CaTip41 regulates protein phosphatase 2A activity, CaRad53 deactivation and the recovery of DNA damage-induced filamentation to yeast form in Candida albicans.
FEMS Yeast Res
; 16(2): fow009, 2016 Mar.
Article
em En
| MEDLINE
| ID: mdl-26851402
ABSTRACT
Phosphorylation and dephosphorylation of the checkpoint kinase CaRad53 is crucial for fungal cells in response to genotoxic stresses. The protein phosphatase 2A (PP2A) CaPph3/CaPsy2 phosphatase complex is involved in CaRad53 dephosphorylation in Candida albicans. In view of the role of ScTip41/ScTap42 in regulating PP2A phosphatases in Saccharomyces cerevisiae, we have explored the function of CaTip41 in C. albicans. Here, we show that CaTIP41 is a functional ortholog of ScTIP41 in the sensitivity of S. cerevisiae cells to rapamycin. Deletion of CaTIP41 causes C. albicans cells to be sensitive to DNA damaging agents, methylmethane sulfonate (MMS) and cisplatin, and resistant to both rapamycin and caffeine. Accordingly, expression of CaTip41 increases in response to MMS and cisplatin. In addition, C. albicans cells lacking CaTIP41 show a delay in the recovery from MMS-induced filamentation to yeast form, decreased PP2A activity and a defect in deactivation of CaRad53 during recovery from DNA damage. Through yeast two-hybrid assay we show that CaTip41 interacts with either CaPph3, CaPsy2 or CaTap42. Therefore, CaTip41 plays regulatory roles in both the CaRad53 deactivation during recovery from DNA damage and the target of rapamycin signaling pathway.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Dano ao DNA
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Candida albicans
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Regulação Fúngica da Expressão Gênica
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Peptídeos e Proteínas de Sinalização Intracelular
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Proteína Fosfatase 2
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Quinase do Ponto de Checagem 2
Idioma:
En
Revista:
FEMS Yeast Res
Assunto da revista:
MICROBIOLOGIA
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
China