@entity3457 ( @entity3457 ) kinases are pivotal components of eukaryotic signaling cascades. Phosphorylation of @entity669 and @entity1889 residues activates @entity3457 kinases, but either dual-specificity or monospecificity phosphatases can inactivate them. The @entity5132 CPP1 gene, a structural member of the VH1 family of dual- specificity phosphatases, was previously cloned by its ability to block the pheromone response @entity3457 kinase cascade in @entity375 . Cpp1p inactivated @entity1 @entity3457 kinases in vitro and acted as a @entity669 -specific enzyme. In @entity5132 a @entity3457 kinase cascade can trigger the transition from the budding @entity375 form to a more invasive filamentous form. Disruption of the CPP1 gene in @entity5132 derepressed the @entity375 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 @entity19 model. A hyper-hyphal pathway may thus have some detrimental effects on @entity5132 cells. Disruption of the @entity3457 kinase homologue CEK1 suppressed the morphological effects of the CPP1 disruption in @entity5132 . The results presented here demonstrate the biological importance of a @entity669 phosphatase in cell-fate decisions and virulence in @entity5132 .

Derepressed hyphal growth and reduced virulence in a VH1 family-related protein phosphatase mutant of the XXXX pathogen @entity5132 .

@entity1 :: ('9606', 'Species') :: ['mammalian'] @entity19 :: ('10090', 'Species') :: ['mouse'] @entity5132 :: ('5476', 'Species') :: ['Candida albicans', 'C. albicans'] @entity1889 :: ('CHEBI:26986', 'Chemical') :: ['threonine'] @entity375 :: ('4932', 'Species') :: ['yeast', 'Saccharomyces cerevisiae'] @entity669 :: ('CHEBI:18186', 'Chemical') :: ['tyrosine'] @entity3457 :: ('OMIM:612348', 'Disease') :: ['Mitogen-activated protein', 'MAP']
@entity1 :: (9606,Species) :: ['human']
