Cdc28 provides a molecular link between Hsp90, morphogenesis, and cell cycle progression in Candida albicans.

ABSTRACT: The trimorphic fungus Candida albicans is the leading cause of systemic candidiasis, a disease with poor prognosis affecting immunocompromised individuals. The capacity of C. albicans to transition between morphological states is a key determinant of its ability to cause life-threatening infection. Recently the molecular chaperone heat shock protein 90 (Hsp90) was implicated as a major regulator of temperature-dependent C. albicans morphogenesis; compromising Hsp90 function induces filamentation and relieves repression of Ras1-protein kinase A (PKA) signaling, although the mechanism involved remains unknown. Here we demonstrate that filaments generated by compromise of Hsp90 function are neither pseudohyphae nor hyphae but closely resemble filaments formed in response to cell cycle arrest.

SUBMITTER: Senn H 

PROVIDER: S-EPMC3258172 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature