Dual Role of BKI1 and 14-3-3 s in Brassinosteroid Signaling to Link Receptor with Transcription Factors

被引:139
作者
Wang, Haijiao [1 ,2 ]
Yang, Cangjin [1 ,2 ]
Zhang, Chi [1 ,2 ]
Wang, Niyan [1 ,2 ]
Lu, Dihong [3 ]
Wang, Jie [4 ]
Zhang, Shanshan [1 ,2 ]
Wang, Zhi-Xin [4 ]
Ma, Hong [1 ,2 ,3 ,5 ]
Wang, Xuelu [1 ,2 ]
机构
[1] Fudan Univ, State Key Lab Genet Engn, Sch Life Sci, Shanghai 200433, Peoples R China
[2] Fudan Univ, Inst Plant Biol, Sch Life Sci, Shanghai 200433, Peoples R China
[3] Penn State Univ, Dept Biol, Intercoll Grad Program Plant Biol, Huck Inst Life Sci, University Pk, PA 16802 USA
[4] Tsinghua Univ, Sch Life Sci, Beijing 100084, Peoples R China
[5] Fudan Univ, Ctr Evolutionary Biol, Inst Biomed Sci, Shanghai 200433, Peoples R China
基金
中国国家自然科学基金;
关键词
GENE-EXPRESSION; PROTEIN-KINASE; GROWTH; BRI1; PHOSPHORYLATION; TRANSDUCTION; BINDING; 14-3-3-PROTEINS; PERCEPTION; ACTIVATION;
D O I
10.1016/j.devcel.2011.08.018
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The plasma membrane-localized plant steroid hormone receptor, BRASSINOSTEROID INSENSITIVE 1 (BRI1), is quiescent in the absence of steroids, largely due to a negative regulator, BRI1 KINASE INHIBITOR 1 (BKI1). Here, we report that the steroid-induced, plasma membrane-dissociated and phosphorylated BKI1 also plays positive roles in BR signaling by interacting with a subset of 14-3-3 proteins. The cytosolic fraction of BKI1 carboxyl terminal region enhances BR signaling. Mutations of two serine residues in this region lead to reduced phosphorylation by the BRI1 kinase and constitutive plasma membrane localization. The 14-3-3 proteins can interact with the phosphorylated BKIl through a motif that contains the two phosphorylation sites to release inhibition of BRI1 by BKI1. Meanwhile, the cytosolic BKIl antagonizes the 14-3-3 s and enhances accumulation of BRI1 EMS SUPPRESSOR 1 (BES1)/BRASSINAZOLE RESISTANT 1 (BZR1) in the nucleus to regulate BR-responses.
引用
收藏
页码:825 / 834
页数:10
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