[HTML][HTML] Carboxyl-terminal splicing of the rat μ opioid receptor modulates agonist-mediated internalization and receptor resensitization
T Koch, S Schulz, H Schro, R Wolf, E Raulf… - Journal of Biological …, 1998 - ASBMB
The rat μ 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 μ receptor agonist [d-Ala 2, N-Me-
Phe 4,-Gly-ol 5] 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 h) but resensitized at a faster rate …
which differ in length and amino acid composition at the carboxyl terminus. When stably
expressed in HEK 293 cells, both splice variants bind the μ receptor agonist [d-Ala 2, N-Me-
Phe 4,-Gly-ol 5] 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 h) but resensitized at a faster rate …