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Vol. 59, Issue 6, 1395-1401, June 2001
Departments of Anesthesiology (D.B.-P., G.I., H.M.S., M.B.) and
Physiology (M.B.), Molecular Biology Institute (M.B.), University of
California Los Angeles School of Medicine, Los Angeles, California
Arrestins have been shown to facilitate the recruitment of G
protein-coupled receptors to the clathrin-coated vesicles that mediate
their internalization. After
8Arg-vasopressin-induced internalization, the human
V2 vasopressin receptor failed to recycle to the cell surface, whereas
the vasopressin type 1a receptor (V1a) subtype did. The possibility
that the lack of recycling could identify a novel role for arrestins
was investigated by examining the effect of coexpressing wild-type and
dominant negative arrestins on the recycling of wild-type and mutant V2 and V1a receptors. Coexpression of the V1a or V2 receptors with the
last 100 amino acids of arrestin reduced significantly their internalization, whereas coexpression of wild-type and mutant arrestins
had diverse effects on internalization. Arrestin3 but not arrestin2
increased the internalization of the V1aR without altering its
recycling pattern. Both nonvisual arrestins enhanced vasopressin type 2 receptor (V2R) internalization, inducing the appearance of a pool of
recycling receptor in addition to the nonrecycling pool. The effect of
arrestins on the internalization of the chimeric V1a/V2 receptor and
its reciprocal chimera was specified by the identity of the
carboxyl-terminal segment. The S363A mutation that confers recycling to
the V2R did not alter its interaction with arrestins. Truncation of the
carboxyl-terminal segment of the V2R impaired ligand-induced
internalization that could be fully restored by wild-type arrestins.
Internalization of the V2 and V1a receptors required dynamin GTPase activity.
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