sHSP
Small heat shock proteins, abbreviated sHSPs, are a diverse family of molecular chaperones found in nearly all organisms. They function as ATP-independent holdases that prevent aggregation of denatured proteins during cellular stress, such as heat, oxidative stress, or desiccation. By binding exposed hydrophobic regions on unfolded polypeptides, sHSPs keep clients in a refolding-competent state and cooperate with ATP-dependent chaperones like Hsp70 to restore proteostasis.
Most sHSPs share a conserved central alpha-crystallin domain flanked by flexible N- and C-terminal extensions. They
Localization and regulation vary by organism and tissue. sHSPs are found in the cytosol and various organelles,
Functions and clinical relevance extend beyond stress protection. sHSPs participate in protein quality control during normal