Please use this identifier to cite or link to this item: http://www.repositorio.ufop.br/handle/123456789/1179
Title: The PLC1 encoded phospholipase C in the yeast Saccharomyces cerevisiae is essential for glucose-induced phosphatidylinositol turnover and activation of plasma membrane H -ATPase.
Authors: Coccetti, Paola
Tisi, Renata
Martegani, Enzo
Teixeira, Leonardo Souza
Brandão, Rogélio Lopes
Castro, Ieso de Miranda
Thevelein, Johan Maria
Keywords: Compound 48/80
Saccharomyces cerevisiae
Glucose induction
Signal transduction
Medium acidification
Issue Date: 1998
Citation: COCCETTI, 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.
Abstract: Addition 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.
URI: http://www.repositorio.ufop.br/handle/123456789/1179
ISSN: 01674889
metadata.dc.rights.license: O periódico Biochimica et Biophysica Acta. Molecular Cell Research concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 3266591238516.
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