Anti-aggregation activity of small heat shock proteins under crowded conditions.

摘要: It is becoming evident that small heat shock proteins (sHsps) are important players of protein homeostasis system. Their ability to bind misfolded may play a crucial role in preventing aggregation cells. The remarkable structural plasticity sHsps considered underlie the mechanism their activity. However, all our knowledge anti-aggregation functioning based on data obtained vitro media greatly different from cellular highly crowded milieu. present review highlights available effect crowding activity sHsps. There some evidence affects conformation and dynamics oligomers as well properties. Crowding stimulates association sHsp-client complexes into large-sized aggregates thus diminishing apparent Nevertheless, it also shown between suboligomers (dissociated forms) client be stabilized exist for longer period time under conditions. Moreover, retard initial stages which correspond formation sHsp-containing nuclei clusters. Thus, dissociation appears an feature media.