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dc.contributor.authorPereira, Michele B. P.-
dc.contributor.authorTisi, Renata-
dc.contributor.authorFietto, Luciano Gomes-
dc.contributor.authorCardoso, Anamaria de Souza-
dc.contributor.authorFrança, Mônica M.-
dc.contributor.authorCarvalho, Fernanda Machado de-
dc.contributor.authorTrópia, Maria José Magalhães-
dc.contributor.authorMartegani, Enzo-
dc.contributor.authorCastro, Ieso de Miranda-
dc.contributor.authorBrandão, Rogélio Lopes-
dc.identifier.citationPEREIRA, M. B. P. et al. Carbonyl cyanidem - chlorophenylhydrazone induced calcium signaling and activation of plasma membrane H1-ATPase in the yeast Saccharomyces cerevisiae. FEMS Yeast Research, v. 8, n.4, p.622-630, jun. 2008. Disponível em: <>. Acesso em: 18 jul. 2012.pt_BR
dc.description.abstractThe plasma membrane H1-ATPase from Saccharomyces cerevisiae is an enzyme that plays a very important role in the yeast physiology. The addition of protonophores, such as 2,4-dinitrophenol (DNP) and carbonyl cyanide m-chlorophenylhydrazone (CCCP), also triggers a clear in vivo activation of this enzyme. Here, we demonstrate that CCCP-induced activation of the plasma membrane H1-ATPase shares some similarities with the sugar-induced activation of the enzyme. Phospholipase C and protein kinase C activities are essential for this activation process while Gpa2p, a G protein involved in the glucose-induced activation of the ATPase, is not required. CCCP also induces a phospholipase Cdependent increase in intracellular calcium. Moreover, we show that the availability of extracellular calcium is required for CCCP stimulation of H1-ATPase, suggesting a possible connection between calcium signaling and activation of ATPase.pt_BR
dc.subjectDepolarizing compoundspt_BR
dc.subjectSaccharomyces cerevisiaept_BR
dc.titleCarbonyl cyanidem - chlorophenylhydrazone induced calcium signaling and activation of plasma membrane H1-ATPase in the yeast Saccharomyces cerevisiae.pt_BR
dc.typeArtigo publicado em periodicopt_BR
dc.rights.licenseO Periódico FEMS Yeast Research concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 500810576.-
Appears in Collections:DEFAR - Artigos publicados em periódicos

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