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Vol. 16, Issue 4, 1971-1986, April 2005
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Protein Gpa2 Act through the cAMP-Protein Kinase A Pathway to Induce Morphogenesis in Candida albicans
* Department of Molecular Microbiology, Flanders Interuniversity Institute for Biotechnology (VIB) and Laboratory of Molecular Cell Biology, Katholieke Universiteit Leuven, B-3001 Leuven-Heverlee, Flanders, Belgium;
Fraunhofer IGB, 70569 Stuttgart, Germany
Submitted September 6, 2004;
Revised January 12, 2005;
Accepted January 13, 2005
Monitoring Editor: Howard Riezman
We investigated the role in cell morphogenesis and pathogenicity of the Candida albicans GPR1 gene, encoding the G protein-coupled receptor Gpr1. Deletion of C. albicans GPR1 has only minor effects in liquid hypha-inducing media but results in strong defects in the yeast-to-hypha transition on solid hypha-inducing media. Addition of cAMP, expression of a constitutively active allele of the G
protein Gpa2 or of the catalytic protein kinase A subunit TPK1 restores the wild-type phenotype of the CaGPR1-deleted strain. Overexpression of HST7, encoding a component of the mitogen-activated protein kinase pathway, does not suppress the defect in filamentation. These results indicate that CaGpr1 functions upstream in the cAMP–protein kinase A (PKA) pathway. We also show that, in the presence of glucose, CaGpr1 is important for amino acid-induced transition from yeast to hyphal cells. Finally, as opposed to previous reports, we show that CaGpa2 acts downstream of CaGpr1 as activator of the cAMP–PKA pathway but that deletion of neither CaGpr1 nor CaGpa2 affects glucose-induced cAMP signaling. In contrast, the latter is abolished in strains lacking CaCdc25 or CaRas1, suggesting that the CaCdc25-CaRas1 rather than the CaGpr1-CaGpa2 module mediates glucose-induced cAMP signaling in C. albicans.
These authors contributed equally to this work.
Address correspondence to: Patrick Van Dijck (patrick.vandijck{at}bio.kuleuven.ac.be).
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