Coccetti, PaolaTisi, RenataMartegani, EnzoTeixeira, Leonardo SouzaBrandão, Rogélio LopesCastro, Ieso de MirandaThevelein, Johan Maria2012-07-192012-07-191998COCCETTI, P. et al. The PLC1 encoded phospholipase C in the yeast Saccharomyces cerevisiae is essential for glucose-induced phosphatidylinositol turnover and activation of plasma membrane H -ATPase. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, v. 1405, n. 1-3, p. 147-154, out. 1998. Disponível em: <https://www.sciencedirect.com/science/article/pii/S0167488998000998>. Acesso em: 19 jul. 2012.01674889http://www.repositorio.ufop.br/handle/123456789/1179Addition of glucose to glucose-deprived cells of the yeast Saccharomyces cerevisiae triggers rapid turnover of phosphatidylinositol, phosphatidylinositol-phosphate and phosphatidylinositol 4,5-bisphosphate. Glucose stimulation of PI turnover was measured both as an increase in the specific ratio of 32P-labeling and as an increase in the level of diacylglycerol after addition of glucose. Glucose also causes rapid activation of plasma membrane H.-ATPase. We show that in a mutant lacking the PLC1 encoded phospholipase C, both processes were strongly reduced. Compound 48/80, a known inhibitor of mammalian phospholipase C, inhibits both processes. However, activation of the plasma membrane H.- ATPase is only inhibited by concentrations of compound 48/80 that strongly inhibit phospholipid turnover. Growth was inhibited by even lower concentrations. Our data suggest that in yeast cells, glucose triggers through activation of the PLC1 gene product a signaling pathway initiated by phosphatidylinositol turnover and involved in activation of the plasma membrane H.-ATPase.en-USCompound 48/80Saccharomyces cerevisiaeGlucose inductionSignal transductionMedium acidificationArtigo publicado em periodicoO periódico Biochimica et Biophysica Acta. Molecular Cell Research concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 3266591238516.