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Updated: May 5, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Reversible phosphorylation of tonoplast proteins involves tonoplast-bound calcium-calmodulin-dependent protein
C Teulieres1, G Alibert, R Ranjeva
1Laboratoire Associé au C.N.R.S., Centre de Physiologie Végétale de l'Université Paul Sabatier, 118 Route de Narbonne, F-31062, Toulouse Cedex, France.
Abstract:
In highly purified tonoplast fractions from Acer pseudoplatanus cells, the in vitro reversible phosphorylation of proteins affected only a restricted set of polypeptides. The phosphorylation process has been shown to be dramatically stimulated by calcium via the mediation of calmodulin as the transducer. The protein kinase(s) was totally inhibited by micromolar concentrations of a calmodulin antagonist. Tonoplast appears to be potentially a good experimental system for the evaluation of the effects of protein phosphorylation on membrane properties in plants.
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