Volume 6 Issue 3, March 2004

Volume 6 Issue 3

Chromosome mal-orientations accumulate before correction by Aurora kinase. cover design: James McQuat

Editorial

Book Review

News and Views

  • News & Views |

    Delivery of transmembrane proteins to the lumen of the lysosome is mediated by their ubiquitination, and subsequent recognition and sorting at the endosome. A new group of ubiquitin-binding proteins has now been identified that seem to function in the delivery of ubiquitinated cargo both from the cell surface and the trans-Golgi network (TGN) to the lysosome.

    • Markus Babst
  • News & Views |

    How do you build a sorting machine that can function with less than half of its sorting components? This problem challenges our understanding of nucleocytoplasmic transport after the finding that yeast can survive with nuclear pore complexes (NPCs) containing only half their original mass of transport-factor-binding domains.

    • Benjamin L. Timney
    •  & Michael P. Rout
  • News & Views |

    Lipid rafts are thought to be important for signalling cascades by compartmentalizing signalling components in the membrane. This view has recently come under fire because the common method used for isolation of rafts — detergent extraction — is fraught with artefacts. A variety of techniques, including FRET, have been used recently to investigate rafts in their native environment in intact cells. Now, FRET analysis provides evidence that rafts may not have a role in T-cell activation after all.

    • Susan K. Pierce
  • News & Views |

    The remarkable fidelity of chromosome segregation during mitosis and meiosis is critical for preventing birth defects and diseases. The Aurora protein kinases prevent defects in segregation by correcting mistakes in chromosome attachment to the spindle before cells divide.

    • Sue Biggins
  • News & Views |

    New studies indicate that an Aplysia californica variant of the translational regulator CPEB exhibits prion-like properties, enabling the protein to establish a stable, self-perpetuating and synapse-specific enhancement of neurotransmission. These studies suggest that a radically new kind of signalling — an autocatalytic change in protein conformation — is involved in maintaining long-term memories.

    • Jonathan M. Levenson
    •  & J. David Sweatt

Technical Report

Articles

Letters