Protein aggregation articles within Nature Cell Biology

Featured

  • News & Views |

    Aggregation of the RNA-binding protein TDP-43 is commonly observed in neurodegenerative disorders. A new study reveals that this process may be blocked by HSPB1, a small heat shock protein that can also regulate TDP-43 phase separation. This may be relevant to neurodegeneration, as loss of HSPB1 correlates with TDP-43 pathology.

    • Yuna M. Ayala
    •  & Zachary R. Grese

  • News & Views |

    Overload of proteasomal clearance triggers formation of a large protein inclusion called the aggresome, which shares similarities with protein aggregates seen in neurodegenerative diseases such as Huntington’s. A new study uncovers how centrosome and centriolar satellite components facilitate stepwise assembly of aggresomes.

    • Elisa Vitiello
    •  & Fanni Gergely

  • News & Views |

    Cells respond to stimuli by reorganizing their contents into subcellular structures. New research demonstrates that yeast pyruvate kinase Cdc19 interacts with fructose-1,6-bisphosphate to coordinate disassembly of stress granules. These findings reveal how proteins can directly sense the cellular energy state to facilitate adaptive reorganization.

    • Christopher M. Jakobson
    •  & Daniel F. Jarosz

  • Perspective |

    In this Perspective, Fuxreiter and Vendruscolo discuss the fundamental nature of the droplet and amyloid states of proteins, the regulatory mechanisms controlling their formation, and the cellular functions associated with these condensed states.

    • Monika Fuxreiter
    •  & Michele Vendruscolo

  • News & Views |

    Secretory proteins undergo multiple rounds of co- and post-translational quality control checks inside the cell, but how their integrity is maintained outside the cell is an emerging topic. A study establishes a model system to investigate how the extracellular proteome is protected and integrates its findings into existing immune pathways.

    • Brant M. Webster
    • , Holly K. Gildea
    •  & Andrew Dillin

  • News & Views |

    It is generally accepted that protein function depends on a defined 3D structure, with unfolding and aggregation dealing a final blow to functionality. A study now shows that the regulated exposure of an unstructured region in yeast pyruvate kinase triggers reversible aggregation to preserve protein function under stress.

    • Jörg Höhfeld

  • Article |

    Mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) lead to accumulation of proteins aggregates in airways. Mutated CFTR promotes transglutaminases-mediated crosslinking of beclin 1, a positive regulator of autophagy, to induce accumulation of LC3-binding protein p62 and prevent autophagic degradation of aggregates.

    • Alessandro Luciani
    • , Valeria Rachela Villella
    •  & Luigi Maiuri

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