Journal
PLANT AND CELL PHYSIOLOGY
Volume 49, Issue 12, Pages 1887-1897Publisher
OXFORD UNIV PRESS
DOI: 10.1093/pcp/pcn172
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Funding
- Italian Ministry of Education, University and Research (MIUR) [PRIN 2005]
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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.
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