Journal
TRENDS IN MICROBIOLOGY
Volume 25, Issue 10, Pages 809-819Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.tim.2017.05.003
Keywords
-
Categories
Funding
- Canadian Institutes of Health Research [MOP-86452, MOP-119520]
- Natural Sciences and Engineering Council (NSERC) of Canada [06261, 462167]
- NSERC [477598]
- National Institutes of Health (NIH) Ruth L. Kirschstein National Research Service Award from the NIAID [AI115947-01]
Ask authors/readers for more resources
Hsp90 is a conserved molecular chaperone that facilitates the folding and function of client proteins. Hsp90 function is dynamically regulated by interactions with co-chaperones and by post-translational modifications. In the fungal pathogen Candida albicans, Hsp90 enables drug resistance and virulence by stabilizing diverse signal transducers. Here, we review studies that have unveiled regulators of Hsp90 function, as well as downstream effectors that govern the key virulence traits of morphogenesis and drug resistance. We highlight recent work mapping the Hsp90 genetic network in C. albicans under diverse environmental conditions, and how these interactions provide insight into circuitry important for drug resistance, morphogenesis, and virulence. Ultimately, elucidating the Hsp90 chaperone network will aid in the development of therapeutics to treat fungal disease.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available