Fiche du document
2016
- doi: 10.1038/ncomms11866
- issn: 2041-1723
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/doi/10.1038/ncomms11866
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pmid/27302750
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/eissn/2041-1723
Ce document est lié à :
info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_51184EB367277
info:eu-repo/semantics/openAccess , Copying allowed only for non-profit organizations , https://serval.unil.ch/disclaimer
Sujets proches
Proteids Modelmaking Modelling Model-making Molding (Clay, plaster, etc.) Clay modeling Modelling Analysis (Mathematics) Interstitial fluid Pattern Model Adherence, Cell Cell adherenceCiter ce document
C. Gomez-Diaz et al., « A CD36 ectodomain mediates insect pheromone detection via a putative tunnelling mechanism. », Serveur académique Lausannois, ID : 10.1038/ncomms11866
Métriques
Partage / Export
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.