Ni Weimin, Xu Shou-Ling, Tepperman James M, Stanley David J, Maltby Dave A, Gross John D, Burlingame Alma L, Wang Zhi-Yong, Quail Peter H
Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720 and U.S. Department of Agriculture/Agriculture Research Service, Plant Gene Expression Center, Albany, CA 94710.
Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143.
Science. 2014 Jun 6;344(6188):1160-1164. doi: 10.1126/science.1250778.
After light-induced nuclear translocation, phytochrome photoreceptors interact with and induce rapid phosphorylation and degradation of basic helix-loop-helix 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.
光诱导核转位后,光敏色素光受体与碱性螺旋-环-螺旋转录因子相互作用并诱导其快速磷酸化和降解,如光敏色素相互作用因子3(PIF3),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。PIF3的光诱导磷酸化是两种蛋白质降解所必需的。我们报道,这种PIF3磷酸化诱导LRB[光响应Bric-a-Brack/Tramtrack/Broad(BTB)]E3泛素连接酶募集到PIF3-phyB复合物中,并且是其必需条件。募集到的LRB在体内促进PIF3和phyB同时多聚泛素化和降解。这些数据揭示了一种连锁的信号传递和衰减机制,涉及受体与其直接信号伴侣的相互确保破坏。