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Plant and Cell Physiology Advance Access published online on November 10, 2008
Plant and Cell Physiology, doi:10.1093/pcp/pcn172
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© The Author 2008. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

ROLE OF THE 14-3-3 C-TERMINAL REGION FOR INTERACTION WITH THE PLASMA MEMBRANE H+-ATPASE

Sabina Visconti, Lorenzo Camoni, Mauro Marra and Patrizia Aducci

Department of Biology, University of Rome "Tor Vergata", via della Ricerca Scientifica, 00133, Rome, Italy.

Address correspondence to: Prof. Patrizia Aducci, Department of Biology University of Rome "Tor Vergata", via della Ricerca Scientifica 00133 Rome, Italy. Tel. +39 0672594082; fax +39062023500. E-mail: aducci{at}uniroma2.it


  Abstract

The 14-3-3 are a family of proteins present in a number of isoforms in all eukaryotes and involved in the control of many cellular functions. Regulation of different activities is achieved by binding to phosphorylated targets through a conserved mechanism. Although in many systems isoform specificity has been demonstrated, the underlying molecular basis are still unclear. Sequences of 14-3-3 isoforms are highly conserved, divergence occurring at the N- and C-terminal regions. Recently it has been suggested that the C-terminal domain of 14-3-3 may regulate protein binding to the targets. In this paper we study the role of the C-terminal region of maize isoform GF14-6 in the interaction with the plant plasma membrane H+-ATPase. Results obtained demonstrate that removal of the last 22 amino acids residues of GF14-6 increases binding to the H+-ATPase and stimulation of its activity. C-terminal deletion, moreover, reduces 14-3-3 sensitivity to cations. We also show that a peptide reproducing the GF14-6 C terminus is able to bind to the C-terminal domain of the H+-ATPase and to stimulate the enzyme activity. Implications of these findings for a integrated model of 14-3-3 interaction with the H+-ATPase are discussed.

Keywords: 14-3-3 proteins - fusicoccin - H+-ATPase - plasma membrane - protein-protein interaction - spermine

(Received October 7, 2008; Accepted November 5, 2008)
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