P2Y receptors modulate ion channel function through interactions involving the C-terminal domain.

@article{Lee2003P2YRM,
  title={P2Y receptors modulate ion channel function through interactions involving the C-terminal domain.},
  author={Choong Hyun Lee and Samuel Carey Wolff and Robert A Nicholas and Scott M O'Grady},
  journal={Molecular pharmacology},
  year={2003},
  volume={63 4},
  pages={
          878-85
        }
}
Nucleotide stimulation of G(q)-coupled P2Y receptors expressed in Xenopus laevis oocytes produces the activation of an endogenous voltage-gated ion channel, previously identified as the transient inward (T(in)) channel. Expression of human P2Y(1), human P2Y(2), rat P2Y(6), human P2Y(11), or skate P2Y receptors in oocytes resulted in modulation of the voltage dependence and inactivation gating of the channel. Expression of the human P2Y(4) receptor, rat M(1)-muscarinic receptor, and human B(1… CONTINUE READING

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