Modulation of BIN2 kinase activity by HY5 controls hypocotyl elongation in the light

Jian Li, William Terzaghi, Yanyan Gong, Congran Li, Jun-Jie Ling, Yangyang Fan, Nanxun Qin, Xinqi Gong (), Danmeng Zhu () and Xing Wang Deng ()
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Jian Li: Peking University
William Terzaghi: Wilkes University
Yanyan Gong: Peking University
Congran Li: Peking University
Jun-Jie Ling: Peking University
Yangyang Fan: Peking University
Nanxun Qin: Peking University
Xinqi Gong: Renmin University of China
Danmeng Zhu: Peking University
Xing Wang Deng: Peking University

Nature Communications, 2020, vol. 11, issue 1, 1-11

Abstract: Abstract ELONGATED HYPOCOTYL 5 (HY5), a basic domain/leucine zipper (bZIP) transcription factor, acts as a master regulator of transcription to promote photomorphogenesis. At present, it’s unclear whether HY5 uses additional mechanisms to inhibit hypocotyl elongation. Here, we demonstrate that HY5 enhances the activity of GSK3-like kinase BRASSINOSTEROID-INSENSITIVE 2 (BIN2), a key repressor of brassinosteroid signaling, to repress hypocotyl elongation. We show that HY5 physically interacts with and genetically acts through BIN2 to inhibit hypocotyl elongation. The interaction of HY5 with BIN2 enhances its kinase activity possibly by the promotion of BIN2 Tyr200 autophosphorylation, and subsequently represses the accumulation of the transcription factor BRASSINAZOLE-RESISTANT 1 (BZR1). Leu137 of HY5 is found to be important for the HY5-BIN2 interaction and HY5-mediated regulation of BIN2 activity, without affecting the transcriptional activity of HY5. HY5 levels increase with light intensity, which gradually enhances BIN2 activity. Thus, our work reveals an additional way in which HY5 promotes photomorphogenesis, and provides an insight into the regulation of GSK3 activity.

Date: 2020
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DOI: 10.1038/s41467-020-15394-7

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