A mutually assured destruction mechanism attenuates light signaling in Arabidopsis.

A mutually assured destruction mechanism attenuates light signaling in Arabidopsis.
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DOI:
10.1126/science.1250778
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发表时间:
2014-06-06
期刊:
Science (New York, N.Y.)
影响因子:
--
通讯作者:
Quail PH
Quail PH
中科院分区:
其他
文献类型:
--
作者:
Ni W;Xu SL;Tepperman JM;Stanley DJ;Maltby DA;Gross JD;Burlingame AL;Wang ZY;Quail PH

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在光诱导核易位后,光敏色素光感受器与bHLH转录因子(如光敏色素相互作用因子3 (PIF3))相互作用并诱导其快速磷酸化和降解,以调节基因表达。同时,这种相互作用触发光敏色素B (phyB)水平的反馈降低。光诱导的PIF3磷酸化对于这两种蛋白的降解是必要的。我们报道这种PIF3磷酸化诱导并且是PIF3- phyb复合物募集LRB (Light-Response brick -a- brack /Tramtrack/Broad (BTB)) E3泛素连接酶的必要条件。募集的LRBs在体内同时促进PIF3和phyB的多泛素化和降解。这些数据揭示了一个相互关联的信号传递和衰减机制,涉及受体及其直接信号伙伴的相互保证破坏。
Following light-induced nuclear translocation, phytochrome photoreceptors interact with and induce rapid phosphorylation and degradation of bHLH transcription factors, such as PHYTOCHROME-INTERACTING FACTOR 3 (PIF3), to regulate gene expression. Concomitantly this interaction triggers feedback reduction of phytochrome B (phyB) levels. Light-induced phosphorylation of PIF3 is necessary for the degradation of both proteins. We report that this PIF3 phosphorylation induces, and is necessary for, recruitment of LRB (Light-Response Bric-a-Brack/Tramtrack/Broad (BTB)) E3 ubiquitin ligases to the PIF3-phyB complex. The recruited LRBs promote concurrent polyubiqutination and degradation of both PIF3 and phyB in vivo. These data reveal a linked signal-transmission and attenuation mechanism involving mutually assured destruction of the receptor and its immediate signaling partner.
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