LAUSR

Small heat shock proteins (sHSPs), often known as molecular chaperones, are most prevalent in nature. Under certain stress-induced conditions, these sHSPs act as an ATP-independent variation and thus prevent the inactivation of various non-native substrate proteins and their aggregation. They also assist other ATP-dependent chaperones in the refolding of these substrates. In the case of prokaryotes and lower eukaryotes, the chaperone functions of sHSPs can bind a wide range of cellular proteins but preferentially protect translation-related proteins and metabolic enzymes. Eukaryotes usually encode a larger number of sHSPs than those of prokaryotes. The chaperone functions of mammalian sHSPs are regulated by phosphorylation in cells and also by temperature. Their sHSPs have different sub-cellular compartments and cell/tissue specificity. The substrate proteins of mammalian sHSPs or eukaryotic sHSPs accordingly reflect their multi-cellular complexity. The sHSPs of animals play roles in different physiological processes as cell differentiation, apoptosis, and longevity. In this work, the characterization, location, tissue specificity, and functional diversity of sHSPs from seven different mammalian species with special emphasis on humans have been studied. Through this extensive work, a novel and significant attempt have been made to classify them based on their omnipresence, tissue specificity, localization, secondary structure, probable mutations, and evolutionary significance.