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Vol. 59, Issue 2, 239-247, February 2001
-Arrestin- and Dynamin-Dependent Endocytosis of the
AT1 Angiotensin Receptor
Department of Physiology, Semmelweis University Medical School,
Budapest, Hungary (Z.G., M.S., L.S., B.B., L.H.); Department of
Molecular Pathology, Joint Research Organization of the Semmelweis
University and the Hungarian Academy of Sciences, Budapest, Hungary
(S.P.); Endocrinology and Reproduction Research Branch, National
Institute of Child Health and Human Development, National Institutes of
Health, Bethesda, Maryland (K.J.C.); and Departments of Endocrinology,
St. Bartholomew's and the Royal London School of Medicine and
Dentistry, West Smithfield, London, United Kingdom
(A.J.L.C.)
The major mechanism of agonist-induced internalization of G
protein-coupled receptors (GPCRs) is 
-arrestin- and
dynamin-dependent endocytosis via clathrin-coated vesicles. However,
recent reports have suggested that some GPCRs, exemplified by the
AT1 angiotensin receptor expressed in human embryonic
kidney (HEK) 293 cells, are internalized by a -arrestin- and
dynamin-independent mechanism, and possibly via a clathrin-independent
pathway. In this study, agonist-induced endocytosis of the rat
AT1A receptor expressed in Chinese hamster ovary (CHO)
cells was abolished by clathrin depletion during treatment with
hyperosmotic sucrose and was unaffected by inhibition of endocytosis
via caveolae with filipin. In addition, internalized
fluorescein-conjugated angiotensin II appeared in endosomes, as
demonstrated by colocalization with transferrin. Overexpression of
-arrestin1(V53D) and -arrestin1(1-349) exerted dominant negative
inhibitory effects on the endocytosis of radioiodinated angiotensin
II in CHO cells. GTPase-deficient (K44A) mutant forms of dynamin-1 and
dynamin-2, and a pleckstrin homology domain-mutant (K535A) dynamin-2
with impaired phosphoinositide binding, also inhibited the endocytosis
of AT1 receptors in CHO cells. Similar results were
obtained in COS-7 and HEK 293 cells. Confocal microscopy using
fluorescein-conjugated angiotensin II showed that overexpression of
dynamin-1(K44A) and dynamin-2(K44A) isoforms likewise inhibited agonist-induced AT1 receptor endocytosis in CHO cells.
Studies on the angiotensin II concentration-dependence of
AT1 receptor endocytosis showed that at higher agonist
concentrations its rate constant was reduced and the inhibitory effects
of dominant negative dynamin constructs were abolished. These data
demonstrate the importance of -arrestin- and dynamin-dependent
endocytosis of the AT1 receptor via clathrin-coated
vesicles at physiological angiotensin II concentrations.
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