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J Biol Chem, Vol. 273, Issue 22, 13652-13657, May 29, 1998
From the Department of Pharmacology and Toxicology,
Otto-von-Guericke University, 39120 Magdeburg, Germany
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-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 h) but resensitized at a faster rate than MOR1 during agonist
withdrawal (20 min). Immunocytochemical analysis revealed that
DAMGO-induced internalization of MOR1B proceeded much faster than that
of MOR1 followed by rapid recycling of the receptor to the cell
surface. In addition, the greater resistance of MOR1B to homologous
desensitization compared with MOR1 as well as MOR1B resensitization was
abolished when receptor reactivation/recycling was blocked with
monensin, an inhibitor of endosomal acidification. It is concluded that
the sequence at the cytoplasmic tail of MOR1B facilitates
clathrin-coated vesicle-mediated endocytosis which, in turn, promotes
accelerated receptor reactivation. Taken together, our findings suggest
that carboxyl-terminal splicing of the rat µ opioid receptor
modulates agonist-induced internalization and receptor
resensitization.
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