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Volume 3 Issue 10, October 2001

Confocal sections through Drosophila egg chambers. Clones of capulet are negatively marked with green fluorescent protein. Actin is shown in red and Enabled is shown in blue. Cover design: Lawrence Keogh

Volume 3 Issue 10

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Article

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Brief Communication

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Editorial

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Commentary

  • Missense mutations in the genes coding for presenilin 1 and presenilin 2 cause familial Alzheimer's disease — a progressive neurodegenerative disorder of the central nervous system. Loss-of-function mutations of these genes in Drosophila, Caenorhabditis elegans and mice cause severe lethal phenotypes, which implicates the presenilins genetically in the Notch signalling pathway. The hypothesis that presenilins are aspartyl proteases that cleave the amyloid precursor protein and Notch can explain the phenotypes. Direct evidence for this hypothesis is, however, difficult to obtain. Moreover, presenilin 1 is a multifunctional protein, as exemplified by its role in the Wnt/β-catenin signalling pathway.

    • Bart De Strooper
    • Wim Annaert
    Commentary
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News & Views

  • Cytoskeletal attachment to the cell cortex is crucial for mechanical and signalling events at the plasma membrane. The adenomatous polyposis coli (APC) protein, as well as β-catenin in a complex with cytoplasmic dynein, is implicated in mediating such cortical attachment.

    • Viki Allan
    • Inke S. Näthke
    News & Views

  • Signalling pathways controlling developmental cell fate rely on a variety of carbohydrate-based protein modifications, including glycosylation of cell-surface and extracellular-matrix proteins. Receptors themselves might be glycosylated during synthesis and secretory trafficking, regulating their subsequent signalling activities. Two recent reports have uncovered a shared requirement for nucleotide–sugar transport in these processes, underscoring the importance of carbohydrates in developmental patterning.

    • Mark E. Fortini
    News & Views

  • Inhibitory neurotransmission by γ-aminobutyric acid (GABA) is regulated by the number and subcellular localization of GABAA receptors in the membrane of the target neuron. A new study suggests that the ubiquitin-like protein Plic-1 stabilizes intracellular GABAA receptors and promotes their accumulation in the plasma membrane.

    • Bernhard Lüscher
    • Cheryl A. Keller
    News & Views
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Book Review

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Review Article

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