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.

  • Structure Watch
  • Published:

Structure Watch

Nature Reviews Molecular Cell Biology volume 14, page 546 (2013)Cite this article

Subjects

Brassinosteroids are hormones that are important for plant growth, development and immune responses. They are sensed by the transmembrane receptor kinase BRASSINOSTEROID INSENSITIVE 1 (BRI1) when they bind to its extracellular Leu-rich repeat (LRR) domain. Brassinosteroid binding to BRI1 is known to induce conformational changes that create a platform in BRI1 for co-receptor binding. Somatic embryogenesis receptor kinases (SERKs; which are also receptor kinases with LRR ectodomains) have been implicated in mediating brassinosteroid signalling, and their size and membrane localization makes them BRI1 co-receptor candidates. This study reveals that BRI1 and SERK1 interact to activate BRI1 signalling. The authors solved the crystal structure of a ternary complex formed by BRI1, the LRR ectodomain of SERK1 and the hormone at 3.3 Å resolution. Their findings indicate that the SERK1 LRR domain forms an integral part of the ligand-binding pocket of the receptor and thus that BRI1 and SERK1 interact in a ligand-dependent manner. Therefore, the activation of the cytoplasmic kinase domain of BRI1, the underlying mechanism of which was unclear, involves BRI1–SERK1 heterodimerization following extracellular hormone binding at the cell surface.

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

Access options

Buy this article

  • Purchase on SpringerLink
  • Instant access to the full article PDF.

USD 39.95

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

References

  1. Santiago, J., Henzler, C. & Hothorn, M. Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases. Science http://dx.doi.org/10.1126/science.1242468 (2013)

Download references

Authors
  1. Kim Baumann
    View author publications

    Search author on:PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Baumann, K. Structure Watch. Nat Rev Mol Cell Biol 14, 546 (2013). https://doi.org/10.1038/nrm3655

Download citation

  • Published:

  • Issue date:

  • DOI: https://doi.org/10.1038/nrm3655

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