Journal Article

Role of the 14-3-3 C-Terminal Region in the Interaction with the Plasma Membrane H<sup>+</sup>-ATPase

Sabina Visconti, Lorenzo Camoni, Mauro Marra and Patrizia Aducci

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 49, issue 12, pages 1887-1897
Published in print December 2008 | ISSN: 0032-0781
Published online December 2008 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcn172
Role of the 14-3-3 C-Terminal Region in the Interaction with the Plasma Membrane H+-ATPase

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  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry

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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

Journal Article.  6216 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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