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Mol. Cells 2010; 29(3): 283-290

Published online January 14, 2010

https://doi.org/10.1007/s10059-010-0035-x

© The Korean Society for Molecular and Cellular Biology

Phosphorylation Dependent Nucleocytoplasmic Shuttling of BES1 Is a Key Regulatory Event in Brassinosteroid Signaling

Hojin Ryu, Hyunwoo Cho, Kangmin Kim, and Ildoo Hwang*

Department of Life Sciences, Pohang University of Science and Technology, Pohang 790-894, Korea

Correspondence to : *Correspondence: ihwang@postech.ac.kr

Received: November 3, 2009; Accepted: November 23, 2009

Abstract

Brassinosteroids (BRs) play important roles in plant growth and development. BRs modulate the phosphorylation status of two crucial transcription factors, BRI1 EMS SUPPRESSOR1 (BES1) and BRASSINAZOLE RESISTANT1 (BZR1). Here we show that BES1 functions as a nucleocytoplasmic signal transmitter, and that its subcellular localization modulates the output intensity of the BR signal. BRASSINOSTEROID INSENSITIVE2 (BIN2) and other group II GLYCOGEN SYNTHASE KINASE 3 (GSK3)-like kinases phosphorylate BES1 and induce its nuclear export by regulating its binding affinity with 14-3-3 proteins. We identified twelve putative phosphorylation residues in BES1. Two of these residues, Ser 171 and Thr 175, are critical for interaction with 14-3-3 proteins. The other putative phosphorylation sites in the N-terminal region are required for the BIN2-mediated nuclear export of BES1. Mutations of these motifs result in increased nuclear accumulation of BES1 and enhanced BR responses in transgenic plants. Taken together, our results indicate that the spatial redistribution of BES1 is important for regulation of the BR signaling output.

Keywords BES1, BIN2, Brassinosteroid, nucleocytoplasmic shuttling, phosphorylation

Article

Research Article

Mol. Cells 2010; 29(3): 283-290

Published online March 31, 2010 https://doi.org/10.1007/s10059-010-0035-x

Copyright © The Korean Society for Molecular and Cellular Biology.

Phosphorylation Dependent Nucleocytoplasmic Shuttling of BES1 Is a Key Regulatory Event in Brassinosteroid Signaling

Hojin Ryu, Hyunwoo Cho, Kangmin Kim, and Ildoo Hwang*

Department of Life Sciences, Pohang University of Science and Technology, Pohang 790-894, Korea

Correspondence to:*Correspondence: ihwang@postech.ac.kr

Received: November 3, 2009; Accepted: November 23, 2009

Abstract

Brassinosteroids (BRs) play important roles in plant growth and development. BRs modulate the phosphorylation status of two crucial transcription factors, BRI1 EMS SUPPRESSOR1 (BES1) and BRASSINAZOLE RESISTANT1 (BZR1). Here we show that BES1 functions as a nucleocytoplasmic signal transmitter, and that its subcellular localization modulates the output intensity of the BR signal. BRASSINOSTEROID INSENSITIVE2 (BIN2) and other group II GLYCOGEN SYNTHASE KINASE 3 (GSK3)-like kinases phosphorylate BES1 and induce its nuclear export by regulating its binding affinity with 14-3-3 proteins. We identified twelve putative phosphorylation residues in BES1. Two of these residues, Ser 171 and Thr 175, are critical for interaction with 14-3-3 proteins. The other putative phosphorylation sites in the N-terminal region are required for the BIN2-mediated nuclear export of BES1. Mutations of these motifs result in increased nuclear accumulation of BES1 and enhanced BR responses in transgenic plants. Taken together, our results indicate that the spatial redistribution of BES1 is important for regulation of the BR signaling output.

Keywords: BES1, BIN2, Brassinosteroid, nucleocytoplasmic shuttling, phosphorylation

Mol. Cells
May 31, 2023 Vol.46 No.5, pp. 259~328
COVER PICTURE
The alpha-helices in the lamin filaments are depicted as coils, with different subdomains distinguished by various colors. Coil 1a is represented by magenta, coil 1b by yellow, L2 by green, coil 2a by white, coil 2b by brown, stutter by cyan, coil 2c by dark blue, and the lamin Ig-like domain by grey. In the background, cells are displayed, with the cytosol depicted in green and the nucleus in blue (Ahn et al., pp. 309-318).

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