Nature Communications (Nov 2016)

Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding

  • Sophia Ungelenk,
  • Fatemeh Moayed,
  • Chi-Ting Ho,
  • Tomas Grousl,
  • Annette Scharf,
  • Alireza Mashaghi,
  • Sander Tans,
  • Matthias P. Mayer,
  • Axel Mogk,
  • Bernd Bukau

DOI
https://doi.org/10.1038/ncomms13673
Journal volume & issue
Vol. 7, no. 1
pp. 1 – 14

Abstract

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Small heat shock proteins (sHsps) contribute to cellular recovery and survival following stress causing elevated levels of misfolded or unfolded proteins. Here the authors demonstrate that sHsps function by maintaining aggregating proteins in close-to-native conformations to facilitate chaperone-mediated refolding.