Chaperones articles within Nature

Featured

  • Article
    | Open Access

    We identify a highly controlled cytosolic surveillance mechanism that integrates independent mitochondrial stress signals to initiate the mitochondrial unfolded protein response (UPR), revealing a link between mitochondrial and cytosolic proteostasis.

    • F. X. Reymond Sutandy
    • , Ines Gößner
    •  & Christian Münch

  • Article |

    Biochemical and structural analysis of intermediates during multipass membrane protein biogenesis showed how an intramembrane chaperone guides nascent membrane proteins to a semi-enclosed lipid-filled cavity where they are inserted and folded correctly.

    • Luka Smalinskaitė
    • , Min Kyung Kim
    •  & Ramanujan S. Hegde

  • Article |

    The cryo-electron microscopy structure of the glucocorticoid receptor (GR)-loading complex—a complex in which Hsp70 loads GR onto Hsp90 and Hop—is described, providing insights into how the chaperones Hsp90 and Hsp70 coordinate to facilitate GR remodelling for activation.

    • Ray Yu-Ruei Wang
    • , Chari M. Noddings
    •  & David A. Agard

  • Article |

    The molecular steps that lead to the disaggregation of amyloid fibrils are shown to involve the synergistic action of HSP70 and its co-chaperones DNAJB1 and HSP110.

    • Anne S. Wentink
    • , Nadinath B. Nillegoda
    •  & Bernd Bukau

  • Article |

    The PAT complex, an intermembrane chaperone complex comprising the ER-resident membrane proteins CCDC47 and Asterix, directly interacts with nascent transmembrane domains to facilitate the biogenesis of multi-spanning membrane proteins.

    • Patrick J. Chitwood
    •  & Ramanujan S. Hegde

  • Article |

    A systematic analysis of the proteostasis network of secreted proteins in Caenorhabditis elegans identifies numerous regulators of protein homeostasis outside the cell, and highlights the contribution of extracellular proteostasis to host defence.

    • Ivan Gallotta
    • , Aneet Sandhu
    •  & Della C. David

  • Article |

    Chaperones interact with a canonical motif in α-synuclein, which can be prevented by phosphorylation of α-synuclein at Tyr39, whereas inhibition of this interaction leads to the localization of α-synuclein to the mitochondria and aggregate formation.

    • Björn M. Burmann
    • , Juan A. Gerez
    •  & Sebastian Hiller

  • Letter |

    Hsp70 binds unfolded protein segments in its groove, but can also bind and stabilize folded protein structures, owing to its moveable lid, with ATP hydrolysis and co-chaperones allowing control of these contrasting effects.

    • Alireza Mashaghi
    • , Sergey Bezrukavnikov
    •  & Sander J. Tans

  • Letter |

    Here, the selection of substrates by the protein–RNA complex known as the signal recognition particle (SRP) is investigated in the bacterium Escherichia coli, revealing that the SRP has a strong preference for hydrophobic transmembrane domains of inner membrane proteins.

    • Daniela Schibich
    • , Felix Gloge
    •  & Günter Kramer

  • Letter |

    An efficient protein disaggregation system uncovered in metazoan cells requires transient interactions between J-protein co-chaperones of classes A and B, which synergistically boost HSP70-dependent disaggregation activity, providing a flexible further level of regulation for metazoan protein quality control, with direct relevance to human diseases such as age-related neurodegeneration.

    • Nadinath B. Nillegoda
    • , Janine Kirstein
    •  & Bernd Bukau

  • Letter |

    Molecular, pharmacological and functional data show that haematopoietic stem cells (HSCs) are predisposed to ER-stress-mediated apoptosis compared to closely related progenitors; a framework for understanding how stress signalling is coordinated within the hematopoietic hierarchy and integrated with stemness is provided, and may have implications for the improvement of clinical transplantation of HSCs.

    • Peter van Galen
    • , Antonija Kreso
    •  & John E. Dick

  • News Feature |

    Susan Lindquist has challenged conventional thinking on how misfolded proteins drive disease and may power evolution. But she still finds that criticism stings.

    • Bijal P. Trivedi

  • Letter |

    Group II chaperonins are present in eukaryotes and archaea and are essential mediators of cellular protein folding. This process is critically dependent on the closure of a built-in lid, which is triggered by ATP hydrolysis, but the structural rearrangements and molecular events leading to lid closure are unknown. Using cryo-electron microscopy, the structures of an archaeal group II chaperonin in the open and closed states are now reported, providing details of this mechanism.

    • Junjie Zhang
    • , Matthew L. Baker
    •  & Wah Chiu

Browse broader subjects

Browse Chaperones across other nature.com journals