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    Olfactory receptor signaling is regulated by the post-synaptic density 95, Drosophila discs large, zona-occludens 1 (PDZ) scaffold multi-PDZ domain protein 1.

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    Authors
    Dooley, Ruth
    Baumgart, Sabrina
    Rasche, Sebastian
    Hatt, Hanns
    Neuhaus, Eva M
    Affiliation
    Molecular Medicine Lab RCSI, Beaumont Hospital, Dublin, Republic of Ireland.
    Issue Date
    2009-12
    MeSH
    Animals
    Calcium Signaling
    Carrier Proteins
    Humans
    Mice
    Olfactory Receptor Neurons
    PDZ Domains
    Protein Transport
    Receptors, Odorant
    Signal Transduction
    
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    Citation
    Olfactory receptor signaling is regulated by the post-synaptic density 95, Drosophila discs large, zona-occludens 1 (PDZ) scaffold multi-PDZ domain protein 1. 2009, 276 (24):7279-90 FEBS J.
    Journal
    The FEBS journal
    URI
    http://hdl.handle.net/10147/127203
    DOI
    10.1111/j.1742-4658.2009.07435.x
    PubMed ID
    19909339
    Abstract
    The unique ability of mammals to detect and discriminate between thousands of different odorant molecules is governed by the diverse array of olfactory receptors expressed by olfactory sensory neurons in the nasal epithelium. Olfactory receptors consist of seven transmembrane domain G protein-coupled receptors and comprise the largest gene superfamily in the mammalian genome. We found that approximately 30% of olfactory receptors possess a classical post-synaptic density 95, Drosophila discs large, zona-occludens 1 (PDZ) domain binding motif in their C-termini. PDZ domains have been established as sites for protein-protein interaction and play a central role in organizing diverse cell signaling assemblies. In the present study, we show that multi-PDZ domain protein 1 (MUPP1) is expressed in the apical compartment of olfactory sensory neurons. Furthermore, on heterologous co-expression with olfactory sensory neurons, MUPP1 was shown to translocate to the plasma membrane. We found direct interaction of PDZ domains 1 + 2 of MUPP1 with the C-terminus of olfactory receptors in vitro. Moreover, the odorant-elicited calcium response of OR2AG1 showed a prolonged decay in MUPP1 small interfering RNA-treated cells. We have therefore elucidated the first building blocks of the putative 'olfactosome', brought together by the scaffolding protein MUPP1, a possible central nucleator of the olfactory response.
    Item Type
    Article
    Language
    en
    ISSN
    1742-4658
    ae974a485f413a2113503eed53cd6c53
    10.1111/j.1742-4658.2009.07435.x
    Scopus Count
    Collections
    Beaumont Hospital

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