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Arch Microbiol ; 204(5): 240, 2022 Apr 04.
Article in English | MEDLINE | ID: mdl-35377020

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.


Subject(s)
Calcineurin , Heat-Shock Proteins , Fungi/metabolism , HSP70 Heat-Shock Proteins , Heat-Shock Proteins/genetics , Heat-Shock Proteins/metabolism , Humans , Protein Processing, Post-Translational
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