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Plant Biol (Stuttg) 2004; 6(4): 422-431
DOI: 10.1055/s-2004-820933
Original Paper

Georg Thieme Verlag Stuttgart KG · New York

Tyrosine Phosphorylation Inhibits the Interaction of 14-3-3 Proteins with the Plant Plasma Membrane H+-ATPase

S. Giacometti1 , L. Camoni2 , C. Albumi1 , S. Visconti2 , M. I. De Michelis1 , P. Aducci2
  • 1Dipartimento di Biologia „L. Gorini“, Università di Milano, CNR Istituto di Biofisica - Sezione di Milano, via G. Celoria 26, 20133 Milano, Italy
  • 2Dipartimento di Biologia, Università di Roma „Tor Vergata“, Roma, Italy
Further Information

Publication History

Publication Date:
12 July 2004 (online)

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Abstract

Interaction of 14-3-3 proteins with their targets depends not only on the phosphorylation status of the target but also on that of 14-3-3 ([Fu et al., 2000]). In this work we demonstrated that the maize 14-3-3 isoform GF14-6 is a substrate of the tyrosine kinase insulin growth factor receptor 1. By means of site-directed mutants of GF14-6, we identified Tyr-137 as the specific tyrosine residue phosphorylated by the insulin growth factor receptor 1. Phosphorylation of GF14-6 on Tyr-137 lowered its affinity for a peptide mimicking the 14-3-3 binding site of the plant plasma membrane H+-ATPase. Moreover, phosphorylation in planta of 14-3-3 tyrosine residues, resulting from incubation with the tyrosine phosphatase inhibitor, phenylarsine oxide, decreased their association to the H+-ATPase.

Key words

14-3-3 proteins - plasma membrane H+-ATPase - tyrosine phosphorylation - signal transduction

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P. Aducci

Dipartimento di Biologia
Università di Roma “Tor Vergata”

via della Ricerca Scientifica

00133 Roma

Italy

Email: aducci@uniroma2.it

Section Editor: G. Thiel