Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs

Nat Rev Microbiol. 2012 Oct;10(10):693-704. doi: 10.1038/nrmicro2875.


Heat shock protein 90 (HSP90) is an essential, abundant and ubiquitous eukaryotic chaperone that has crucial roles in protein folding and modulates the activities of key regulators. The fungal Hsp90 interactome, which includes numerous client proteins such as receptors, protein kinases and transcription factors, displays a surprisingly high degree of plasticity that depends on environmental conditions. Furthermore, although fungal Hsp90 levels increase following environmental challenges, Hsp90 activity is tightly controlled via post-translational regulation and an autoregulatory loop involving heat shock transcription factor 1 (Hsf1). In this Review, we discuss the roles and regulation of fungal Hsp90. We propose that Hsp90 acts as a biological transistor that modulates the activity of fungal signalling networks in response to environmental cues via this Hsf1-Hsp90 autoregulatory loop.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Feedback, Physiological
  • Fungal Proteins / physiology*
  • Fungi / physiology*
  • Gene Expression Regulation, Fungal
  • HSP90 Heat-Shock Proteins / physiology*
  • Signal Transduction
  • Transcriptome


  • Fungal Proteins
  • HSP90 Heat-Shock Proteins