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Review
. 2023 Jan 29;13(2):251.
doi: 10.3390/biom13020251.

Organismal Roles of Hsp90

Patricija van Oosten-Hawle  1
Affiliations
Review

Organismal Roles of Hsp90

Patricija van Oosten-Hawle. Biomolecules. .

Abstract

Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that assists in the maturation of many client proteins involved in cellular signal transduction. As a regulator of cellular signaling processes, it is vital for the maintenance of cellular proteostasis and adaptation to environmental stresses. Emerging research shows that Hsp90 function in an organism goes well beyond intracellular proteostasis. In metazoans, Hsp90, as an environmentally responsive chaperone, is involved in inter-tissue stress signaling responses that coordinate and safeguard cell nonautonomous proteostasis and organismal health. In this way, Hsp90 has the capacity to influence evolution and aging, and effect behavioral responses to facilitate tissue-defense systems that ensure organismal survival. In this review, I summarize the literature on the organismal roles of Hsp90 uncovered in multicellular organisms, from plants to invertebrates and mammals.

Keywords: Hsp90; cell nonautonomous; inter-tissue stress signaling; organismal; proteostasis; stress response.

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Conflict of interest statement

The author declares no conflict of interest.

Figures

Figure 1
Figure 1
Organismal roles of Hsp90 in different multicellular model systems. In metazoans, such as C. elegans, Mus musculus, D. melanogaster, Danio rerio and A. thaliana, Hsp90 acts in diverse biological processes to ensure organismal proteostasis.
Figure 2
Figure 2
Transcellular chaperone signaling pathways. (A) Overexpression of Hsp90 in the nervous system mediates upregulation of Hsp90 in muscle cells via PQM-1, CLEC-41 and glutamatergic neurotransmission. Overexpression of Hsp90 in the intestine relays the signal to upregulate Hsp90 in muscle cells via PQM-1 and ASP-12. The transcription factor regulating Hsp90 in muscle cells in response to TCS has not been determined. The organismal consequences are increased health span and reduced protein aggregation in the muscle tissue. (B) Knockdown of Hsp90 in the intestine relays the signal to muscle cells via the secreted lipases TXT-4 and TXT-8. There, TXT-1 signals to the transcription factor CEH-58 to induce Hsp70 expression, resulting in increased longevity and stress resilience. HSF-1 functions as a suppressor of this process.
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This work was supported by laboratory start-up funds to P.v.O.-H. from the University of North Carolina at Charlotte.