A CD36 ectodomain mediates insect pheromone detection via a putative tunnelling mechanism

Carolina Gomez-Diaz, Benoîte Bargeton, Liliane Abuin, Natalia Bukar, Jaime H. Reina, Tudor Bartoi, Marion Graf, Huy Ong, Maximilian H. Ulbrich, Jean-Francois Masson and Richard Benton ()
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Carolina Gomez-Diaz: Center for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne
Benoîte Bargeton: Center for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne
Liliane Abuin: Center for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne
Natalia Bukar: Centre for Self-Assembled Chemical Structures (CSACS), McGill University
Jaime H. Reina: Center for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne
Tudor Bartoi: BIOSS Centre for Biological Signalling Studies, University of Freiburg
Marion Graf: Center for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne
Huy Ong: Faculty of Pharmacy, Université de Montréal
Maximilian H. Ulbrich: BIOSS Centre for Biological Signalling Studies, University of Freiburg
Jean-Francois Masson: Centre for Self-Assembled Chemical Structures (CSACS), McGill University
Richard Benton: Center for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne

Nature Communications, 2016, vol. 7, issue 1, 1-17

Abstract: Abstract 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.

Date: 2016
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DOI: 10.1038/ncomms11866

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