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Plant function and evolutionary biology
RESEARCH ARTICLE

Brassinosteroid-independent function of BRI1 / CLV1 chimeric receptors

Anne Diévart A B , Matthew J. Hymes A , Jianming Li A and Steven E. Clark A C
+ Author Affiliations
- Author Affiliations

A Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048, USA.

B Current address: CIRAD AMIS-BIOTROP, Avenue Agropolis — TA 40 / 03, 34398 Montpellier Cedex 5, France.

C Corresponding author. Email: clarks@umich.edu

D This paper originates from a presentation at the Third International Conference on Legume Genomics and Genetics, Brisbane, Queensland, Australia, April 2006.

Functional Plant Biology 33(8) 723-730 https://doi.org/10.1071/FP06080
Submitted: 10 April 2006  Accepted: 17 May 2006   Published: 2 August 2006

Abstract

CLAVATA1 (CLV1) and BRASSINOSTEROID INSENSITIVE 1 (BRI1) belong to the leucine-rich repeat receptor-like kinase (LRR-RLK) family, comprising more than 200 members in Arabidopsis thaliana (L.) Heynh. and playing important roles in development and defence responses in many plant species (Diévart and Clark 2003, 2004; Shiu and Bleecker 2001a, b). To dissect the mechanisms of receptor function, we assessed the ability of chimeric proteins containing regions from two different receptors to function in vivo. Using domains from the receptor-kinases CLAVATA1 and BRASSINOSTEROID INSENSITIVE1, we tested the ability of the resulting chimeric receptors to replace CLV1 function. Receptors with the BRI1 extracellular domain and CLV1 kinase domain were able to partially replace CLV1 function. Both loss-of-function and gain-of-function mutations within the BRI1 leucine-rich repeats (LRRs) altered the extent of rescue. Chimeric receptor function was unaffected by addition of either exogenous brassinosteroids (BR) or BR biosynthesis inhibitors, suggesting that the chimeric receptors function in a ligand-independent fashion. We propose that the BRI1 LRR domain drives chimeric receptor homodimerisation, and that the BRI1 LRR domain mutations influence homodimerisation efficiency independent of ligand binding.


Acknowledgments

We thank Tadao Asami for kindly providing brassinazole. This work was supported by grants from the National Institutes of Health to SEC (GM62962–05) and JL (GM60519). Anne Diévart was supported in part by the National Institutes of Health Organogenesis Training Program.


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