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Abstract Small Heat Shock Protein Family B (HSPB) members are ATP-independent chaperones essential for maintaining cellular proteostasis. Together with chaperones and co-chaperones such as HSP70 and BAG3, they prevent aberrant protein folding and suppress protein aggregation, particularly under proteotoxic stress. HSPBs have also been extensively linked to neurodegenerative disease and in promoting chemoresistance in cancer.
Conflicts of Interest The authors declare no conflicts of interest. Supporting Information Filename Description jgm70013-sup-0001-FigureS1.pngPNG image, 316.6 KB Figure S1. High viral titres cause neuronal toxicity. (A) Single RT-qPCR experiment showing the relative expression of HSPB8 at Day 24 in human iPSC–derived motor neurons left untreated or transduced with a shRNA construct.
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