A mutually assured destruction mechanism attenuates light signaling in Arabidopsis.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 24904166.
- Also identified by DOI 10.1126/science.1250778 and PMC identifier 4414656.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
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.
Medical subject headings
- Arabidopsis
- Arabidopsis Proteins
- Basic Helix-Loop-Helix Proteins
- Cullin Proteins
- Light Signal Transduction
- Phytochrome B
- Ubiquitination