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Vol. 8, Issue 12, 2539-2551, December 1997
§ and§
*Centre de Recherche, Hôtel-Dieu de Montréal and
Department of Pharmacology, University of Montreal, Montreal, Quebec,
Canada H2W 1T8;
Mitogen-activated protein (MAP) kinases are pivotal components of
eukaryotic signaling cascades. Phosphorylation of tyrosine and
threonine residues activates MAP kinases, but either dual-specificity or monospecificity phosphatases can inactivate them. The Candida albicans CPP1 gene, a structural member of the VH1 family of
dual- specificity phosphatases, was previously cloned by its ability to
block the pheromone response MAP kinase cascade in Saccharomyces cerevisiae. Cpp1p inactivated mammalian MAP kinases in vitro
and acted as a tyrosine-specific enzyme. In C. albicans
a MAP kinase cascade can trigger the transition from the budding yeast
form to a more invasive filamentous form. Disruption of the
CPP1 gene in C. albicans derepressed the
yeast to hyphal transition at ambient temperatures, on solid surfaces.
A hyphal growth rate defect under physiological conditions in vitro was
also observed and could explain a reduction in virulence associated
with reduced fungal burden in the kidneys seen in a systemic mouse
model. A hyper-hyphal pathway may thus have some detrimental effects on
C. albicans cells. Disruption of the MAP kinase
homologue CEK1 suppressed the morphological effects of
the CPP1 disruption in C. albicans. The
results presented here demonstrate the biological importance of a
tyrosine phosphatase in cell-fate decisions and virulence in C.
albicans.
Eukaryotic Genetics Group, National
Research Council of Canada, Biotechnology Research Institute, Montreal,
Quebec, Canada H4P 2R2;
Institute of Clinical
Microbiology and Immunology, University of Erlangen, D-91054 Erlangen,
Germany; and
§Biology Department, McGill University,
Montreal, Quebec, Canada H3A 1B1
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