SNMP is a signaling component required for pheromone sensitivity in
 Drosophila

Jin, Xin; Ha, Taejin; Smith, Dean P.

doi:10.1073/pnas.0803309105

Cited by 263 publications

(300 citation statements)

References 38 publications

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“…The effect of indole on the structure of OBP4 correlates well with our previous findings for the Drosophila OBP LUSH, where binding of ligand induces a significant conformational ordering that is required to regulate its interactions with other components of the olfactory signaling cascade including sensory neuron membrane protein (26,53,57,58). Conformational heterogeneity has been observed in several other OBPs (14,17,59,60) and is most often associated with residues that regulate access to the ligand binding pocket.…”

Section: Discussionsupporting

confidence: 70%

New Insights into the Mechanism of Odorant Detection by the Malaria-transmitting Mosquito Anopheles gambiae

Davrazou

Dong

Murphy

et al. 2011

Journal of Biological Chemistry

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Anopheles gambiae mosquitoes that transmit Plasmodium falciparum malaria use a series of olfactory cues present in human sweat to locate their hosts for a blood meal. Recognition of these odor cues occurs through the interplay of odorant receptors and odorant-binding proteins (OBPs) that bind to odorant molecules and transport and present them to the receptors. Recent studies have implicated potential heterodimeric interactions between two OBPs, OBP1 and OBP4, as important for perception of indole by the mosquito (Biessmann, H., Andronopoulou, E., Biessmann, M. R., Douris, V., Dimitratos, S. D., Eliopoulos, E., Guerin, P. M., Iatrou, K., Justice, R. W., Kröber, T., Marinotti, O., Tsitoura, P., Woods, D. F., and Walter, M. F. (2010) PLoS ONE 5, e9471; Qiao, H., He, X., Schymura, D., Ban, L., Field, L., Dani, F. R., Michelucci, E., Caputo, B., della Torre, A., Iatrou, K., Zhou, J. J., Krieger, J., and Pelosi, P. (2011) Cell. Mol. Life Sci. 68, 1799 -1813). Here we present the 2.0 Å crystal structure of the OBP4-indole complex, which adopts a classical odorant-binding protein fold, with indole bound at one end of a central hydrophobic cavity. Solution-based NMR studies reveal that OBP4 exists in a molten globule state and binding of indole induces a dramatic conformational shift to a well ordered structure, and this leads to the formation of the binding site for OBP1. Analysis of the OBP4-OBP1 interaction reveals a network of contacts between residues in the OBP1 binding site and the core of the protein and suggests how the interaction of the two proteins can alter the binding affinity for ligands. These studies provide evidence that conformational ordering plays a key role in regulating heteromeric interactions between OBPs.Anopheles gambiae mosquitoes are the primary vectors for malaria caused by Plasmodium falciparum and have an extremely high preference for feeding on human hosts (1, 2) and are attracted to odor molecules from incubated human sweat and other skin emanations (3-6). Disrupting the normal olfactory responses to these odors presents an attractive tool to combat transmission of malaria and other mosquito borne diseases, and a number of efforts are now under way to discover novel reagents for this purpose.In insects the detection of odorants occurs primarily in the olfactory sensilla and involves the interplay of membranebound olfactory receptors (7) and odorant-binding proteins (OBPs), 3 which are expressed into the lymph fluid that surrounds the olfactory dendrites (8) where they can reach concentrations in the millimolar range (9, 10). OBPs have multiple roles including protecting odors from degradation and transporting them to the olfactory receptors (11, 12). There is evidence that OBPs have two primary roles in odorant perception. In the first model a number of groups have proposed that OBPs act as passive carriers for the odorant, and pH changes in the vicinity of the dendritic membrane lead to conformational changes that stimulate ligand release, freeing the ligand to activate the receptor (1...

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Section: Discussionsupporting

confidence: 70%

New Insights into the Mechanism of Odorant Detection by the Malaria-transmitting Mosquito Anopheles gambiae

Davrazou

Dong

Murphy

et al. 2011

Journal of Biological Chemistry

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“…dATP8B mutants were identified in a screen for cVA defective mutants (1). The wild-type strain used in this study was w 1118 .…”

Section: Methodsmentioning

confidence: 99%

“…1 A-C) (1)(2)(3). Approximately half of the Or67d neurons from these four lines were insensitive to all concentrations of cVA, and those that did respond had severely impaired cVA sensitivity compared with wild-type controls ( Fig.…”

mentioning

confidence: 99%

Lipid flippase modulates olfactory receptor expression and odorant sensitivity in Drosophila

