Using yeast to uncover the regulation of protein kinase Cδ by ceramide

Cláudia Bessa, Clara Pereira, Mariana Leão, Cláudia Maciel, Sara Gomes, Jorge Gonçalves, Manuela Corte-Real, Vítor Costa, Lucília Saraiva*

*Autor correspondente para este trabalho

Resultado de pesquisarevisão de pares

3 Citações (Scopus)


The regulation of protein kinase C (PKC) isoforms by ceramide is still controversial. In this work, the yeast Saccharomyces cerevisiae was used as a model to elucidate the effect of ceramide on the activity of mammalian PKC isoforms. For that, isc1Δ cells, with a deletion in the pathway for ceramide production by hydrolysis of complex sphingolipids, individually expressing mammalian PKCα, δ and ζ were used. Contrary to PKCα and ζ, expression of PKCδ in isc1Δ cells exhibited a similar phenotype to that observed with wild-type yeast cells expressing PKCδ treated with a PKC activator, as phorbol 12-myristate 13-acetate (PMA), specifically a growth inhibition associated with a G2/M cell cycle arrest. Interestingly, in isc1Δ yeast cells expressing PKCδ this phenotype was completely abrogated in the presence of exogenous ceramide. Moreover, using a yeast-based assay previously developed for the screening of PKC inhibitors, it was also shown that, like the known PKC inhibitor NPC 15437, ceramide reduced the PMA-induced growth inhibition, supporting an inhibitory effect of ceramide on PKCδ. Altogether, these results may indicate that ceramide distinctly interfere with the activity of PKCα, δ and ζ. Most importantly, they showed that ceramide is an inhibitor of PKCδ.

Idioma originalEnglish
Páginas (de-até)700-705
Número de páginas6
RevistaFEMS Yeast Research
Número de emissão7
Estado da publicaçãoPublicado - nov. 2013

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