Possible involvement of a phosphatidylinositol-type signaling pathway in glucose-induced activation of plasma membrane ATPase and cellular proton in the yeast Sacchamyces cerevisiae.
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1994
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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.
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Signal transduction, Protein kinase C, Neomycin, Medium acidification
Citação
BRANDÃO, R. L. et al. Possible involvement of a phosphatidylinositol-type signaling pathway in glucose-induced activation of plasma membrane ATPase and cellular proton in the yeast Sacchamyces cerevisiae. Biochimica et Biophysica Acta. Molecular Cell Research, v. 1223, p. 117-124, 1994. Disponível em: <http://www.sciencedirect.com/science/article/pii/0167488994900809?np=y>. Acesso em: 10 jan. 2017.