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Tyrosine phosphorylation controls brassinosteroid receptor activation by triggering membrane release of its kinase inhibitor

Jaillais, Yvon and Hothorn, Michael and Belkhadir, Youssef and Dabi, Tsegaye and Nimchuk, Zachary L. and Meyerowitz, Elliot M. and Chory, Joanne (2011) Tyrosine phosphorylation controls brassinosteroid receptor activation by triggering membrane release of its kinase inhibitor. Genes and Development, 25 (3). pp. 232-237. ISSN 0890-9369. PMCID PMC3034898. doi:10.1101/gad.2001911.

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Receptor tyrosine kinases control many critical processes in metazoans, but these enzymes appear to be absent in plants. Recently, two Arabidopsis receptor kinases-BRASSINOSTEROID INSENSITIVE 1 (BRI1) and BRI1-ASSOCIATED KINASE1 (BAK1), the receptor and coreceptor for brassinosteroids-were shown to autophosphorylate on tyrosines. However, the cellular roles for tyrosine phosphorylation in plants remain poorly understood. Here, we report that the BRI1 KINASE INHIBITOR 1 (BKI1) is tyrosine phosphorylated in response to brassinosteroid perception. Phosphorylation occurs within a reiterated [KR][KR] membrane targeting motif, releasing BKI1 into the cytosol and enabling formation of an active signaling complex. Our work reveals that tyrosine phosphorylation is a conserved mechanism controlling protein localization in all higher organisms.

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Meyerowitz, Elliot M.0000-0003-4798-5153
Additional Information:© 2011 Cold Spring Harbor Laboratory Press. Received October 11, 2010; revised version accepted December 20, 2010. We thank T. Hunter and J. Meisenhelder for helpful discussions, W. Chen for technical assistance, J. Meisenhelder for designing and synthesizing peptides, and M. Dreux and U. Pedmale for providing feedback on the manuscript. The Max Planck society and SALK Institute provided insertion mutant lines, N. Geldner provided the vector pNIGEL, J. Long provided the vector pBJ36, K. Nito provided the vector TNT-Flag, R. Tsien provided mCHERRY and mCITRINE constructs, G. Stier provided plasmid pETM11, Y. Yin provided the BES1 antibody, and the NASC and ABRC provided other materials. Post-doctoral fellowships to Y.J. from the European Molecular Biology Organization, to M.H. from the International Human Frontier Science Program Organization, and from Life Sciences Research Foundation to Y.B. supported this work; Y.J. and M.H. are also supported by the Marc and Eva Stern Foundation. This work was supported by the Howard Hughes Medical Institute and grants from the National Science Foundation (IOS-0649389) (to J.C.) and the National Institutes of Health (1 R01 GM086639) (to E.M.M.). Y.J. performed the plant experiments. M.H. carried out bioinformatics analyses, calorimetry assays and purified proteins. Y.B. provided reagents and purified proteins. T.D. expressed and purified proteins. Z.L.N. carried out bioinformatics analyses and provided reagents. Y.J., M.H., Y.B., Z.L.N., E.M.M., and J.C. analyzed the data. J.C. supervised the work. Y.J., M.H., and J.C. wrote the paper.
Funding AgencyGrant Number
European Molecular Biology Organization (EMBO)UNSPECIFIED
Human Frontier Science ProgramUNSPECIFIED
Life Sciences Research FoundationUNSPECIFIED
Marc and Eva Stern FoundationUNSPECIFIED
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
NIH1 R01 GM086639
Subject Keywords:tyrosine phosphorylation; linear motif; plant receptor kinase; brassinosteroid signaling
Issue or Number:3
PubMed Central ID:PMC3034898
Record Number:CaltechAUTHORS:20110314-140440303
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:22865
Deposited By: Tony Diaz
Deposited On:15 Mar 2011 21:29
Last Modified:09 Nov 2021 16:08

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