The maize root plasma membrane H(+)-ATPase is regulated by a sugar-induced transduction pathway.
H(+)-ATPase, the key enzyme for the energization 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, here we address the question as to whether sugar sensing plays a role in the regulation of H(+)-ATPase. The data reported here show that sugar depletion inhibits the association of 14-3-3 proteins with H(+)-ATPase by hampering phosphorylation of the 14-3-3 binding site of the enzyme. By using non-metabolizable disaccharides, we show that H(+)-ATPase regulation by 14-3-3 proteins can involve a specific sugar perception and transduction mechanism.
Camoni
Lorenzo
L
Department of Biology, University of Rome 'Tor Vergata', via della Ricerca Scientifica, 00133 Rome, Italy.
Marra
Mauro
M
Garufi
Alessandra
A
Visconti
Sabina
S
Aducci
Patrizia
P
D048948:14-3-3 Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry / Q000201:enzymology*; D004187:Disaccharides / Q000378:metabolism*; D010766:Phosphorylation; D018517:Plant Roots / Q000737:chemistry / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*; D014161:Transduction, Genetic; D003313:Zea mays / Q000737:chemistry / Q000201:enzymology*
D048948:14-3-3 Proteins; D004187:Disaccharides; D006180:Proton-Translocating ATPases