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Showing 1–12 of 12 results
Advanced filters: Author: Axel Mogk Clear advanced filters

  • 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.

    • Sophia Ungelenk
    • Fatemeh Moayed
    • Bernd Bukau
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-14

  • In the E. coli Hsp100/Hsp70 system, the M domain of ClpB is essential for ClpB cooperation with DnaK and DnaJ and for protein disaggregation, but its function was largely unknown. New biochemical and biophysical data now indicate that the M domain acts as a molecular toggle that reversibly interacts with the AAA-1 domain of ClpB to regulate ATP hydrolysis and protein disaggregation activities. Also in this issue, Seyffer et al. show how DnaK interactions with M domain further enhance ClpB activity.

    • Yuki Oguchi
    • Eva Kummer
    • Bernd Bukau
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 1338-1346

  • The sequestration of misfolded proteins into large assemblies by sequestrases is now considered as the third pillar in protein quality control besides chaperones and proteases. Here the authors characterise the functions of the sequestrases Hsp42 and Btn2 in the proteostasis network of S. cerevisiae and find that they protect cells from too exhaustive depletion of the Hsp70 system.

    • Chi-ting Ho
    • Tomas Grousl
    • Axel Mogk
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-15

  • DnaK targets protein aggregates to ClpB. New data show that DnaK also activates ClpB in a species-specific manner through direct interactions with the M domain of ClpB, stabilizing a derepressed state that increases the ATP hydrolysis and protein disaggregation activities of the chaperone. Also in this issue, Oguchi et al. show how the M domain of ClpB acts as a reversible toggle to regulate these activities.

    • Fabian Seyffer
    • Eva Kummer
    • Axel Mogk
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 1347-1355

  • A combination of optical tweezers and fluorescent-particle tracking is used to dissect the dynamics of the Hsp100 disaggregase ClpB, and show that the processive extrusion of polypeptide loops is the mechanistic basis of its activity.

    • Mario J. Avellaneda
    • Kamila B. Franke
    • Sander J. Tans
    Research
    Nature
    Volume: 578, P: 317-320

  • The Lon protease is an important protein degradation machine and is conserved across the three domains of life. Here, the authors describe a small proteotoxic stress-induced protein that functions as an allosteric activator of Lon.

    • Deike J. Omnus
    • Matthias J. Fink
    • Kristina Jonas
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-19

  • Azinas et al. report the cryo-EM structure of the MecA/ClpC/ClpP complex from Staphylococcus aureus, revealing how MecA forms a crown-like structure that likely facilitates substrate transfer to ClpC. They uncover asymmetric, activity-dependent interactions between ClpC and ClpP and demonstrate reciprocal allosteric regulation which enhances ATPase and proteolytic activity in bacterial AAA+ proteases.

    • Stavros Azinas
    • Karin Wallden
    • Marta Carroni
    ResearchOpen Access
    Communications Biology
    Volume: 8, P: 1-18

  • The aggregation of misfolded proteins is associated with the perturbation of cellular function and ageing. However, protein aggregation can also be a regulated process that deposits aggregates at specific cellular sites. This is protective as it facilitates aggregate solubilization, refolding and degradation by the protein quality-control network.

    • Jens Tyedmers
    • Axel Mogk
    • Bernd Bukau
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 11, P: 777-788