自然杂志 ›› 2019, Vol. 41 ›› Issue (3): 188-196.doi: 10.3969/j.issn.0253-9608.2019.03.005

• 专题综述 • 上一篇    下一篇

植物远红光受体——光敏色素A的研究进展

周杨杨,李继刚   

  1. State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing
    100193, China
  • 收稿日期:2019-01-18 出版日期:2019-06-25 发布日期:2019-06-27
  • 作者简介:李继刚,通信作者,“青年千人计划”入选者,研究方向:植物光形态建成与逆境应答。E-mail: jigangli@cau.edu.cn

Research progress in phytochrome A signaling

ZHOU Yangyang, LI Jigang   


  • Received:2019-01-18 Online:2019-06-25 Published:2019-06-27

摘要: 光敏色素是植物中感受红光和远红光的光受体,而光敏色素A(phyA)是植物中唯一感受并响应远红光信号的光受体。phyA以Pr形式在细胞质中合成,接受光照后被激活,转换为具有生物活性的Pfr形式。Pfr形式的phyA与穿梭蛋白FHY1/FHL结合并被转运进入细胞核,在细胞核中与FHY1/FHL分离;FHY1/FHL出核,进行下一个转运phyA进入细胞核的循环。近年发展的phyA数学模型指出,phyA受体Pr与Pfr形式间的转换,以及特异性依赖FHY1/FHL转运进入细胞核,决定其成为植物远红光的光受体。在细胞核中,激活形式的phyA与COP1和SPA蛋白直接相互作用,抑制其形成有功能的E3泛素连接酶复合体;从而使转录因子HY5等蛋白能够积累,促进光形态建成的发生。Pfr形式的phyA也可以与转录因子PIFs相互作用,并介导PIFs的快速磷酸化和降解,从而解除PIFs对光形态建成的抑制作用。FHY3和FAR1是转座酶衍生的一类转录因子,能够在远红光下直接激活FHY1/FHL的基因表达;而HY5能够负反馈调控FHY3/FAR1对于FHY1/FHL的转录激活作用,从而维持远红光信号的动态平衡。Pfr形式的phyA在细胞核内能够被磷酸化,磷酸化的phyA是COP1/SPA的E3泛素连接酶复合体优先降解的底物;而最新的研究表明,磷酸化的phyA可能是一种活性更强的形式,在诱导植物远红光信号响应中扮演重要的角色。

关键词: 光敏色素A, 远红光受体, 磷酸化, 信号转导

Abstract: Phytochromes are red (R) and far-red (FR) light photoreceptors in plants, and phytochrome A (phyA) is the only plant photoreceptor that perceives FR light and then mediates various responses to this signal. The phyA is synthesized in the cytosol in the inactive Pr form; upon light illumination, phyA is converted to the biologically active Pfr form, and interact directly with the shuttle proteins FHY1 and FHL. The phyA is then imported into the nucleus by FHY1/FHL, while the phyA-FHY1/FHL complexes dissociate in the nucleus and FHY1/FHL return to the cytosol for the next phyA transportation cycle. A recently developed mathematical model suggested that the photoconversion of phyA between Pr and Pfr forms and FHY1/FHL-dependent nuclear trafficking cycles determine phyA’s response profile to far-red light. In the nucleus, phyA interacts with COP1 and SPA proteins directly, leading to the disruption and inactivation of the COP1/SPA complexes and the accumulation of HY5, a bZIP family transcription factor acting as a key positive regulator of photomorphogenesis. The Pfr form of phyA also interacts directly with the PIF proteins, a group of bHLH family transcription factors acting as repressors of photomorphogenesis, and induces rapid phosphorylation and degradation of PIFs. FHY3 and FAR1 are transposase-derived transcription factors which directly activate the transcription of FHY1 and FHL under farred light; however, HY5 negatively regulates FHY3/FAR1-activated FHY1/FHL expression, thus playing a role in fine-tuning phyA signaling homeostasis. The Pfr form of phyA could be phosphorylated in the nucleus, and the phosphorylated phyA form may serve as the preferred substrate for the COP1/SPA complex-mediated degradation. It was recently shown that the phosphorylated phyA form may represent a moreactive form of phyA, thus playing an essential role in inducing the FR light response.