Zhao Yan, Shi Hui, Pan Ying, Lyu Mohan, Yang Zhixuan, Kou Xiaoxia, Deng Xing Wang, Zhong Shangwei
State Key Laboratory of Protein and Plant Gene Research, School of Life Sciences, Peking University, Beijing 100871, China.
College of Life Sciences, Capital Normal University, and Beijing Key Laboratory of Plant Gene Resources and Biotechnology for Carbon Reduction and Environmental Improvement, Beijing 100048, China.
Cell. 2023 Mar 16;186(6):1230-1243.e14. doi: 10.1016/j.cell.2023.02.011.
Although Ca has long been recognized as an obligatory intermediate in visual transduction, its role in plant phototransduction remains elusive. Here, we report a Ca signaling that controls photoreceptor phyB nuclear translocation in etiolated seedlings during dark-to-light transition. Red light stimulates acute cytosolic Ca increases via phyB, which are sensed by Ca-binding protein kinases, CPK6 and CPK12 (CPK6/12). Upon Ca activation, CPK6/12 in turn directly interact with and phosphorylate photo-activated phyB at Ser80/Ser106 to initiate phyB nuclear import. Non-phosphorylatable mutation, phyB, abolishes nuclear translocation and fails to complement phyB mutant, which is fully restored by combining phyB with a nuclear localization signal. We further show that CPK6/12 function specifically in the early phyB-mediated cotyledon expansion, while Ser80/Ser106 phosphorylation generally governs phyB nuclear translocation. Our results uncover a biochemical regulatory loop centered in phyB phototransduction and provide a paradigm for linking ubiquitous Ca increases to specific responses in sensory stimulus processing.
尽管长期以来人们一直认为钙是视觉转导过程中的一种必需中间体,但其在植物光转导中的作用仍不清楚。在此,我们报道了一种钙信号传导,它在黄化幼苗从黑暗到光照的转变过程中控制光受体phyB的核转运。红光通过phyB刺激细胞质钙的急剧增加,钙结合蛋白激酶CPK6和CPK12(CPK6/12)能感知这种增加。钙激活后,CPK6/12反过来直接与光激活的phyB在Ser80/Ser106位点相互作用并使其磷酸化,从而启动phyB的核输入。不可磷酸化的phyB突变体消除了核转运,并且无法互补phyB突变体,而将phyB与核定位信号结合则可使其完全恢复。我们进一步表明,CPK6/12在早期phyB介导的子叶扩展中具有特异性功能,而Ser80/Ser106位点的磷酸化通常控制phyB的核转运。我们的结果揭示了一个以phyB光转导为中心的生化调节环,并为将普遍存在的钙增加与感觉刺激处理中的特定反应联系起来提供了一个范例。