sci. U.S.A. 80 156–159 - PMC - PubMed

[5] Ayoub M. A., Levoye A., Delagrange P., Jockers R. (2004). Preferential formation of MT1/MT2 melatonin receptor heterodimers with distinct ligand interaction properties compared with MT2 homodimers. Mol. Pharmacol. 66 312–321 - PubMed

[6] Ayoub M. A., Levoye A., Delagrange P., Jockers R. (2004). Preferential formation of MT1/MT2 melatonin receptor heterodimers with distinct ligand interaction properties compared with MT2 homodimers. Mol. Pharmacol. 66 312–321 - PubMed

[7] Bai M., Trivedi S., Brown E. M. (1998). Dimerization of the extracellular calcium-sensing receptor (CaR) on the cell surface of CaR-transfected HEK293 cells. J. Biol. Chem. 273 23605–23610 - PubMed

[8] Bai M., Trivedi S., Brown E. M. (1998). Dimerization of the extracellular calcium-sensing receptor (CaR) on the cell surface of CaR-transfected HEK293 cells. J. Biol. Chem. 273 23605–23610 - PubMed

[9] Bayburt T. H., Vishnivetskiy S. A., Mclean M. A., Morizumi T., Huang C. C., Tesmer J. J., et al. (2011). Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding. J. Biol. Chem. 286 1420–1428 - PMC - PubMed

[10] Bayburt T. H., Vishnivetskiy S. A., Mclean M. A., Morizumi T., Huang C. C., Tesmer J. J., et al. (2011). Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding. J. Biol. Chem. 286 1420–1428 - PMC - PubMed

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Receptor oligomerization: from early evidence to current understanding in class B GPCRs

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Receptor oligomerization: from early evidence to current understanding in class B GPCRs

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