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SNAP-25 regulates spine formation through postsynaptic binding to p140Cap

Author

Listed:
  • Romana Tomasoni

    (University of Milan
    Humanitas Clinical and Research Center)

  • Daniele Repetto

    (University of Turin
    Present address: Institute of Anatomy and Molecular Neurobiology, Westfälische Wilhelms-University Münster, Münster, Germany)

  • Raffaella Morini

    (University of Milan
    Humanitas Clinical and Research Center)

  • Chiara Elia

    (University of Milan
    CNR, Institute of Neuroscience)

  • Fabrizio Gardoni

    (University of Milan)

  • Monica Di Luca

    (University of Milan)

  • Emilia Turco

    (University of Turin)

  • Paola Defilippi

    (University of Turin)

  • Michela Matteoli

    (University of Milan
    Humanitas Clinical and Research Center)

Abstract

Synaptosomal-associated protein of 25 kDa (SNAP-25) is a member of the Soluble N-ethylmaleimide-sensitive-factor attachment protein receptors (SNARE) protein family, required for exocytosis of synaptic vesicles and regulation of diverse ion channels. Here, we show that acute reduction of SNAP-25 expression leads to an immature phenotype of dendritic spines that are, consistently, less functional. Conversely, over-expression of SNAP-25 results in an increase in the density of mature, Postsynaptic Density protein 95 (PSD-95)-positive spines. The regulation of spine morphogenesis by SNAP-25 depends on the protein’s ability to bind both the plasma membrane and the adaptor protein p140Cap, a key protein regulating actin cytoskeleton and spine formation. We propose that SNAP-25 allows the organization of the molecular apparatus needed for spine formation by recruiting and stabilizing p140Cap.

Suggested Citation

  • Romana Tomasoni & Daniele Repetto & Raffaella Morini & Chiara Elia & Fabrizio Gardoni & Monica Di Luca & Emilia Turco & Paola Defilippi & Michela Matteoli, 2013. "SNAP-25 regulates spine formation through postsynaptic binding to p140Cap," Nature Communications, Nature, vol. 4(1), pages 1-13, October.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3136
    DOI: 10.1038/ncomms3136
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