期刊
SCIENCE
卷 344, 期 6188, 页码 1160-1164出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1250778
关键词
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资金
- National Institutes of Health (NIH) [2R01 GM-047475]
- U.S. Department of Energy (DOE) [DEFG03-87ER13742]
- USDA ARS Current Research Information System [5335-21000-032-00D]
- NIH [5R01GM066258, 8P41GM103481, P50 GM082250]
- DOE [DEFG02-08ER15973]
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.
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