alexa Reversible phosphorylation of tonoplast proteins involves tonoplast-bound calcium-calmodulin-dependent protein kinase(s) and protein phosphatase(s).
Environmental Sciences

Environmental Sciences

Journal of Biodiversity, Bioprospecting and Development

Author(s): Teulieres C, Alibert G, Ranjeva R

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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. This article was published in Plant Cell Rep and referenced in Journal of Biodiversity, Bioprospecting and Development

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