Xia

Zhang

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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In Drosophila melanogaster, the male-specific pheromone cVA (11-cis-vaccenyl acetate) functions as a sex-specific social cue. However, our understanding of the molecular mechanisms underlying cVA pheromone transduction and its regulation are incomplete. Using a genetic screen combined with an electrophysiological assay to monitor pheromone-evoked activity in the cVA-sensing Or67d neurons, we identified an olfactory sensitivity factor encoded by the dATP8B gene, the Drosophila homolog of mammalian ATP8B. dATP8B is expressed in all olfactory neurons that express Orco, the odorant receptor coreceptor, and the odorant responses in most Orco-expressing neurons are reduced. Or67d neurons are severely affected, with strongly impaired cVA-induced responses and lacking spontaneous spiking in the mutants. The dATP8B locus encodes a member of the P4-type ATPase family thought to flip aminophospholipids such as phosphatidylserine and phosphatidylethanolamine from one membrane leaflet to the other. dATP8B protein is concentrated in the cilia of olfactory neuron dendrites, the site of odorant transduction. Focusing on Or67d neuron function, we show that Or67d receptors are mislocalized in dATP8B mutants and that cVA responses can be restored to dATP8B mutants by misexpressing a wild-type dATP8B rescuing transgene, by expressing a vertebrate P4-type ATPase member in the pheromone-sensing neurons or by overexpressing Or67d receptor subunits. These findings reveal an unexpected role for lipid translocation in olfactory receptor expression and sensitivity to volatile odorants.olfaction | aminophospholipid translocase

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“…1 to 3). There is a family of membrane proteins in insects called sensory neuron membrane proteins (SNMPs) that have similar structural features to CD36 (3,11). Of these, SNMP-1 is believed to facilitate the detection of pheromones via a G-protein coupled receptor expressed by the sensory neurons (7).…”

Section: The Effect Of Onx On Kodia-pc Perception In Micementioning

confidence: 99%

A role of CD36 in the perception of an oxidised phospholipid species in mice

et al. 2015

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CD36 is a broadly expressed transmembrane protein that engages multiple ligands, including polar lipids. This protein is thought to even contribute to the chemosensory detection of long-chain fatty acids in the oral cavity of rodents. In this study, we assessed whether animals consciously perceive a ligand of CD36, 1-(palmitoyl)-2-(5-keto-6-octanedioyl)phosphatidylcholine (KOdiA-PC), and if so, whether CD36 is involved in sensing the oxidised phospholipid species. We found that mice avoided or hesitated to ingest fluids containing KOdiA-PC, suggesting a conscious perception of the lipid in the animals. We assessed the involvement and role of CD36 in the KOdiA-PC perception by comparing the behavioural responses of wild-type and CD36-deficient mice to the test fluids, and provided evidence that the protein could play a role in sensing a lower level of the lipid. We also found that transection of the olfactory nerve of wild-type mice resulted in an inability to perceive KOdiA-PC, suggesting the significance of olfactory system in the lipid sensing. Our findings, coupled with the recent finding of CD36 expression in the mouse olfactory epithelium, led us to predict that the site of CD36 action in the KOdiA-PC sensing plausibly lies within the nasal cavity of the animal.Animals have highly developed chemosensory systems that enable efficient detection of diverse soluble or volatile molecules. Detection of exogenous molecules by taste bud cells and/or olfactory receptor cells transmits signals to the brain and consequently induces various behavioural responses (e.g., appetitive or aversive response to foods) (21, 25). To better understand the mechanisms underlying chemosensory perception, much effort has gone into identifying sensory proteins in the oral and nasal cavities (4, 5). CD36 is a broadly expressed transmembrane protein associated with the recognition of multiple molecules (e.g., amphipathic lipids) (15,19). For instance, in macrophages, CD36 contributes to the clearance of oxidised forms of low-density lipoprotein from the blood by recognising distinct phospholipid species on the surface of the particles (6,20). Furthermore, CD36 expressed by enterocytes is believed to participate in not only recognition and absorption of long-chain fatty acids but also in formation of chylomicrons (18). In addition to its well-characterized functions, CD36 has been postulated to play an important role in the chemosensory detection of longchain fatty acids in the oral cavity, leading to an appetitive response to the lipid species in rodents. Several lines of evidence support this finding: CD36 is localised to the apical surface of taste bud cells in

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SNMP is a signaling component required for pheromone sensitivity in Drosophila

Cited by 263 publications

References 38 publications

New Insights into the Mechanism of Odorant Detection by the Malaria-transmitting Mosquito Anopheles gambiae

New Insights into the Mechanism of Odorant Detection by the Malaria-transmitting Mosquito Anopheles gambiae

Lipid flippase modulates olfactory receptor expression and odorant sensitivity in Drosophila

<b>A role of CD36 in the perception of an oxidised phospholipid species in </b><b>mice </b>

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