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.

Structural biology

Active arrestin proteins crystallized

Nature volume 497, pages 45–46 (2013)Cite this article

Subjects

Arrestin proteins regulate cellular signalling cascades initiated by ubiquitous G-protein-coupled receptors. Crystal structures reveal that two arrestins undergo similar structural changes on activation. See Letters p.137 & p.142

Physical abilities, cognitive skills and many other activities of humans and other organisms are generated by the coordinated actions of millions of cells. Each cell contributes to these activities by interacting with molecules outside itself. Many of these interactions are mediated through G-protein-coupled receptors (GPCRs), which in turn activate the eponymous intracellular G proteins, and so act as the starting points for numerous cellular signalling pathways. Arrestin proteins regulate the activity of these pathways by interacting with GPCRs, thus preventing G-protein-induced signalling and/or inducing additional signalling through G-protein-independent pathways. Two papers1,2 in this issue report the first X-ray crystal structures of arrestins in their active statesFootnote 1.

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

Access options

Rent or buy this article

Prices vary by article type

from$1.95

to$39.95

Learn more

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

Figure 1: Comparison of inactive and active arrestins.

Notes

  1. *This article and the papers under discussion1,2 were published online on 24 April 2013.

References

  1. Kim, Y. J. et al. Nature 497, 142–146 (2013).

    Article  ADS  CAS  PubMed  Google Scholar 

  2. Shukla, A. K. et al. Nature 497, 137–141 (2013).

    Article  ADS  CAS  PubMed  PubMed Central  Google Scholar 

  3. Palczewski, K. et al. Science 289, 739–745 (2000).

    Article  ADS  CAS  PubMed  Google Scholar 

  4. Granzin, J. et al. Nature 391, 918–921 (1998).

    Article  ADS  CAS  PubMed  Google Scholar 

  5. Hirsch, J. A., Schubert, C., Gurevich, V. V. & Sigler, P. B. Cell 97, 257–269 (1999).

    Article  CAS  PubMed  Google Scholar 

  6. Choe, H.-W. et al. Nature 471, 651–655 (2011).

    Article  ADS  CAS  PubMed  Google Scholar 

  7. Granzin, J. et al. J. Mol. Biol. 416, 611–618 (2012).

    Article  CAS  PubMed  Google Scholar 

  8. Han, M., Gurevich, V. V., Vishnivetskiy, S. A., Sigler, P. B. & Schubert, C. Structure 9, 869–880 (2001).

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Valentin Borshchevskiy and Georg Büldt are at the Institute of Complex Systems (ICS-5), Research Centre Jülich, 52425 Jülich, Germany, and at the Moscow Institute of Physics and Technology, Russia.,

    Valentin Borshchevskiy & Georg Büldt

Authors
  1. Valentin Borshchevskiy
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Georg Büldt
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Georg Büldt.

Related links

Related links

Related links in Nature Research

NOBEL 2012 Chemistry: Studies of a ubiquitous receptor family

https://doi.org/10.1038/11634

Structural biology: Snapshot of a signalling complex

Cell signalling: Binding the receptor at both ends

Structural biology: A receptor unlocked

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Borshchevskiy, V., Büldt, G. Active arrestin proteins crystallized. Nature 497, 45–46 (2013). https://doi.org/10.1038/nature12096

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nature12096

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