ИСТИНА

Small heat shock proteins - is a ubiquitous group of proteins that expresses in a wide range of organisms: from archea to human. It`s may be explained by a lot of sHSP functions. For instance, sHSPs involve in maintenance of Red-Ox status in cells, in apoptosis and proteostasis. A hallmark of small heat shock proteins group is an ability to prevent aggregation of partially denatured proteins or ability to so called chaperone-like activity. In view of these, unsurprisingly, mutations in sHSP genes are associated with different diseases. We studied physical-chemical properties of several sHsp mutants. Research demonstrates that all pathological mutations lead to alteration of oligomers stability. Both increase and decrease of stability result in disfunction of small heat shock proteins. In other world optimum is exist and must be observe. In addition, all pathological mutations lead to change of heterooligomerization and chaperone-like activity. At last, it was found abnormality of phosphorylation and, consequently, activity regulation. It seems that the key element of sHSP dysfunction is alteration of sHSP stability. So formation of metastable oligomers is essential to normal sHSP functioning.