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Showing 1–3 of 3 results
Advanced filters: Author: Fabian Seyffer Clear advanced filters

  • 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

  • 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

  • Viral pathogens frequently target host cell antigen-processing pathways, including MHC-I–TAP peptide transporters, to evade host immunity. Blander and colleagues describe how MHC-I molecules can still cross-present antigen by re-routing ERGIC-resident MHC molecules to phagosomal vesicles, where phagolysosomal proteases act to shape the peptide repertoire for MHC-I presentation.

    • Gaëtan Barbet
    • Priyanka Nair-Gupta
    • J. Magarian Blander
    Research
    Nature Immunology
    Volume: 22, P: 497-509