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First published online 11 July 2006
doi: 10.1242/jcs.03033
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Research Article |
1 Laboratório de Microbiologia, Centro de Estudos de Química Orgânica, Fitoquímica e Farmacologia da Universidade do Porto (CEQOFFUP), Faculdade de Farmácia, Universidade do Porto, Rua Aníbal Cunha 164, 4050-047 Porto, Portugal
2 Centro de Biologia, Universidade do Minho, Campus de Gualtar, 4710-057 Braga, Portugal
3 Laboratório de Farmacologia, Centro de Estudos de Química Orgânica, Fitoquímica e Farmacologia da Universidade do Porto (CEQOFFUP), Faculdade de Farmácia, Universidade do Porto, Rua Aníbal Cunha 164, 4050-047 Porto, Portugal
* Author for correspondence (e-mail: mcortereal{at}bio.uminho.pt)
Accepted 3 May 2006
Mammalian protein kinase C (PKC) isoforms have been subject of particular attention because of their ability to modulate apoptotic proteins. However, the roles played by each PKC isoform in apoptosis are still unclear. Here, expression of individual mammalian PKC isoforms in Saccharomyces cerevisiae is used as a new approach to study the role of each isoform in apoptosis. The four isoforms tested, excepting PKC-
, stimulate S. cerevisiae acetic-acid-induced apoptosis essentially through a mitochondrial ROS-dependent pathway. However, their co-expression with Bcl-xL reveals a PKC-isoform-dependent modulation of Bcl-xL anti-apoptotic activity. A yeast pathway homologue to the mammalian SAPK/JNK is responsible for acetic-acid-induced Bcl-xL phosphorylation that is differently modulated by PKC isoforms. The data obtained suggest conservation of an ancient mechanism of apoptosis regulation in yeast and mammals and offer new insights into mammalian apoptosis modulation by PKC isoforms.
Key words: Apoptosis regulation, Bcl-xL, Mammalian PKC isoforms, Yeast
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