« Previous AbstractHeadspace collection of grapevine volatiles in a Hungarian vineyard    Next Abstract'Move or Not to Move'-Red Deer Stags Movement Activity during the Rut »

Mol Biol Cell

Title:		Derepressed hyphal growth and reduced virulence in a VH1 family-related protein phosphatase mutant of the human pathogen Candida albicans
Author(s):		Csank C; Makris C; Meloche S; Schroppel K; Rollinghoff M; Dignard D; Thomas DY; Whiteway M;
Address:		"Centre de Recherche, Hotel-Dieu de Montreal and Department of Pharmacology, University of Montreal, Montreal, Quebec, Canada H2W 1T8"
Journal Title:		Mol Biol Cell
Year:		1997
Volume:		8
Issue:		12
Page Number:		2539 - 2551
DOI:		10.1091/mbc.8.12.2539
ISSN/ISBN:		1059-1524 (Print) 1059-1524 (Linking)
Abstract:		"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"
Keywords:		Amino Acid Sequence Animals Binding Sites Candida albicans/*enzymology/genetics/metabolism/*pathogenicity Candidiasis/microbiology Cell Division Cell Size Dual-Specificity Phosphatases Female Fungal Proteins/antagonists & inhibitors/genetics/metabolism Ge;
Notes:		"MedlineCsank, C Makris, C Meloche, S Schroppel, K Rollinghoff, M Dignard, D Thomas, D Y Whiteway, M eng Research Support, Non-U.S. Gov't 1997/12/17 Mol Biol Cell. 1997 Dec; 8(12):2539-51. doi: 10.1091/mbc.8.12.2539"