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

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Ressource 1Télécharger: ncomms11866.pdf (3107.18 [Ko])
Etat: Public
Version: Final published version
ID Serval
serval:BIB_51184EB36727
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
A CD36 ectodomain mediates insect pheromone detection via a putative tunnelling mechanism.
Périodique
Nature Communications
Auteur(s)
Gomez-Diaz C., Bargeton B., Abuin L., Bukar N., Reina J.H., Bartoi T., Graf M., Ong H., Ulbrich M.H., Masson J.F., Benton R.
ISSN
2041-1723 (Electronic)
ISSN-L
2041-1723
Statut éditorial
Publié
Date de publication
2016
Volume
7
Pages
11866
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: epublish
Résumé
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.
Pubmed
Web of science
Open Access
Oui
Création de la notice
07/05/2016 20:11
Dernière modification de la notice
20/08/2019 14:06
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