Structure and Function of Small Heat Shock Proteins

Dear Colleagues,

Small heat shock proteins form a very large and diverse family of proteins ubiquitously expressed in viruses, archaea, bacteria, plants and animals. Together with other chaperones small heat shock proteins control proper protein folding and prevent accumulation of denatured proteins in the cells. As a rule several isoforms of small heat shock proteins are simultaneously expressed in the cell and these isoforms can form both homo- and heterooligomeric complexes and can interact with other chaperones providing effective protein quality control. Small heat shock proteins undergo different posttranslational modifications that affect their structure, function and interaction with partner proteins. Small heat shock proteins are involved in many intra- and extracellular processes including control of redox state, proteasomal and autosomal protein degradation, apoptosis, regulation of cytoskeleton and muscle contraction, immunological response and many others. Mutations of small heat shock proteins correlate with many congenital disorders including cataract, different neurodegenerative diseases, cardiomyopathies and myopathies. Moreover, small heat shock proteins can be used as markers of different human diseases including cancer.

The goal of this special issue is to present the current knowledge on the structure and function of small heat shock proteins and their probable involvement in different cellular processes and human diseases.

We look forward to your contributions.

Prof. Dr. Nikolai B. Gusev
Guest Editor

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