Tyrosine phosphorylation regulates the activity of phytochrome photoreceptors.

Tyrosine phosphorylation regulates the activity of phytochrome photoreceptors.
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DOI:
10.1016/j.celrep.2013.05.006
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发表时间:
2013-06-27
期刊:
影响因子:
8.8
通讯作者:
Chory J
Chory J
中科院分区:
生物学1区
文献类型:
--
作者:
Nito K;Wong CC;Yates JR 3rd;Chory J

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光敏色素是在植物光形态建成中起作用的红光/远红光受体。光敏色素在红光下的光异构化导致其易位到细胞核,在那里它调节基因表达。我们研究了光敏色素是否被磷酸化,在响应光,并报告phyB的N-末端包含一个区域与一些磷酸丝氨酸,苏氨酸和酪氨酸。酪氨酸104(Y104)的光依赖性磷酸化似乎在phyB的活性中起着决定性作用,因为磷酸化模拟突变体phyBY 104 E不能补充任何phyB相关的表型,在与其信号伴侣PIF 3的结合中有缺陷,并且不能形成稳定的核体,即使它在体外保持正常的光化学。相反,稳定表达不可磷酸化突变体phyBY 104 F的植物对光过敏。由于对光环境变化的适当反应对植物生存至关重要,我们的研究将酪氨酸磷酸化带到了光信号机制的最前沿。
Phytochromes are red/far-red light receptors that function in photomorphogenesis of plants. Photoisomerization of phytochrome by red light leads to its translocation to the nucleus where it regulates gene expression. We examined whether phytochrome is phosphorylated in response to light, and report that phyB’s N-terminus contains a region with a number of phospho-serines, threonines and tyrosines. The light-dependent phosphorylation of tyrosine 104 (Y104) appears to play a negatve role in phyB’s activity because a phospho-mimic mutant, phyBY104E is unable to complement any phyB-related phenotype, is defective in binding to its signaling partner PIF3, and fails to form stable nuclear bodies, even though it retains normal photochemistry in vitro. In contrast, plants stably expressing a non-phosphorylatable mutant phyBY104F are hypersensitive to light. Because the proper response to changes in the light environment is crucial to plant survival, our study brings tyrosine phosphorylation to the forefront of light signaling mechanisms.
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