Carboxyl-terminal splicing of the rat mu opioid receptor modulates agonist-mediated internalization and receptor resensitization.

@article{Koch1998CarboxylterminalSO,
  title={Carboxyl-terminal splicing of the rat mu opioid receptor modulates agonist-mediated internalization and receptor resensitization.},
  author={Thomas Koch and Stefan Schulz and Helmut Schroeder and Roland Wolf and E Raulf and Volker Hoellt},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 22},
  pages={
          13652-7
        }
}
The rat mu opioid receptor is alternatively spliced into two isoforms (MOR1 and MOR1B) which differ in length and amino acid composition at the carboxyl terminus. When stably expressed in HEK 293 cells, both splice variants bind the mu receptor agonist [D-Ala2,N-Me-Phe4,-Gly-ol5]enkephalin (DAMGO) with similar affinity and exhibit functional coupling to adenylyl cyclase with similar efficiency. However, the shorter isoform, MOR1B, desensitized at a slower rate during prolonged DAMGO exposure (4… CONTINUE READING
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