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Activation of the plasma membrane H + -ATPase of the yeast  Saccharomyces cerevisiae  by glucose is a complex process that has not yet been completely elucidated. This study aimed to shed light on the role of lipids and the lateral mobility of the enzyme complex during its activation by glucose. The significance of H + -ATPase oligomerization for the activation of H + -ATPase by glucose was shown using the strains  lcb1-100  and  erg6 , with the disturbed synthesis of sphyngolipid and ergosterol, respectively. Experiments with GFP-fused H + -ATPase showed a decrease in fluorescence anisotropy during the course of glucose activation, suggesting structural reorganization of the molecular domains. An immunogold assay showed that the incubation with glucose results in the spatial redistribution of ATPase complexes in the plasma membrane. The data suggest that (1) to be activated by glucose, H + -ATPase is supposed to be in an oligomeric state, and (2) glucose activation is accompanied by the spatial movements of H + -ATPase clusters in the PM.

Activation of H+-ATPase of the Plasma Membrane of Saccharomyces cerevisiae by Glucose: The Role of Sphingolipid and Lateral Enzyme Mobility