Small Heat shock proteins (sHsps)
This family of molecular chaperones is unique as its members form ensembles of oligomeric complexes, which interact with their client proteins in an ATP-independent way. They are regulated by different mechanisms, such as posttranslational modifications or increasing temperatures. We focus on the influence of different sHsps from human, C. elegans or yeast on cell physiology and ageing. Of note, the most prominent family member is α-crystallin, a major component of the eye lens. There, α-crystallin is thought to ensure its transparency and to prevent the aggregation of aging or damaged lens proteins, thus suppressing the development of cataracts. Our goal is to understand the complexity of the eye lens and the fundamental role α-crystallin plays in maintaining the transparency and function of the eye lens.