Journal
BIOMOLECULES
Volume 13, Issue 2, Pages -Publisher
MDPI
DOI: 10.3390/biom13020251
Keywords
Hsp90; organismal; cell nonautonomous; proteostasis; stress response; inter-tissue stress signaling
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Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that assists in the maturation of client proteins involved in cellular signal transduction. It plays a crucial role in maintaining cellular proteostasis and adapting to environmental stresses. Hsp90 also functions as an environmentally responsive chaperone in multicellular organisms, contributing to inter-tissue stress signaling responses and organismal health.
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.
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