Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • News & Views
  • Published:

Unraveling the structural basis of GPCR activation and inactivation

Nature Structural & Molecular Biology volume 20, pages 539–541 (2013)Cite this article

Subjects

By comparing ligand-free G protein–coupled receptor (GPCR) structures with those of receptors bound to inverse agonists, agonists and signaling effectors, two recent papers refine the understanding of GPCR activation. One group also reported the oligomeric assembly of the β1 adrenergic receptor in its ligand-free form, raising the question of the role of oligomers in receptor activation.

This is a preview of subscription content, access via your institution

Relevant articles

Open Access articles citing this article.

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Alternative models describing the transition between active and inactive states in GPCRs.
Figure 2: Oligomeric states and activation of GPCRs.

References

  1. Audet, M. & Bouvier, M. Cell 151, 14–23 (2012).

    Article  CAS  Google Scholar 

  2. Huang, J., Chen, S., Zhang, J.J. & Huang, X.Y. Nat. Struct. Mol. Biol. 20, 419–425 (2013).

    Article  CAS  Google Scholar 

  3. Warne, T. et al. Nature 454, 486–491 (2008).

    Article  CAS  Google Scholar 

  4. Warne, T. et al. Nature 469, 241–244 (2011).

    Article  CAS  Google Scholar 

  5. Scheerer, P. et al. Nature 455, 497–502 (2008).

    Article  CAS  Google Scholar 

  6. Rasmussen, S.G. et al. Nature 469, 175–180 (2011).

    Article  CAS  Google Scholar 

  7. Moukhametzianov, R. et al. Proc. Natl. Acad. Sci. USA 108, 8228–8232 (2011).

    Article  CAS  Google Scholar 

  8. Nygaard, R. et al. Cell 152, 532–542 (2013).

    Article  CAS  Google Scholar 

  9. Galandrin, S., Oligny-Longpre, G. & Bouvier, M. Trends Pharmacol. Sci. 28, 423–430 (2007).

    Article  CAS  Google Scholar 

  10. Rajagopal, S., Rajagopal, K. & Lefkowitz, R.J. Nat. Rev. Drug Discov. 9, 373–386 (2010).

    Article  CAS  Google Scholar 

  11. Vaidehi, N. & Kenakin, T. Curr. Opin. Pharmacol. 10, 775–781 (2010).

    Article  CAS  Google Scholar 

  12. Bulenger, S., Marullo, S. & Bouvier, M. Trends Pharmacol. Sci. 26, 131–137 (2005).

    Article  CAS  Google Scholar 

  13. Smith, N.J. & Milligan, G. Pharmacol. Rev. 62, 701–725 (2010).

    Article  CAS  Google Scholar 

  14. Fotiadis, D. et al. Curr. Opin. Struct. Biol. 16, 252–259 (2006).

    Article  CAS  Google Scholar 

  15. Wu, B. et al. Science 330, 1066–1071 (2010).

    Article  CAS  Google Scholar 

  16. Manglik, A. et al. Nature 485, 321–326 (2012).

    Article  CAS  Google Scholar 

  17. Wu, H. et al. Nature 485, 327–332 (2012).

    Article  CAS  Google Scholar 

  18. Pin, J.P. et al. J. Physiol. (Lond.) 587, 5337–5344 (2009).

    Article  CAS  Google Scholar 

  19. Whorton, M.R. et al. Proc. Natl. Acad. Sci. USA 104, 7682–7687 (2007).

    Article  CAS  Google Scholar 

  20. Fung, J.J. et al. EMBO J. 28, 3315–3328 (2009).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Michel Bouvier is at the Department of Biochemistry, Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, Québec, Canada.,

    Michel Bouvier

Authors
  1. Michel Bouvier
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Michel Bouvier.

Ethics declarations

Competing interests

The author declares no competing financial interests.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Bouvier, M. Unraveling the structural basis of GPCR activation and inactivation. Nat Struct Mol Biol 20, 539–541 (2013). https://doi.org/10.1038/nsmb.2584

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nsmb.2584

This article is cited by

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing