Volume 11 Issue 11, November 2010

From The Editors

Research Highlights

Progress

  • Progress |

    Transport protein particle (TRAPP; also known as trafficking protein particle) complexes activate the GTPase Ypt1 or RAB1 to regulate membrane traffic in yeast and mammals, respectively. Two different TRAPP complexes tether coated vesicles during endoplasmic reticulum–Golgi and intra-Golgi traffic, respectively, and a third complex functions in autophagy. The TRAPP complexes thereby connect GTPase activation to unique membrane-tethering events.

    • Jemima Barrowman
    • , Deepali Bhandari
    • , Karin Reinisch
    •  & Susan Ferro-Novick

Reviews

  • Review Article |

    Organisms can anticipate environmental changes owing to an intrinsic molecular clock. Our molecular understanding of circadian oscillators has advanced over the past decade with the deployment of systems biology approaches, enabling a multiscale view of circadian systems from the molecular level to the intact organism.

    • Eric E. Zhang
    •  & Steve A. Kay
  • Review Article |

    The aggregation of misfolded proteins is associated with the perturbation of cellular function and ageing. However, protein aggregation can also be a regulated process that deposits aggregates at specific cellular sites. This is protective as it facilitates aggregate solubilization, refolding and degradation by the protein quality-control network.

    • Jens Tyedmers
    • , Axel Mogk
    •  & Bernd Bukau
  • Review Article |

    Proteomes are typically analyzed by mass spectrometry, and recent advances have greatly increased the fraction of the proteome that can be identified and quantified in a single study. Mapping complete proteomes and using such maps for targeted quantitative proteomics will increase the impact of proteomics on biological and clinical research.

    • Christian H. Ahrens
    • , Erich Brunner
    • , Ermir Qeli
    • , Konrad Basler
    •  & Ruedi Aebersold
  • Review Article |

    Focal adhesion kinase (FAK) is a scaffold and tyrosine kinase protein that binds to itself and cellular partners through its four-point-one, ezrin, radixin, moesin (FERM) domain. Recent structural work reveals how regulatory proteins activate FAK by binding to its FERM domain, enabling it to coordinate diverse cellular responses.

    • Margaret C. Frame
    • , Hitesh Patel
    • , Bryan Serrels
    • , Daniel Lietha
    •  & Michael J. Eck