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Plant and Cell Physiology Advance Access originally published online on November 10, 2008
Plant and Cell Physiology 2008 49(12):1887-1897; 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 email: journals.permissions@oxfordjournals.org

Role of the 14-3-3 C-Terminal Region in the 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

*Corresponding author: E-mail, aducci{at}uniroma2.it; Fax, +39-062023500.


  Abstract

The 14-3-3 proteins 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 is still unclear. The 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. Here 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 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 H+-ATPase and to stimulate the enzyme activity. The implications of these findings for a integrated model of 14-3-3 interaction with H+-ATPase are discussed.

Keywords: 14-3-3 proteins - Fusicoccin - H+-ATPase - Plasma membrane - Protein–protein interaction - Spermine

Abbreviations: AHA1, Arabidopsis H+-ATPase isoform 1; BSA, bovine serum albumin; ER, endoplasmic reticulum; FC, fusicoccin; GST, glutathione S-transferase; MHA2, Maize H+-ATPase isoform 2; PBS, phosphate-buffered saline

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