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Hye Sup Yun Young Hee Bae Yun Ji Lee Soo Chul Chang Seong-Ki Kim Jianming Li Kyoung Hee Nam 《Molecules and cells》2009,27(2):183-190
The plasma membrane-localized BRASSINOSTEROID-INSENSITIVE1 (BRI1) and BRI1-ASSOCIATED KINASE1 (BAK1) are a well-known receptor
pair involved in brassinosteroids (BR) signaling in Arabidposis. The formation of a receptor complex in response to BRs and
the subsequent activation of cytoplasmic domain kinase activity share mechanistic characteristics with animal receptor kinases.
Here, we demonstrate that BRI1 and BAK1 are BR-dependently phosphorylated, and that phosphorylated forms of the two proteins
persist for different lengths of time. Mutations of either protein abolished phosphorylation of the counterpart protein, implying
transphosphorylation of the receptor kinases. To investigate the specific amino acids critical for formation of the receptor
complex and activation of BAK1 kinase activity, we expressed several versions of BAK1 in yeast and plants. L32E and L46E substitutions
resulted in a loss of binding of BAK1 to BRI1, and threonine T455 was essential for the kinase activity of BAK1 in yeast.
Transgenic bri1 mutant plants overexpressing BAK1(L46E) displayed reduced apical dominance and seed development. In addition, transgenic
wild type plants overexpressing BAK1(T455A) lost the phosphorylation activity normally exhibited in response to BL, leading
to semi-dwarfism. These results suggest that BAK1 is a critical component regulating the duration of BR efficacy, even though
it cannot directly bind BRs in plants. 相似文献
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Jie Wang Jianjun Jiang Jue Wang Lei Chen Shi-Long Fan Jia-Wei Wu Xuelu Wang Zhi-Xin Wang 《Cell research》2014,24(11):1328-1341
Brassinosteroids (BRs) are essential steroid hormones that have crucial roles in plant growth and development. BRs are perceived by the cell-surface receptor-like kinase brassinosteroid insensitive 1 (BRI1). In the absence of BRs, the cytosolic kinase domain (KD) of BRI1 is inhibited by its auto-inhibitory carboxyl terminus, as well as by interacting with an inhibitor protein, BRI1 kinase inhibitor 1 (BKI1). How BR binding to the extracellular domain of BRI1 leads to activation of the KD and dissociation of BKI1 into the cytosol remains unclear. Here we report the crystal structure of BRI1 KD in complex with the interacting peptide derived from BKI1. We also provide biochemical evidence that BRI1-associated kinase 1 (BAK1) plays an essential role in initiating BR signaling. Steroid-dependent heterodimerization of BRI1 and BAK1 ectodomains brings their cytoplasmic KDs in the right orientation for competing with BKI1 and transphosphorylation. 相似文献
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