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A potential cost of evolving epibatidine resistance in poison frogs.

Julia M YorkCecilia M BorgheseAndrew A GeorgeDavid C CannatellaHarold H Zakon
Published in: bioRxiv : the preprint server for biology (2023)
While S108C protects these species against sequestered epibatidine, it incurs a potential physiological cost of disrupted α4β2 nAChR function. These results may explain the high conservation of a serine at this site in vertebrates, as well as provide an example of a tradeoff between beneficial and deleterious effects of an evolutionary change. They also provide important clues for future work on assembly and trafficking of this important neurotransmitter receptor.
Keyphrases
  • human health
  • genome wide
  • current status
  • risk assessment
  • binding protein
  • climate change
  • protein kinase