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Cellular trafficking of G protein-coupled receptor/beta-arrestin endocytic complexes.

Publication ,  Journal Article
Zhang, J; Barak, LS; Anborgh, PH; Laporte, SA; Caron, MG; Ferguson, SS
Published in: J Biol Chem
April 16, 1999

beta-Arrestins are multifunctional proteins identified on the basis of their ability to bind and uncouple G protein-coupled receptors (GPCR) from heterotrimeric G proteins. In addition, beta-arrestins play a central role in mediating GPCR endocytosis, a key regulatory step in receptor resensitization. In this study, we visualize the intracellular trafficking of beta-arrestin2 in response to activation of several distinct GPCRs including the beta2-adrenergic receptor (beta2AR), angiotensin II type 1A receptor (AT1AR), dopamine D1A receptor (D1AR), endothelin type A receptor (ETAR), and neurotensin receptor (NTR). Our results reveal that in response to beta2AR activation, beta-arrestin2 translocation to the plasma membrane shares the same pharmacological profile as described for receptor activation and sequestration, consistent with a role for beta-arrestin as the agonist-driven switch initiating receptor endocytosis. Whereas redistributed beta-arrestins are confined to the periphery of cells and do not traffic along with activated beta2AR, D1AR, and ETAR in endocytic vesicles, activation of AT1AR and NTR triggers a clear time-dependent redistribution of beta-arrestins to intracellular vesicular compartments where they colocalize with internalized receptors. Activation of a chimeric AT1AR with the beta2AR carboxyl-terminal tail results in a beta-arrestin membrane localization pattern similar to that observed in response to beta2AR activation. In contrast, the corresponding chimeric beta2AR with the AT1AR carboxyl-terminal tail gains the ability to translocate beta-arrestin to intracellular vesicles. These results demonstrate that the cellular trafficking of beta-arrestin proteins is differentially regulated by the activation of distinct GPCRs. Furthermore, they suggest that the carboxyl-tail of the receptors might be involved in determining the stability of receptor/betaarrestin complexes and cellular distribution of beta-arrestins.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

April 16, 1999

Volume

274

Issue

16

Start / End Page

10999 / 11006

Location

United States

Related Subject Headings

  • beta-Arrestins
  • Recombinant Fusion Proteins
  • Receptors, Cell Surface
  • Luminescent Proteins
  • Humans
  • Green Fluorescent Proteins
  • GTP-Binding Proteins
  • Endocytosis
  • Cell Line
  • Biochemistry & Molecular Biology
 

Citation

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Zhang, J., Barak, L. S., Anborgh, P. H., Laporte, S. A., Caron, M. G., & Ferguson, S. S. (1999). Cellular trafficking of G protein-coupled receptor/beta-arrestin endocytic complexes. J Biol Chem, 274(16), 10999–11006. https://doi.org/10.1074/jbc.274.16.10999
Zhang, J., L. S. Barak, P. H. Anborgh, S. A. Laporte, M. G. Caron, and S. S. Ferguson. “Cellular trafficking of G protein-coupled receptor/beta-arrestin endocytic complexes.J Biol Chem 274, no. 16 (April 16, 1999): 10999–6. https://doi.org/10.1074/jbc.274.16.10999.
Zhang J, Barak LS, Anborgh PH, Laporte SA, Caron MG, Ferguson SS. Cellular trafficking of G protein-coupled receptor/beta-arrestin endocytic complexes. J Biol Chem. 1999 Apr 16;274(16):10999–1006.
Zhang, J., et al. “Cellular trafficking of G protein-coupled receptor/beta-arrestin endocytic complexes.J Biol Chem, vol. 274, no. 16, Apr. 1999, pp. 10999–1006. Pubmed, doi:10.1074/jbc.274.16.10999.
Zhang J, Barak LS, Anborgh PH, Laporte SA, Caron MG, Ferguson SS. Cellular trafficking of G protein-coupled receptor/beta-arrestin endocytic complexes. J Biol Chem. 1999 Apr 16;274(16):10999–11006.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

April 16, 1999

Volume

274

Issue

16

Start / End Page

10999 / 11006

Location

United States

Related Subject Headings

  • beta-Arrestins
  • Recombinant Fusion Proteins
  • Receptors, Cell Surface
  • Luminescent Proteins
  • Humans
  • Green Fluorescent Proteins
  • GTP-Binding Proteins
  • Endocytosis
  • Cell Line
  • Biochemistry & Molecular Biology