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J Biol Chem, Vol. 274, Issue 44, 31515-31523, October 29, 1999
From the Howard Hughes Medical Institute, Departments of Cell
Biology and Medicine, Divisions of Gastroenterology and Cardiology,
Duke University Medical Center, Durham, North Carolina 27710
The endocytic pathway of the secretin receptor, a
class II GPCR, is unknown. Some class I G protein-coupled receptors
(GPCRs), such as the
Properties of Secretin Receptor Internalization Differ from
Those of the
2-Adrenergic Receptor
2-adrenergic receptor
(2-AR), internalize in clathrin-coated vesicles and this
process is mediated by G protein-coupled receptor kinases (GRKs),
-arrestin, and dynamin. However, other class I GPCRs, for example,
the angiotensin II type 1A receptor (AT1AR), exhibit
different internalization properties than the 2-AR. The secretin receptor, a class II GPCR, is a GRK substrate, suggesting that
like the 2-AR, it may internalize via a -arrestin and
dynamin directed process. In this paper we characterize the
internalization of a wild-type and carboxyl-terminal (COOH-terminal)
truncated secretin receptor using flow cytometry and fluorescence
imaging, and compare the properties of secretin receptor
internalization to that of the 2-AR. In HEK 293 cells,
sequestration of both the wild-type and COOH-terminal truncated
secretin receptors was unaffected by GRK phosphorylation, whereas
inhibition of cAMP-dependent protein kinase mediated
phosphorylation markedly decreased sequestration. Addition of secretin
to cells resulted in a rapid translocation of -arrestin to plasma
membrane localized receptors; however, secretin receptor
internalization was not reduced by expression of dominant negative
-arrestin. Thus, like the AT1AR, secretin receptor
internalization is not inhibited by reagents that interfere with
clathrin-coated vesicle-mediated internalization and in accordance with
these results, we show that secretin and AT1A receptors
colocalize in endocytic vesicles. This study demonstrates that the
ability of secretin receptor to undergo GRK phosphorylation and
-arrestin binding is not sufficient to facilitate or mediate its
internalization. These results suggest that other receptors may undergo
endocytosis by mechanisms used by the secretin and AT1A
receptors and that kinases other than GRKs may play a greater role in
GPCR endocytosis than previously appreciated.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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