Putative alternative functions of human stefin B (cystatin B): binding to amyloid-beta, membranes, and copper

J Mol Recognit. 2017 Jan;30(1). doi: 10.1002/jmr.2562. Epub 2016 Aug 31.

Abstract

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.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / metabolism*
  • Binding Sites
  • Cell Membrane / metabolism*
  • Copper / metabolism*
  • Cystatin B / chemistry*
  • Cystatin B / genetics
  • Cystatin B / metabolism*
  • Humans
  • Models, Molecular
  • Mutation, Missense
  • Protein Binding
  • Protein Conformation
  • Protein Folding

Substances

  • Amyloid beta-Peptides
  • CSTB protein, human
  • Copper
  • Cystatin B