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Sci. Signal., 10 May 2011
Vol. 4, Issue 172, p. ra29
[DOI: 10.1126/scisignal.2001258]

RESEARCH ARTICLES

Methylation of a Phosphatase Specifies Dephosphorylation and Degradation of Activated Brassinosteroid Receptors

Guang Wu1,2,3,4*{dagger}, Xiuling Wang4, Xianbin Li5, Yuji Kamiya2, Marisa S. Otegui3, and Joanne Chory1,6{dagger}

1 Plant Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
2 Plant Science Center, RIKEN, Yokohama, Kanagawa 230-0045, Japan.
3 Department of Botany, University of Wisconsin, Madison, WI 53706, USA.
4 State Key Laboratory of Crop Biology, Shandong Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Taian, Shandong 271018, PR China.
5 College of Agriculture, Shandong Agricultural University, Taian, Shandong 271018, PR China.
6 Howard Hughes Medical Institute, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.

* Present address: U.S. Department of Agriculture Plant Gene Expression Center, 800 Buchanan Street, Albany, CA 94710, USA.

Abstract: Internalization of cell surface receptors, followed by either recycling back to the plasma membrane or degradation, is crucial for receptor homeostasis and signaling. The plant brassinosteroid (BR) receptor, BRASSINOSTEROID INSENSITIVE 1 (BRI1), undergoes constitutive cycling between the plasma membrane and the internal membranes. We show that protein phosphatase 2A (PP2A) dephosphorylated BRI1 and that Arabidopsis thaliana rcn1, a mutant for a PP2A subunit, caused an increase in BRI1 abundance and BR signaling. We report the identification, in A. thaliana, of a suppressor of bri1, sbi1, which caused selective accumulation of BR-activated BRI1, but not the BR co-receptor BAK1 (BRI1-ASSOCIATED KINASE 1), in the membranous compartment. SBI1 mRNA was induced by BRs, and SBI1 encodes a leucine carboxylmethyltransferase (LCMT) that methylated PP2A and controlled its membrane-associated subcellular localization. We propose that BRs increase production of SBI1, which methylates PP2A, thus facilitating its association with activated BRI1. This leads to receptor dephosphorylation and degradation, and thus to the termination of BR signaling.

{dagger} To whom correspondence should be addressed. E-mail: gwu3{at}wisc.edu (G.W.); chory{at}salk.edu (J.C.)

Citation: G. Wu, X. Wang, X. Li, Y. Kamiya, M. S. Otegui, J. Chory, Methylation of a Phosphatase Specifies Dephosphorylation and Degradation of Activated Brassinosteroid Receptors. Sci. Signal. 4, ra29 (2011).

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