Abstract
The HSP90 protein is a molecular chaperone intensively studied for its role in numerous cellular processes both under physiological and stress conditions. This protein acts on a wide range of substrates with a well-established role in cancer and neurological disorders. In this review, we focused on the involvement of HSP90 in the silencing of transposable elements and in the genomic integrity maintenance. The common feature of transposable elements is the potential jumping in new genomic positions, causing chromosome structure rearrangements, gene mutations, and influencing gene expression levels. The role of HSP90 in the control of these elements is evolutionarily conserved and opens new perspectives in the HSP90-related mechanisms underlying human disorders. Here, we discuss the hypothesis that its role in the piRNA pathway regulating transposons may be implicated in the onset of neurological diseases.
Highlights
In Drosophila melanogaster, it has recently been established that the HSP90/HSP70 chaperone machinery including HSP70/HSP90 organizing protein (Hop), Hsc70-4, and Hsp40, is ordinarily required to load Piwi Interacting RNAs (piRNAs) onto Argonaute 3 (Ago3) during piRNAs biogenesis (Figure 1)
We demonstrated that dFmr1 genetically and biochemically interacts in gonads and in the nervous system with Ago1 and with Aubergine, the partner of Ago3 in the ping-pong process [52]
We focused on the HSP90-mediated role in the piRNA pathway regulating the transposable elements and preventing genome instability
Summary
The HSP90 protein exhibits an extraordinary conservation of sequence and functions during evolution and is expressed from bacteria to humans. Due to its role as a molecular chaperone, HSP90 binds and stabilizes hundreds of proteins with roles in many processes such as cellular and oxidative stress, and is involved in cancer and neurological disorders [1,2,3,4,5,6,7,8]. One class of cochaperone contains a tetratricopeptide repeat (TPR) domain that binds the C-terminal domain of HSP90 This class includes evolutionarily conserved peptidylprolyl isomerases, most of which belong to the FK506-binding protein (FKBP) family. The crucial activities of HSP90 on the genomes include its role in the DNA damage sensing signaling and repair [23] and its activity to avoid the deleterious jumping of transposable elements (TEs) [24,25]
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