We describe studies performed thus far on stefin B from the family of cystatins as a model protein for folding and amyloid fibril formation studies. We also briefly mention our studies on aggregation of some of the missense EPM1 mutants of stefin B in cells, which mimic additional pathological traits (gain in toxic function) in selected patients with EPM1 disease. We collected data on the reported interactors of stefin B and discuss several hypotheses of possible cytosolic alternative functions.
Keywords: amyloid; chaperone; cystatins; membrane binding; oligomers; oxidative stress; protein aggregation; protein folding.
Copyright © 2016 John Wiley & Sons, Ltd.