Chaperones are proteins that assist in protein folding and multi-protein complex assembly co-translationally or post-translationally. Generally, a single chaperone has multiple client proteins. An example of chaperones are heat shock proteins, which are upregulated in response to heat – a risk factor for protein misfolding and aggregation.

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  • 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
    Nature Cell Biology 23, 1053-1055
  • 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
    Nature Cell Biology 22, 911-912
  • News & Views |

    The second Keystone Symposium on AAA+ proteins, “AAA+ Proteins: From Atomic Structures to Organisms”, was held in Tahoe City, USA in January 2020. The program highlighted recent advances from structural, biochemical and cellular approaches that have extended our understanding of these important ATP-driven molecular machines.

    • Steven E. Glynn
    • , Julia R. Kardon
    •  & Carol Cho