Volume 14 Issue 10, October 2013

Volume 14 Issue 10

'Quality Control' by Vicky Summersby, inspired by this Focus issue.

Research Highlights



  • Review Article |

    Disruption of the protein quality control system can lead to protein misfolding, inactivity and aggregation. New structural and biochemical insights into how disaggregases collaborate with co-chaperones and utilize ATP to untangle these aggregates are now being gained. This is clinically relevant, as aggregation is often linked to common neurodegenerative diseases.

    • Shannon M. Doyle
    • , Olivier Genest
    •  & Sue Wickner
  • Review Article |

    Chaperones are heavy-duty molecular machines that assist nascent proteins to reach their native fold but also mediate unfolding and prevent the accumulation of toxic protein aggregates. There is an increasing structural understanding of how they might perform such large-scale rearrangements.

    • Helen Saibil
  • Review Article |

    The addition or removal of poly(A) tails from the 3′ ends of eukaryotic RNAs is a key regulator of RNA stability and, consequently, of gene expression. Recent work has revealed that RNA turnover is also controlled by the addition of oligo(U) tails.

    • Chris J. Norbury
  • Review Article |

    Damage signalling in response to DNA double-strand breaks is under tight negative regulation. These control mechanisms, which include post-translational modifications and changes in chromatin structure, ensure that pathways are spatially and temporally regulated and that they become inactivated when repair is complete.

    • Stephanie Panier
    •  & Daniel Durocher


  • Review Article |

    Nuclear factor-κB (NF-κB) signalling is tightly regulated through ubiquitylation and phosphorylation of its components. Integral to this post-translational regulation is the polyubiquitin-binding protein NF-κB essential modulator (NEMO), which controls the modification of numerous NF-κB signalling proteins, such as the canonical IκB kinase (IKKs) and IKK-related kinases.

    • Kristopher Clark
    • , Sambit Nanda
    •  & Philip Cohen



  • Opinion |

    Structural and mechanistic studies have revealed common features of the way in which RNA and proteins are prepared for degradation by the exosome and proteasome, respectively. By extrapolating from what has been learnt about the proteasome, we may gain increased understanding of how its RNA counterpart, the exosome, is assembled and controlled.

    • Debora L. Makino
    • , Felix Halbach
    •  & Elena Conti