Calcium signaling and sugar-induced activation of plasma membrane H+-ATPase in Saccharomyces cerevisiae cells.
In this work, we show that glucose-induced activation of plasma membrane H+-ATPase from Saccharomyces cerevisiae is strongly dependent on calcium metabolism and that the glucose sensor Snf3p works in a parallel way with the G protein Gpa2p in the control of the pathway. The role of Snf3p is played b...
| Authors: | , , , , , , , |
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| Format: | article |
| Status: | Published version |
| Publication Date: | 2006 |
| Country: | Brasil |
| Institution: | Universidade Federal de Ouro Preto (UFOP) |
| Repository: | Repositório Institucional da UFOP |
| Language: | English |
| OAI Identifier: | oai:repositorio.ufop.br:123456789/1167 |
| Online Access: | http://www.repositorio.ufop.br/handle/123456789/1167 |
| Access Level: | Open access |
| Keyword: | Calcium signaling Sugar-induced activation Plasma membrane ATPase |
| Summary: | In this work, we show that glucose-induced activation of plasma membrane H+-ATPase from Saccharomyces cerevisiae is strongly dependent on calcium metabolism and that the glucose sensor Snf3p works in a parallel way with the G protein Gpa2p in the control of the pathway. The role of Snf3p is played by the Snf3p C-terminal tail, since in a strain with the deletion of the SNF3 gene, but also expressing a chimera protein formed by Hxt1p (a glucose transporter) and the Snf3p C-terminal tail, a normal glucose-activation process can be observed. We present evidences indicating that Snf3p would be the sensor for the internal signal (phosphorylated sugars) of this pathway that would connect calcium signaling and activation of the plasma membrane ATPase. We also show that Snf3p could be involved in the control of Pmc1p activity that would regulate the calcium availability in the cytosol. |
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