Camoni Lorenzo, Marra Mauro, Garufi Alessandra, Visconti Sabina, Aducci Patrizia
Department of Biology, University of Rome 'Tor Vergata', via della Ricerca Scientifica, 00133 Rome, Italy.
Plant Cell Physiol. 2006 Jun;47(6):743-7. doi: 10.1093/pcp/pcj046. Epub 2006 Apr 13.
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.
H(+)-ATP酶是使离子和营养物质跨质膜运输获得能量的关键酶,它通过磷酸化依赖性的14-3-3结合而被激活。由于最近发现14-3-3蛋白参与了糖感知调节的过程,因此我们在此探讨糖感知是否在H(+)-ATP酶的调节中发挥作用。本文报道的数据表明,糖缺乏通过阻碍该酶14-3-3结合位点的磷酸化,抑制了14-3-3蛋白与H(+)-ATP酶的结合。通过使用不可代谢的双糖,我们表明14-3-3蛋白对H(+)-ATP酶的调节可能涉及特定的糖感知和转导机制。