Control of plant phosphate homeostasis by inositol pyrophosphates and the SPX domain.
Jung JYDepartment of Plant Molecular Biology, University of Lausanne, Lausanne, Switzerland.
Ried MKStructural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, Geneva, Switzerland.
Hothorn MStructural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, Geneva, Switzerland. Electronic address: Michael.hothorn@unige.ch.
Poirier YDepartment of Plant Molecular Biology, University of Lausanne, Lausanne, Switzerland. Electronic address: yves.poirier@unil.ch.
English
Proteins containing a SPX domain are involved in phosphate (Pi) homeostasis, including Pi transport and adaptation to Pi deficiency. The SPX domain harbors a basic surface binding Pi at low affinity and inositol pyrophosphates (PP-InsPs) at high affinity. Genetic and biochemical studies revealed that PP-InsPs serve as ligands for the SPX domain. Residues in the PHO1 SPX domain involved in PP-InsPs binding are critical for its Pi export activity, and the interaction between SPX proteins and the PHR1 transcription factor, which results in PHR1 inactivation, is promoted by PP-InsPs. Changes in PP-InsPs levels in response to Pi deficiency may thus contribute to the adaptation of plants to stress via the modulation of the activity of SPX-containing proteins and their interactors. Modulating PP-InsP levels or the affinity/specificity of the SPX domain for PP-InsP could potentially be used to engineer crops to maintain high yield under reduced Pi fertilizer input.