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.

PubMed Disclaimer

Cited by

Structural-Functional Features of the Thyrotropin Receptor: A Class A G-Protein-Coupled Receptor at Work.
Kleinau G, Worth CL, Kreuchwig A, Biebermann H, Marcinkowski P, Scheerer P, Krause G. Kleinau G, et al. Front Endocrinol (Lausanne). 2017 Apr 24;8:86. doi: 10.3389/fendo.2017.00086. eCollection 2017. Front Endocrinol (Lausanne). 2017. PMID: 28484426 Free PMC article. Review.
Membranes on the move: The functional role of the extracellular vesicle membrane for contact-dependent cellular signalling.
Jahnke K, Staufer O. Jahnke K, et al. J Extracell Vesicles. 2024 Apr;13(4):e12436. doi: 10.1002/jev2.12436. J Extracell Vesicles. 2024. PMID: 38649339 Free PMC article. Review.
Extracellular bimolecular fluorescence complementation for investigating membrane protein dimerization: a proof of concept using class B GPCRs.
Garelja ML, Alexander TI, Walker CS, Hay DL. Garelja ML, et al. Biosci Rep. 2024 Oct 30;44(10):BSR20240449. doi: 10.1042/BSR20240449. Biosci Rep. 2024. PMID: 39361899 Free PMC article.
New Insights into the Structure and Function of Class B1 GPCRs.
Cary BP, Zhang X, Cao J, Johnson RM, Piper SJ, Gerrard EJ, Wootten D, Sexton PM. Cary BP, et al. Endocr Rev. 2023 May 8;44(3):492-517. doi: 10.1210/endrev/bnac033. Endocr Rev. 2023. PMID: 36546772 Free PMC article.
Single-molecule imaging reveals dimerization/oligomerization of CXCR4 on plasma membrane closely related to its function.
Ge B, Lao J, Li J, Chen Y, Song Y, Huang F. Ge B, et al. Sci Rep. 2017 Dec 4;7(1):16873. doi: 10.1038/s41598-017-16802-7. Sci Rep. 2017. PMID: 29203889 Free PMC article.

See all "Cited by" articles

References

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
1. 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
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
1. 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
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

LinkOut - more resources

Full Text Sources
Other Literature Sources
- scite Smart Citations

[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

Save citation to file

Email citation

Add to Collections

Add to My Bibliography

Your saved search

Create a file for external citation management software

Your RSS Feed

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

Affiliation

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

Authors

Affiliation

Abstract

Similar articles

Cited by

References

LinkOut - more resources

Full Text Sources

Other Literature Sources

Abstract

Similar articles

Cited by

References

Related information

LinkOut - more resources

Full Text Sources

Other Literature Sources