| Literature DB >> 24904166 |
Weimin Ni1, Shou-Ling Xu2,3, James M Tepperman1, David J Stanley2, Dave A Maltby2, John D Gross2, Alma L Burlingame2, Zhi-Yong Wang3, Peter H Quail1.
Abstract
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.Entities:
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Year: 2014 PMID: 24904166 PMCID: PMC4414656 DOI: 10.1126/science.1250778
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728