Heat shock proteins and the calcineurin-crz1 signaling regulate stress responses in fungi

Arch Microbiol. 2022 Apr 4;204(5):240. doi: 10.1007/s00203-022-02833-w.

Abstract

The heat shock proteins (Hsps) act as a molecular chaperone to stabilize client proteins involved in various cell functions in fungi. Hsps are classified into different families such as HSP90, HSP70, HSP60, HSP40, and small HSPs (sHsps). Hsp90, a well-studied member of the Hsp family proteins, plays a role in growth, cell survival, and pathogenicity in fungi. Hsp70 and sHsps are involved in the development, tolerance to stress conditions, and drug resistance in fungi. Hsp60 is a mitochondrial chaperone, and Hsp40 regulates fungal ATPase machinery. In this review, we describe the cell functions, regulation, and the molecular link of the Hsps with the calcineurin-crz1 calcium signaling pathway for their role in cell survival, growth, virulence, and drug resistance in fungi and related organisms.

Keywords: Antifungal drug; Calcienruin-crz1; Calcium; Heat shock proteins; Stress response.

Publication types

  • Review

MeSH terms

  • Calcineurin*
  • Fungi / metabolism
  • HSP70 Heat-Shock Proteins
  • Heat-Shock Proteins* / genetics
  • Heat-Shock Proteins* / metabolism
  • Humans
  • Protein Processing, Post-Translational

Substances

  • HSP70 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Calcineurin