HSPB8 (heat shock protein family B member 8) is a small chaperone protein that plays a crucial role in chaperone-assisted selective autophagy (CASA), a protein quality control mechanism particularly important in mechanically strained tissues like muscle 1. HSPB8 functions within a complex that includes HSPA, the cochaperone BAG3, and the E3 ubiquitin ligase STUB1 to promote selective degradation of misfolded and aggregating proteins 1. The protein exhibits temperature-dependent chaperone activity and is essential for maintaining cellular proteostasis under stress conditions 2. HSPB8 mutations cause several neuromuscular disorders including Charcot-Marie-Tooth disease type 2L, myofibrillar myopathy 13, and distal hereditary motor neuropathy type 2 34. Frameshift mutations in HSPB8 lead to protein aggregation that sequesters CASA components and autophagy receptors, resulting in impaired proteostasis and altered muscle cell differentiation 1. Beyond neuromuscular disorders, HSPB8 is involved in cancer biology, where it can have dual roles in tumor development and progression, and may contribute to chemoresistance 5. The protein's expression can be modulated by retinoic acid, which downregulates HSPB8 levels in breast cancer cells 6.