Activation of plasma membrana H+-ATPase of Saccharomyces cerevisiae by glucose is mediated by dissociation of H+-ATPase/acetylated tubulin complex.

CAMPETELLI, A.N.; PREVITALI, G; CARLOS ANGEL ARCE; BARRA, H.S.; CASALE, C.H.

WILEY-BLACKWELL PUBLISHING, INC

Año: 2005 vol. 272 p. 5742 - 5742

p class="MsoNormal" style="MARGIN: 0cm 0cm 0pt; LINE-HEIGHT: 150%; tab-stops: 21.6pt">In the yeast Saccharomyces cerevisiae, plasma membrane H+-ATPase is activated by D-glucose. We found that in the absence of glucose, this enzyme forms a complex with acetylated tubulin. Acetylated tubulin usually displays hydrophilic properties, but behaves as a hydrophobic compound when complexed with H+-ATPase, and therefore partitions into a detergent phase. When cells were treated with glucose, the H+-ATPase/tubulin complex was disrupted, with two consequences: (i) the amount of acetylated tubulin in plasma membrane decreased as a function of glucose concentration; (ii) H+-ATPase activity increased as a function of glucose concentration, as measured by both ATP-hydrolyzing capacity and H+-pumping activity. Addition of 2-deoxy-D-gluc