Specific modulation of apoptosis and Bcl-xL phosphorylation in yeast by distinct mammalian protein kinase C isoforms

• Type: Article in International Scientific Journal
• Date: 2006

Authors

Lucilia Saraiva (Author) FFUP; Rui D Silva (Author) Other; Gil Pereira (Author) Other; Jorge Goncalves (Author) FFUP; Manuela Corte Real (Author) Other

Journal

Title: Journal of Cell Science

Vol. 119 No. 15

Pages: 3171-3181

ISSN: 0021-9533

Publisher: The Company of Biologists Ltd.

Indexing

ISI Web of Knowledge - 30 Citations

ISI Web of Science

Scopus - 33 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

CORDIS: Health sciences

Other information

Authenticus ID: P-004-J66

DOI: 10.1242/jcs.03033

Resumo (PT): 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-d, 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. <br> <br> <a target="_blank" href="http://ejournals.ebsco.com/Article.asp?ContributionID=9519059"> Texto integral</a> <br> <br>

Abstract (EN): 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-delta, stimulate S. cerevisiae acetic-acid-induced apoptosis essentially through a mitochondrial ROS-dependent pathway. However, their coexpression 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 11