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Title: POSSIBLE INVOLVEMENT OF A PHOSPHATIDYLINOSITOL-TYPE SIGNALING PATHWAY IN GLUCOSE-INDUCED ACTIVATION OF PLASMA-MEMBRANE H+-ATPASE AND CELLULAR PROTON EXTRUSION IN THE YEAST SACCHAROMYCES-CEREVISIAE
Authors: BRANDAO, RL ×
DEMAGALHAESROCHA, NM
ALIJO, R
RAMOS, J
Thevelein, Johan #
Issue Date: 1994
Publisher: ELSEVIER SCIENCE BV
Series Title: Biochimica et Biophysica Acta. Molecular Cell Research vol:1223 issue:1 pages:117-124
Conference: date:KATHOLIEKE UNIV LEUVEN,MOLEC CELBIOL LAB,B-3001 LOUVAIN,BELGIUM; UNIV CORDOBA,ESCUELA SUPER INGENIEROS AGRON,DEPT MICROBIOL,E-14071 CORDOBA,SPAIN; UNIV FED OURO PRETO,ESCOLA FARM,BIOQUIM & FISIOL MICRORGANISMOS LAB,BR-3540000 OURO PRETO,MG,BRAZIL
Abstract: Addition of glucose to cells of the yeast Saccharomyces cerevisiae causes rapid activation of plasma membrane H+-ATPase and a stimulation of cellular H+ extrusion. We show that addition of diacylglycerol and other activators of protein kinase C to intact cells also activates the H+-ATPase and causes at the same time a stimulation of H+ extrusion from the cells. Both effects are reversed by addition of staurosporine, a protein kinase C inhibitor. Addition of staurosporine or calmidazolium, an inhibitor of Ca2+/calmodulin-dependent protein kinases, separately, causes a partial inhibition of glucose-induced H+-ATPase activation and stimulation of cellular H+ extrusion; together they cause a more potent inhibition. Addition of neomycin, which complexes with phosphatidylinositol 4,5-bisphosphate, or addition of compound 48/80, a phospholipase C inhibitor, also causes near complete inhibition. Diacylglycerol and other protein kinase C activators had no effect on the activity of the K+-uptake system and the activity of trehalase and glucose-induced activation of the K+-uptake system and trehalase was not inhibited by neomycin, supporting the specificity of the effects observed on the H+-ATPase. The results support a model in which glucose-induced activation of H+-ATPase is mediated by a phosphatidylinositol-type signaling pathway triggering phosphorylation of the enzyme both by protein kinase C and one or more Ca2+/calmodulin-dependent protein kinases.
ISSN: 0167-4889
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Microbiology and Biotechnology Section - miscellaneous
× corresponding author
# (joint) last author

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