Please use this identifier to cite or link to this item: http://www.repositorio.ufop.br/handle/123456789/7427
Title: Possible involvement of a phosphatidylinositol-type signaling pathway in glucose-induced activation of plasma membrane ATPase and cellular proton in the yeast Sacchamyces cerevisiae.
Authors: Brandão, Rogélio Lopes
Rocha, Neuza Maria de Magalhaes
Alijo, Rafael
Ramos, José
Thevelein, Johan Maria
Keywords: Signal transduction
Protein kinase C
Neomycin
Medium acidification
Issue Date: 1994
Citation: 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.
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.
URI: http://www.repositorio.ufop.br/handle/123456789/7427
metadata.dc.identifier.uri2: http://www.sciencedirect.com/science/article/pii/0167488994900809?np=y
metadata.dc.identifier.doi: https://doi.org/10.1016/0167-4889(94)90080-9
ISSN: 1097-0061
Appears in Collections:DEFAR - Artigos publicados em periódicos

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