The ER has many complex proteins and so have a robust system for heat-shock protein assisted folding1/19/2024 In mammalian cells, they are classified into five families according to their molecular weight: Hsp100, Hsp90, Hsp70, Hsp60 and small heat shock proteins including Hsp27. It is now known that heat shock proteins function as molecular chaperones and can play many roles in the cell in addition to modulating the heat shock response. ![]() They were accidentally discovered in 1962, as a set of genes whose expression is elevated by heat shock in Drosophila melanogaster. Although the proteins are frequently associated with the cellular stress response, they also play an important role in supporting normal cellular processes such as development and differentiation. The multi-functional nature of heat shock proteins enables them to play critical roles in the regulation of protein homeostasis and cell survival. They are involved in a wide range of cellular processes such as assisting protein folding and degradation of misfolded proteins, intracellular trafficking, modulating signalling pathways and regulating immune responses. Heat shock proteins are a group of highly conserved proteins found in both eukaryotic and prokaryotic cells.
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