Heat Shock Protein Beta 11 (HSPb11)

Heat shock proteins (HSP) were originally identified as stress-responsive proteins required to deal with proteotoxic stresses.HSPB11 was shown to form oligomeric complexes and to prevent the aggregation of in vitro denaturated aldolase and glyceraldehyde-3-phosphate dehydrogenase in accordance with the chaperone model of HSPB1 and HSPB5. HSPB11 overexpression protected against etoposide-induced cell death which correlated with a decreased release of mitochondrial cytochrome c into the cytosol. Inhibiting HSP90 function completely abrogated the protective effect of HSPB11. This would suggest that at least in the case of HSPB11, interaction with other chaperone machines besides HSPA1A may contribute to functional specificity and cellular functioning.