Plant and Cell Physiology Advance Access published online on April 13, 2006
Plant and Cell Physiology, doi:10.1093/pcp/pcj046
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1 Department of Biology, University of Rome "Tor Vergata", via della Ricerca Scientifica, 00133 Rome, Italy
* To whom correspondence should be addressed. The H+-ATPase, the key enzyme for the energisation of ion and nutrient transport across the plasma membrane, is activated by phosphorylation-dependent 14-3-3 binding. Since the involvement of 14-3-3 proteins in sugar sensing regulated processes has recently emerged, in this paper we address the question as to whether sugars sensing plays a role in the regulation of the H+-ATPase. The data reported here show that sugar depletion inhibits the association of 14-3-3 proteins to the H+-ATPase by hampering phosphorylation of the 14-3-3 binding site of the enzyme. By using non-metabolizable disaccharides it is proven that H+-ATPase regulation by 14-3-3 proteins can involve a specific sugar perception and transduction mechanism.
Received December 15, 2005
Accepted April 2, 2006
Regular Paper
The Maize Root Plasma Membrane H+-ATPase Is Regulated by a Sugar-Induced Transduction Pathway
Lorenzo Camoni 1,
Mauro Marra 1,
Alessandra Garufi 1,
Sabina Visconti 1,
and
Patrizia Aducci 1 *
Patrizia Aducci, E-mail: Aducci{at}uniroma2.it
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