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Volume 12 Issue 10, October 2005

Sec15 is a component of the exocyst complex involved in vesicle transport and localization. Sec15 recognizes vesicles associated with Rab GTPases. Quiocho and colleagues show that the C-terminal helical domain of Drosophila Sec15 interacts with Rab11 in a GTP-dependent manner, co-localizes with this Rab GTPase in specialized structures within the fly eye called rhabdomeres (cover), and is important for rhabdomere morphology. pp 879-885

Volume 12 Issue 10

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Editorial

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Meeting Report

  • RNA localization and translational control are crucial for cellular fine-tuning of gene expression in space and time. A recent meeting in Tucson, Arizona pointed out mechanisms conserved across different species and cell types that contribute to the establishment of cell polarity and cell migration. Furthermore, it is becoming increasingly clear that these post-transcriptional control processes are relevant for various diseases.

    • Ralf-Peter Jansen
    • Michael Kiebler
    Meeting Report
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News & Views

  • A bacteriophage has a mechanism for producing a family of receptor-binding proteins that rivals the immunoglobulins in diversity.

    • Kurt Drickamer
    • Maureen E Taylor
    News & Views

  • Telomeres are crucial for maintaining the integrity of the genome. Several alternative structures have been proposed for these caps, and understanding their biological significance is a matter of great interest. Probing of native telomeres now reveals that telomere end-binding proteins may control the formation of G-quadruplex DNA in vivo.

    • Peter Baumann
    News & Views

  • How are individual transmembrane helices in polytopic membrane proteins delivered from the Sec translocon into the lipid bilayer? A new study on the aquaporin-4 water channel shows that they move out of the translocon in succession but may linger nearby for an extended period of time.

    • Gunnar von Heijne
    News & Views

  • The stress-activated protein kinases PKR and GCN2 regulate protein synthesis by phosphorylating the α subunit of translation initiation factor 2. Three recent studies reveal the molecular basis for the exquisite substrate specificity of this family of kinases and address the role of interlobe flexibility in kinase activation.

    • Alan G Hinnebusch
    News & Views

  • A recent study broadens the substrate profile of the COMPASS histone methyltransferase complex to include a kinetochore component and links the lysine methylation activity of COMPASS to the process of chromosome segregation.

    • Adam Wood
    • Ali Shilatifard
    News & Views
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