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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MetadadosDescriçãoIdioma
Autor(es): dc.creatorBrandão, Rogélio Lopes-
Autor(es): dc.creatorRocha, Neuza Maria de Magalhaes-
Autor(es): dc.creatorAlijo, Rafael-
Autor(es): dc.creatorRamos, José-
Autor(es): dc.creatorThevelein, Johan Maria-
Data de aceite: dc.date.accessioned2025-08-21T15:15:24Z-
Data de disponibilização: dc.date.available2025-08-21T15:15:24Z-
Data de envio: dc.date.issued2017-03-22-
Data de envio: dc.date.issued2017-03-22-
Data de envio: dc.date.issued1994-
Fonte completa do material: dc.identifierhttp://www.repositorio.ufop.br/handle/123456789/7427-
Fonte completa do material: dc.identifierhttp://www.sciencedirect.com/science/article/pii/0167488994900809?np=y-
Fonte completa do material: dc.identifierhttps://doi.org/10.1016/0167-4889(94)90080-9-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1008132-
Descrição: dc.descriptionAddition 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.-
Formato: dc.formatapplication/pdf-
Idioma: dc.languageen-
Direitos: dc.rightsrestrito-
Palavras-chave: dc.subjectSignal transduction-
Palavras-chave: dc.subjectProtein kinase C-
Palavras-chave: dc.subjectNeomycin-
Palavras-chave: dc.subjectMedium acidification-
Título: dc.titlePossible 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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