Phosphorus is an essential building block for nucleic acids and membranes, forms an important energy currency of the cell and can act as a signaling molecule. Soil-living organisms take up phosphorus in the form of inorganic phosphate. How cells ‘measure’ phosphate concentrations to maintain sufficient phosphate levels in their cells and tissues is poorly understood. The group of Michael Hothorn has now elucidated that phosphate homeostasis in plants is regulated by an inositol pyrophosphate signaling molecule, which is generated by a bifunctional kinase/phosphatase enzyme in response to changing ATP and phosphate levels. The signaling molecule then binds to a cellular receptor, which in turn inactivates a transcription factor regulating phosphate starvation responses. Thus, a signaling molecule relays the nutrient status of the plant to a signaling cascade, allowing for nutrient uptake, storage and redistribution. The groups of Dorothea Fiedler (Leibniz Institute for Molecular Pharmacology, Berlin, Germany), Alisdair Fernie (Max Planck Institute for Molecular Plant Physiology, Golm, Germany) and Gabriel Schaaf (University of Bonn, Germany) contributed to this study that was published in eLife on August 22.
Plants perceive light as an important environmental cue. They sense the UV-B part of the solar spectrum through the UVR8 photoreceptor that activates acclimatory responses associated with protection against this potentially damaging radiation. UVR8 enhances the stability of the HY5 transcription factor by inhibiting the activity of COP1, an E3 ubiquitin ligase that targets HY5 for degradation. The teams of Michael Hothorn and of Roman Ulm have now discovered that the UVR8 mechanism of action involves direct competition between active UVR8 and HY5 through interaction domain mimicry and overlapping binding sites on COP1. This mechanism was found to be conserved in other photoreceptor signaling pathways. The study was published in The EMBO Journal on July 15, 2019.