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Vol. 59, Issue 4, 758-764, April 2001
-Arrestins with the
Intracellular Domains of Different Opioid Receptors
Shanghai Institute of Cell Biology, Shanghai Institutes for
Biological Sciences, Chinese Academy of Sciences,
Shanghai (B.C., Y.X., G.P.); and National Laboratory of Medical
Neurobiology, Medical Center of Fudan University, Shanghai, People's
Republic of China (L.M.)
-arrestins have been shown to play important roles in regulation of
signaling and desensitization of opioid receptors in many in vivo
studies. The current study was carried out to measure the direct
interaction of -arrestins with two functional intracellular domains,
the third intracellular loop (I3L) and the carboxyl terminus (CT), of
-, µ-, and 
-opioid receptors (DOR, MOR, and KOR, respectively). Results from the pull-down assay using glutathione
S-transferase fusion proteins demonstrated that
-arrestins (1 and 2) were able to bind to the I3L of DOR and to the
CT of DOR and KOR. Surface plasmon resonance measurement gave similar
results with typical dissociation equilibrium constant
(KD) values in the micromolar range. The
site-directed mutagenesis experiment further revealed that certain
specific serine/threonine residues in these receptor domains play a
critical role in their interaction with -arrestins. Taken together,
our data clearly indicated that -arrestins interact differentially
with the functional domains of different opioid receptors; this may
provide a possible molecular basis for differential regulation of
opioid receptors by -arrestins.
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