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Updated: Aug 16, 2026

Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis
Published on: June 25, 2020
Noncompetitive inhibition of plant protein Ser/Thr phosphatase PP7 by phosphate
1Research School of Biological and Molecular Sciences, Oxford Brookes University, Oxford, Headington, OX3 0BP, United Kingdom.
Abstract:
Changes in the cytoplasmic inorganic phosphate (P(i)) concentrations are an important cue for the plant cells to regulate their metabolism and phosphate homeostasis. However, phosphate sensors/receptors involved in this regulation are largely unknown. P(i) is a common nonspecific competitive inhibitor of phosphatases, usually in millimolar range. Here we report a procedure to refold recombinant Arabidopsis thaliana protein Ser/Thr phosphatase PP7 and demonstrate that PP7 is inhibited by submillimolar P(i) concentrations (IC(50) = 0.66 +/- 0.14 mM) via a mainly noncompetitive mechanism. The results indicate that PP7 may possess a specific P(i)-binding site responsible for its allosteric regulation, and suggest a possible phosphate sensor function for this protein phosphatase.
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