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Accessory protein determines whether pheromones are detected


Pheromones are like the molecules you taste as you chomp on a greasy french fry: big and fatty. In research to be published in the October 17 advance online issue of Nature, Rockefeller University researchers reveal an unanticipated role for a new CD36-like protein to help cells detect these invisible communication signals that drive a wide range of behaviors, from recognizing a sibling to courting a mate, a finding that may explain what pheromone communication, pathogen recognition and fat taste perception all have in common.

Scientists led by Leslie Vosshall, head of the Laboratory of Neurogenetics and Behavior, have found that this protein, called SNMP, or Sensory Neuron Membrane Protein, plays an accessory, yet essential role in helping neurons detect pheromones. Although SNMP plays a specific role in insect pheromone detection, it is a member of the CD36 family of proteins, which are found on the surfaces of many cells and have diverse biological functions, ranging from fatty-acid breakdown to innate immunity.

The pheromone that Vosshall and her colleagues tested, cVA, also known as cis-vaccenyl acetate, binds to a receptor complex and induces aggregation in Drosophila melanogaster. “I think of it as a ‘party pheromone,’” says Vosshall. “If a few male flies are hanging out, other flies, male and female, will smell the cVA and tend to gather, and if the mood hits them, the males will court the females that join the group.” When Drosophila do mate, the male transfers cVA to the female and marks her as taken, making her less interesting to other males. Prior research has implicated the receptor complex in pheromone detection, but this is the first time researchers have shown that SNMP is essential for neurons to respond to these signals.

When neurons detect cVA, those that express SNMP fire very rapidly, a response not seen in neurons that lack SNMP. However, when mutants were reengineered to express the protein, this response was restored. In another experiment, when Vosshall and her colleagues presented a moth pheromone to fruit flies that expressed moth pheromone receptors instead of their own, the researchers found that the fruit flies’ neurons fired. This response also requires SNMP, suggesting that SNMP may be essential for handing off insect pheromones of all types and is probably important for pheromone reception in all insects.

Given these findings, Vosshall and her colleagues propose a unified mechanism of action for all CD36 proteins, despite their wide range of biological functions. “Our work suggests that wherever you have lipid-like molecules that need to be detected or captured by cells, these CD36 proteins appear to be necessary to grab these molecules and present them to a specific cell-surface receptor,” says Vosshall. In the case of immune recognition, a CD36 protein snatches a bacterial lipid fragment and delivers it to its receptor.

And because CD36 proteins are also found in the tongue, Vosshall suspects that they play a role in our ability to taste fatty foods, as an accessory protein that binds that big, lipid-like molecule from your french fry and presents it to the real, as yet unidentified, fat taste receptor.


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