Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Sci. Signal., 26 June 2012
Vol. 5, Issue 230, p. pe28
[DOI: 10.1126/scisignal.2003274]

PERSPECTIVES

How Plant Lysin Motif Receptors Get Activated: Lessons Learned from Structural Biology

Roland Willmann* and Thorsten Nürnberger*

University of Tübingen, Center for Plant Molecular Biology (ZMBP)–Plant Biochemistry, D-72076 Tübingen, Germany.

Abstract: Lysin motif (LysM) receptor kinases are unique to plants and serve important functions in plant-microbe interactions. These proteins recognize microbe-derived N-acetylglucosamine (NAG)–containing ligands, but the molecular mode of ligand perception and of receptor activation has remained unknown. The three-dimensional structure of the LysM receptor kinase CERK1 (chitin elicitor receptor kinase 1) from Arabidopsis thaliana has been reported. CERK1 binds NAG oligomers derived from chitin—the major constituent of fungal cell walls—and mediates immunity to fungal infection. The crystal structure of CERK1 complexed with a NAG pentamer revealed that three NAG moieties attach tightly to one of three lysin motifs within the CERK1 ectodomain. Receptor activation and immune signaling requires, however, ligand-induced CERK1 homodimerization. By acting as bivalent ligands, NAG octamers stabilize CERK1 dimers, providing a structural explanation for why the immunogenic activity of NAG oligomers is restricted to fragments larger than those required for receptor binding. Because CERK1 might serve as a paradigm for the functionality of a whole class of plant LysM proteins, insight into its mode of action will direct future research on these receptors.

* Corresponding authors. E-mail: roland.willmann{at}uni-tuebingen.de (R.W.); nuernberger{at}uni-tuebingen.de (T.N.)

Citation: R. Willmann, T. Nürnberger, How Plant Lysin Motif Receptors Get Activated: Lessons Learned from Structural Biology. Sci. Signal. 5, pe28 (2012).

Read the Full Text



To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882