serval:BIB_51184EB36727
A CD36 ectodomain mediates insect pheromone detection via a putative tunnelling mechanism.
10.1038/ncomms11866
000378683900001
27302750
Gomez-Diaz
C.
author
Bargeton
B.
author
Abuin
L.
author
Bukar
N.
author
Reina
J.H.
author
Bartoi
T.
author
Graf
M.
author
Ong
H.
author
Ulbrich
M.H.
author
Masson
J.F.
author
Benton
R.
author
article
2016
Nature Communications
2041-1723
2041-1723
journal
7
11866
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.
eng
60_published
true
Publication types: Journal Article
Publication Status: epublish
University of Lausanne
mailto:serval_help@unil.ch
http://www.unil.ch/serval
http://serval.unil.ch/disclaimer
https://serval.unil.ch/notice/serval:BIB_51184EB36727