Hsp90 interaction networks in fungi – tools and techniques

Julia L Crunden, Stephanie Diezmann*

*Corresponding author for this work

Research output: Contribution to journalReview article (Academic Journal)peer-review

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Abstract

Heat-shock protein 90 (Hsp90) is a central regulator of cellular proteostasis. It
stabilizes numerous proteins that are involved in fundamental processes of life, including cell growth, cell cycle progression, and the environmental response. In addition to stabilizing proteins, Hsp90 governs gene expression and controls the release of cryptic genetic variation. Given its central role in evolution and development, it is important to identify proteins and genes that interact with Hsp90. This requires sophisticated genetic and biochemical tools, including extensive mutant collections, suitable epitope tags, proteomics approaches and
Hsp90 specific pharmacological inhibitors for chemogenomic screens. These usually only exist in model organisms, such as the yeast Saccharomyces cerevisiae. Yet, the importance of other fungal species, such as Candida albicans and Cryptococcus neoformans, as serious human pathogens accelerated the development of genetic tools to study their virulence and stress response pathways. These tools can also be exploited to map Hsp90 interaction
networks. Here, we review tools and techniques for Hsp90 network mapping available in different fungi and provide a summary of existing mapping efforts. Mapping Hsp90 networks in fungal species spanning >500 million years of evolution provides a unique vantage point, allowing tracking of the evolutionary history of eukaryotic Hsp90 networks.
Original languageEnglish
JournalFEMS Yeast Research
Early online date28 Oct 2021
DOIs
Publication statusE-pub ahead of print - 28 Oct 2021

Keywords

  • protein-protein interactions
  • proteomics
  • chemogenomics
  • Hsp90
  • synthetic lethality
  • mutant libraries
  • Candida
  • Cryptococcus neoformans
  • Aspergillus fumigatus

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