| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 276, Issue 20, 17442-17447, May 18, 2001
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Department of Psychiatry and Department of Cellular and
Molecular Pharmacology, Program in Cell Biology, University of
California, San Francisco, California 94143-0984 and
§ Department of Anesthesiology, University of California,
Los Angeles, California 90024
We have observed an unexpected type of
nonreciprocal "cross-regulation" of the agonist-induced endocytosis
of G protein-coupled receptors by clathrin-coated pits.
Isoproterenol-dependent internalization of
Heterologous Inhibition of G Protein-coupled Receptor Endocytosis
Mediated by Receptor-specific Trafficking of
-Arrestins*
,
2-adrenergic receptors in stably transfected
HEK293 cells was specifically blocked (>65% inhibition) by
vasopressin-induced activation of V2 vasopressin receptors co-expressed
at similar levels. In contrast, activation of 2
receptors caused no detectable effect on V2 receptor internalization in
the same cells. Several pieces of evidence suggest that this
nonreciprocal inhibition of endocytosis is mediated by
receptor-specific intracellular trafficking of -arrestins. First,
previous studies showed that the activation of V2 but not
2 receptors caused pronounced recruitment of
-arrestins to endocytic membranes (Oakley, R. H., Laporte, S. A., Holt, J. A., Barak, L. S., and Caron, M. G. (1999) J. Biol. Chem. 274, 32248-32257). Second,
overexpression of arrestin 2 or 3 (-arrestin 1 or 2) abolished the
V2 receptor-mediated inhibition of 2 receptor
internalization. Third, mutations of the V2 receptor that block
endomembrane recruitment of -arrestins eliminated the V2
receptor-dependent blockade of 2 receptor
internalization. These results identify a novel type of heterologous
regulation of G protein-coupled receptors, define a new functional role
of receptor-specific intracellular trafficking of -arrestins, and suggest an experimental method to rapidly modulate the functional activity of -arrestins in intact cells.
*
These studies were supported by research grants from the
National Institutes of Health.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported during part of these studies by a postdoctoral
fellowship from the American Heart Association. To whom correspondence should be addressed: Advanced Medicine, Inc., Dept. of Biochemistry, 901 Gateway Blvd., South San Francisco, CA 94080. Tel.: 650-808-6088; Fax: 313-557-2727; E-mail: uklein@advmedicine.com.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  M.-J. Rabiet, E. Huet, and F. Boulay Complement Component 5a Receptor Oligomerization and Homologous Receptor Down-regulation J. Biol. Chem., November 7, 2008; 283(45): 31038 - 31046. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 E.-N. N'Diaye, A. C. Hanyaloglu, K. K. Kajihara, M. A. Puthenveedu, P. Wu, M. von Zastrow, and E. J. Brown The Ubiquitin-like Protein PLIC-2 Is a Negative Regulator of G Protein-coupled Receptor Endocytosis Mol. Biol. Cell, March 1, 2008; 19(3): 1252 - 1260. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Breit, K. Gagnidze, L. A. Devi, M. Lagace, and M. Bouvier Simultaneous Activation of the {delta} Opioid Receptor ({delta}OR)/Sensory Neuron-Specific Receptor-4 (SNSR-4) Hetero-Oligomer by the Mixed Bivalent Agonist Bovine Adrenal Medulla Peptide 22 Activates SNSR-4 but Inhibits {delta}OR Signaling Mol. Pharmacol., August 1, 2006; 70(2): 686 - 696. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. T. Cao, A. Brelot, and M. von Zastrow The Composition of the {beta}-2 Adrenergic Receptor Oligomer Affects Its Membrane Trafficking after Ligand-Induced Endocytosis Mol. Pharmacol., January 1, 2005; 67(1): 288 - 297. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Breit, M. Lagace, and M. Bouvier Hetero-oligomerization between {beta}2- and {beta}3-Adrenergic Receptors Generates a {beta}-Adrenergic Signaling Unit with Distinct Functional Properties J. Biol. Chem., July 2, 2004; 279(27): 28756 - 28765. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Terrillon, C. Barberis, and M. Bouvier Heterodimerization of V1a and V2 vasopressin receptors determines the interaction with {beta}-arrestin and their trafficking patterns PNAS, February 10, 2004; 101(6): 1548 - 1553. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 F. Schmidlin, D. Roosterman, and N. W. Bunnett The third intracellular loop and carboxyl tail of neurokinin 1 and 3 receptors determine interactions with {beta}-arrestins Am J Physiol Cell Physiol, October 1, 2003; 285(4): C945 - C958. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. Schmidlin, O. Dery, N. W. Bunnett, and E. F. Grady Heterologous regulation of trafficking and signaling of G protein-coupled receptors: beta -Arrestin-dependent interactions between neurokinin receptors PNAS, March 5, 2002; 99(5): 3324 - 3329. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
