Volatile pheromone signalling in Drosophila

Research output: Contribution to journalReview article

8 Scopus citations

Abstract

Once captured by the antenna, the male-specific pheromone 11-cis vaccenyl acetate (cVA) binds to an extracellular binding protein called LUSH that undergoes a conformational shift upon cVA binding. The stable LUSH-cVA complex is the activating ligand for pheromone receptors present on the dendrites of the aT1 neurones, comprising the only class of neurones that detect volatile cVA pheromone. This mechanism can explain the single molecule sensitivity of pheromone detection. The receptor that recognizes activated LUSH consists of a complex of several proteins, including Or67d, a member of the tuning odourant receptor family, Orco, a co-receptor ion channel, and SNMP, a CD36 homologue that may be an inhibitory subunit. In addition, genetic screens and reconstitution experiments reveal additional factors that are important for pheromone detection. Identification and functional dissection of these factors in Drosophila melanogaster Meigen should permit the identification of homologous factors in pathogenic insects and agricultural pests, which, in turn, may be viable candidates for novel classes of compounds to control populations of target insect species without impacting beneficial species.

Original languageEnglish (US)
Pages (from-to)19-24
Number of pages6
JournalPhysiological Entomology
Volume37
Issue number1
DOIs
StatePublished - Mar 1 2012

Keywords

  • Behaviour
  • Odorant binding protein
  • Pheromone detection
  • Signal transduction

ASJC Scopus subject areas

  • Physiology
  • Ecology, Evolution, Behavior and Systematics
  • Insect Science

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