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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Gomez-Diaz C,Bargeton B,Abuin L,Bukar N,Reina JH,Bartoi T,Graf M,Ong H,Ulbrich MH,Masson JF,Benton Rdoi
10.1038/ncomms11866subject
Has Abstractpub_date
2016-06-15 00:00:00pages
11866issn
2041-1723pii
ncomms11866journal_volume
7pub_type
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