@article{GomezDiaz2016-06-15ectod-35498,
  year={2016},
  doi={10.1038/ncomms11866},
  title={A CD36 ectodomain mediates insect pheromone detection via a putative tunnelling mechanism},
  volume={7},
  journal={Nature Communications},
  author={Gomez-Diaz, Carolina and Bargeton, Benoîte and Abuin, Liliane and Bukar, Natalia and Reina, Jaime H. and Bartoi, Tudor and Graf, Marion and Ong, Huy and Ulbrich, Maximilian H. and Benton, Richard},
  note={Article Number: 11866}
}

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    <dc:contributor>Abuin, Liliane</dc:contributor>
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    <dcterms:title>A CD36 ectodomain mediates insect pheromone detection via a putative tunnelling mechanism</dcterms:title>
    <dc:creator>Abuin, Liliane</dc:creator>
    <dc:contributor>Reina, Jaime H.</dc:contributor>
    <dcterms:abstract xml:lang="eng">CD36 transmembrane proteins have diverse roles in lipid uptake, cell adhesion and pathogen sensing. Despite numerous in vitro studies, how they act in native cellular contexts is poorly understood. A Drosophila CD36 homologue, sensory neuron membrane protein 1 (SNMP1), was previously shown to facilitate detection of lipid-derived pheromones by their cognate receptors in olfactory cilia. Here we investigate how SNMP1 functions in vivo. Structure-activity dissection demonstrates that SNMP1's ectodomain is essential, but intracellular and transmembrane domains dispensable, for cilia localization and pheromone-evoked responses. SNMP1 can be substituted by mammalian CD36, whose ectodomain can interact with insect pheromones. Homology modelling, using the mammalian LIMP-2 structure as template, reveals a putative tunnel in the SNMP1 ectodomain that is sufficiently large to accommodate pheromone molecules. Amino-acid substitutions predicted to block this tunnel diminish pheromone sensitivity. We propose a model in which SNMP1 funnels hydrophobic pheromones from the extracellular fluid to integral membrane receptors.</dcterms:abstract>
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