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

Plant cell reports ·Vol. 4 ·No. 4 ·1985-08-00 ·Pages 199-201

Teulieres C, Alibert G, Ranjeva R

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.

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Teulieres C

Laboratoire Associé au C.N.R.S., Centre de Physiologie Végétale de l'Université Paul Sabatier, 118 Route de Narbonne, F-31062, Toulouse Cedex, France.

Alibert G

Ranjeva R

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Article Info

Journal

Plant cell reports

Abbr.

Plant Cell Rep

ISSN

0721-7714

DOI

10.1007/BF00269288

Published

1985-08-00

Pages

199-201

Language

English

Region

Germany

NLM ID

9880970

External Links

PubMed source DOI: 10.1007/BF00269288 View journal details

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

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