Role of HSPB8 in the Proteostasis Network: From Protein Synthesis to Protein Degradation and Beyond

摘要: Proper protein folding is crucial for stability and function; when fails, due to stress or genetic mutations, proteins may become toxic. Cells have evolved a complex quality control (PQC) system protect against the toxicity exerted by aberrantly folded proteins, that aggregate accumulating in various cellular compartments perturbing essential activities, ultimately leading cell neuron death. The PQC comprises molecular chaperones, degradative systems (proteasome autophagy) components of unfolded response. Prevention aggregation, clearance misfolded substrates attenuation translation, which decreases amount misfolding clients levels manageable are all key steps maintenance proteostasis survival. In parallel, alterations also (indirectly) influence RNA homeostasis; fact, RNA-containing aggregates, known as granules, accumulate cells with impaired autophagy colocalizing proteinaceous aggregates several neurodegenerative diseases. Among different here we will focus on small heat shock HSPB8, expressed neurons basal conditions upregulated response accumulation. HSPB8 exerts protective functions models conformation putative sites action confer pro-survival anti-aggregation discussed, well its potential role at cross-road between ribostasis.