The essential molecular chaperone heat shock protein 90 (Hsp90) is a highly conserved protein hub, which modulates the genotype to phenotype translation in animals, plants and fungi. In doing so, Hsp90 interacts with up to 10% of the eukaryotic cell’s proteome. In the leading fungal pathogen of humans, Candida albicans, Hsp90 governs virulence, morphogenesis and drug resistance. While specific Hsp90 clients have been identified and described, a global overview of Hsp90 interactions in this pathogen remained elusive until recently.Here we discuss recent advancements in mapping the C. albicans Hsp90 chaperone network. We describe the first Hsp90 genetic interaction network in C. albicans, discuss its divergence from that of its relative Saccharomyces cerevisiae and illustrate how the network informs our understanding of fungal biology, stress responses and virulence. Deciphering the Hsp90 chaperone network holds great promise for the development of suitable measures to combat fungal drug resistance and counter the ever-increasing number of Candida infections.
|Title of host publication||The Molecular Chaperones Interaction Networks in Protein Folding and Degradation|
|Number of pages||22|
|Publication status||Published - 2014|