Review Article
Molecular Chaperones of Leishmania: Central Players in Many Stress-Related and -Unrelated Physiological Processes
Table 1
Main classes of molecular chaperones.
| Family name | Functions |
| HSP100 | Unfolding, solubilisation of aggregates, proteolysis |
| HSP90 | Protein maturation of steroid receptors, protein kinases, and other components of cellular signalling pathways. Organelle-specific variants exist |
| HSP70 | Nascent-protein folding, refolding of denatured proteins, and translocation across membranes. Organelle-specific variants exist |
| HSP60/chaperonins | Protein folding and prevention of aggregation (bacterial and mitochondrial proteins) |
| CCT (TRiC) | Folding of cytoskeleton components |
| HSP40 | Hsp70 ATPase activators and intrinsic chaperone activity |
| Small HSPs (sHSPs) | Prevention of aggregation, probable role in membrane homeostasis |
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