IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v7y2016i1d10.1038_ncomms13673.html
   My bibliography  Save this article

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

Author

Listed:
  • Sophia Ungelenk

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance
    German Cancer Research Center (DKFZ))

  • Fatemeh Moayed

    (FOM Institute for Atomic and Molecular Physics (AMOLF))

  • Chi-Ting Ho

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance
    German Cancer Research Center (DKFZ))

  • Tomas Grousl

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance
    German Cancer Research Center (DKFZ))

  • Annette Scharf

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance)

  • Alireza Mashaghi

    (FOM Institute for Atomic and Molecular Physics (AMOLF))

  • Sander Tans

    (FOM Institute for Atomic and Molecular Physics (AMOLF))

  • Matthias P. Mayer

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance)

  • Axel Mogk

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance
    German Cancer Research Center (DKFZ))

  • Bernd Bukau

    (Center for Molecular Biology of the University of Heidelberg (ZMBH), DKFZ-ZMBH Alliance
    German Cancer Research Center (DKFZ))

Abstract

Small heat shock proteins (sHsp) constitute an evolutionary conserved yet diverse family of chaperones acting as first line of defence against proteotoxic stress. sHsps coaggregate with misfolded proteins but the molecular basis and functional implications of these interactions, as well as potential sHsp specific differences, are poorly explored. In a comparative analysis of the two yeast sHsps, Hsp26 and Hsp42, we show in vitro that model substrates retain near-native state and are kept physically separated when complexed with either sHsp, while being completely unfolded when aggregated without sHsps. Hsp42 acts as aggregase to promote protein aggregation and specifically ensures cellular fitness during heat stress. Hsp26 in contrast lacks aggregase function but is superior in facilitating Hsp70/Hsp100-dependent post-stress refolding. Our findings indicate the sHsps of a cell functionally diversify in stress defence, but share the working principle to promote sequestration of misfolding proteins for storage in native-like conformation.

Suggested Citation

  • Sophia Ungelenk & Fatemeh Moayed & Chi-Ting Ho & Tomas Grousl & Annette Scharf & Alireza Mashaghi & Sander Tans & Matthias P. Mayer & Axel Mogk & Bernd Bukau, 2016. "Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding," Nature Communications, Nature, vol. 7(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13673
    DOI: 10.1038/ncomms13673
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms13673
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms13673?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Moritz Mühlhofer & Carsten Peters & Thomas Kriehuber & Marina Kreuzeder & Pamina Kazman & Natalia Rodina & Bernd Reif & Martin Haslbeck & Sevil Weinkauf & Johannes Buchner, 2021. "Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
    2. Y Hoang & Christopher A. Azaldegui & Rachel E. Dow & Maria Ghalmi & Julie S. Biteen & Anthony G. Vecchiarelli, 2024. "An experimental framework to assess biomolecular condensates in bacteria," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    3. Kevin Wu & Thomas C. Minshull & Sheena E. Radford & Antonio N. Calabrese & James C. A. Bardwell, 2022. "Trigger factor both holds and folds its client proteins," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13673. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.