• myGriffith
    • Staff portal
    • Contact Us⌄
      • Future student enquiries 1800 677 728
      • Current student enquiries 1800 154 055
      • International enquiries +61 7 3735 6425
      • General enquiries 07 3735 7111
      • Online enquiries
      • Staff phonebook
    View Item 
    •   Home
    • Griffith Research Online
    • Journal articles
    • View Item
    • Home
    • Griffith Research Online
    • Journal articles
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

  • All of Griffith Research Online
    • Communities & Collections
    • Authors
    • By Issue Date
    • Titles
  • This Collection
    • Authors
    • By Issue Date
    • Titles
  • Statistics

  • Most Popular Items
  • Statistics by Country
  • Most Popular Authors
  • Support

  • Contact us
  • FAQs
  • Admin login

  • Login
  • Doublecortin interacts with the ubiquitin protease DFFRX, which associates with microtubules in neuronal processes

    Author(s)
    Friocourt, G
    Kappeler, C
    Saillour, Y
    Fauchereau, F
    Rodriguez, MS
    Bahi, N
    Vinet, MC
    Chafey, P
    Poirier, K
    Taya, S
    Wood, SA
    Dargemont, C
    Francis, F
    Chelly, J
    Griffith University Author(s)
    Wood, Stephen A.
    Year published
    2005
    Metadata
    Show full item record
    Abstract
    Doublecortin (DCX) is a microtubule-associated protein involved in neuronal migration, which causes X-linked lissencephaly and subcortical laminar heterotopia (SCLH) when mutated. Here we show that DCX interacts with the ubiquitin-specific protease Drosophila fat facets related on X chromosome (DFFRX). This interaction was confirmed by targeted mutagenesis, colocalization, and immunoprecipitation studies. DFFRX is thought to deubiquitinate specific substrates including ߭catenin, preventing their degradation by the proteasome. Interestingly, unlike ߭catenin, no ubiquitinated forms of DCX could be detected, and indeed we show ...
    View more >
    Doublecortin (DCX) is a microtubule-associated protein involved in neuronal migration, which causes X-linked lissencephaly and subcortical laminar heterotopia (SCLH) when mutated. Here we show that DCX interacts with the ubiquitin-specific protease Drosophila fat facets related on X chromosome (DFFRX). This interaction was confirmed by targeted mutagenesis, colocalization, and immunoprecipitation studies. DFFRX is thought to deubiquitinate specific substrates including ߭catenin, preventing their degradation by the proteasome. Interestingly, unlike ߭catenin, no ubiquitinated forms of DCX could be detected, and indeed we show that DCX interacts with a novel recognition domain in DFFRX, located outside of its catalytic site. We also show that DFFRX associates with microtubules at specific subcellular compartments, including those enriched in DCX. These results thus suggest that in addition to vesicular trafficking, DCX may play a role in the regulation of cell adhesion via its interaction with DFFRX in migrating and differentiating neurons.
    View less >
    Journal Title
    Molecular and Cellular Neuroscience
    Volume
    28
    Issue
    1
    Publisher URI
    http://www.sciencedirect.com/science/journal/10447431
    DOI
    https://doi.org/10.1016/j.mcn.2004.09.005
    Subject
    Neurosciences
    Neurosciences not elsewhere classified
    Cognitive and computational psychology
    Publication URI
    http://hdl.handle.net/10072/22234
    Collection
    • Journal articles

    Footer

    Disclaimer

    • Privacy policy
    • Copyright matters
    • CRICOS Provider - 00233E
    • TEQSA: PRV12076

    Tagline

    • Gold Coast
    • Logan
    • Brisbane - Queensland, Australia
    First Peoples of Australia
    • Aboriginal
    • Torres Strait Islander