Volume 7 Issue 10, October 2006

From The Editors

Research Highlights


  • Review Article |

    The ARP2/3 complex regulates the initiation of actin polymerization and the organization of filaments into y-branched networks. Recent studies have begun to reveal the role of this complex in diverse cellular processes and its molecular mechanisms of action, as well as its misregulation during disease.

    • Erin D. Goley
    •  & Matthew D. Welch
  • Review Article |

    Recent studies of the early secretory pathway have analysed cargo selection and transport-carrier formation by components of the endoplasmic-reticulum-associated coat protein complex-II (COPII). Results are indicative of a unifying model of cage and coat function in vesicle and tubule formation as well as fission in endomembrane traffic.

    • Cemal Gürkan
    • , Scott M. Stagg
    • , Paul LaPointe
    •  & William E. Balch
  • Review Article |

    Processive DNA polymerases that replicate chromosomes interact with a ring-shaped clamp that encircles DNA and slides along the duplex. The sliding clamp is loaded onto DNA by a clamp-loader complex. Structural and biochemical studies have provided mechanistic insights into the clamp-loading process.

    • Chiara Indiani
    •  & Mike O'Donnell
  • Review Article |

    The study of muscular dystrophies has shown that mutant proteins result in perturbations of many cellular components. These findings have revealed important insights for cell biologists, and have also identified unexpected and exciting new approaches for therapy.

    • Kay E Davies
    •  & Kristen J Nowak



  • Innovation |

    Recently, a method was developed to encode unnatural amino acids genetically in bacteria, yeast and mammalian cells. This provides a powerful tool for exploring protein structure and function in vitro and in vivo, and for generating proteins with new or enhanced properties.

    • Jianming Xie
    •  & Peter G. Schultz
  • Opinion

  • Opinion |

    The SUN-domain family of nuclear envelope proteins interacts with KASH-domain proteins, which are also nuclear envelope proteins, to form 'bridges' across the inner and outer nuclear membranes. SUN-domain proteins are now proposed to provide a mechanical connection between the nucleoskeleton and the cytoskeleton.

    • Yonatan B. Tzur
    • , Katherine L. Wilson
    •  & Yosef Gruenbaum