Endocytosis of G protein-coupled receptors: roles of G protein-coupled receptor kinases and ß-arrestin proteins
Abstract
Sequestration of G protein-coupled receptors from the cell surface is a commonly observed phenomenon following agonist-stimulation. This process is now believed to be important for receptor resensitization as well as for signal transduction. Over the years, numerous studies have aimed at understanding the molecular mechanisms underlying internalization. Proteins such as the G protein-coupled receptor kinases (GRKs) and the beta-arrestins, which were initially characterized as desensitizing molecules, have been shown to be important regulators of the endocytic process. Recently, numerous interacting partners have been identified for each of these two classes of proteins. However, the details regarding the sequence of these interactions and the cross-talk between signaling pathways containing the different protein complexes are just beginning to be uncovered. In this review, we summarize these findings and discuss the role of GRKs and beta-arrestins, two families of key regulatory proteins that regulate G protein-coupled receptor endocytosis.
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Activation of receptors promotes posttranslational modification of ion channels and recruitment of mediators including ubiquitin ligases and β-arrestins, which are key components of ion channel endocytosis.
“In brief, the activation of receptors promotes the posttranslational modification (PTM) of IChs and recruitment of mediators including ubiquitin ligases and β-arrestins, which are the key components of ion channel endocytosis [92,93].”
From Insights of Endocytosis Signaling in Health and Disease (2023) · cites this paper as [93]
Cites
Oakley, R. H., Laporte, S. A., Holt, J. A., Barak, L. S., & Caron, M. G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101450200 · Cited by 455 · see citing works
A serine cluster prevents recycling of the V2 vasopressin receptor
Innamorati, G., Sadeghi, H. M., Tran, N. T., & Birnbaumer, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2222 · Cited by 127 · see citing works
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Beaulieu, J.-M., & Gainetdinov, R. R. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.002642 · Cited by 2,763 · see citing works
Hunyady, L., & Catt, K. J. (2006) · Molecular Endocrinology · doi:10.1210/me.2004-0536 · Cited by 541 · see citing works
Control of aldosterone secretion: a model for convergence in cellular signaling pathways
SPÄT, A., & HUNYADY, L. (2004) · Physiological Reviews · doi:10.1152/physrev.00030.2003 · Cited by 494 · see citing works
Role of β-Adrenoceptor Signaling in Skeletal Muscle: Implications for Muscle Wasting and Disease
Lynch, G. S., & Ryall, J. G. (2008) · Physiological Reviews · doi:10.1152/physrev.00028.2007 · Cited by 410 · see citing works
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Chen, W., ten Berge, D., Brown, J., Ahn, S., Hu, L. A., Miller, W. E., Caron, M. G., Barak, L. S., Nusse, R., & Lefkowitz, R. J. (2003) · Science · doi:10.1126/science.1082808 · Cited by 334 · see citing works
Lorton, D., & Bellinger, D. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16035635 · Cited by 221 · see citing works
Opioids in gastroenterology: treating adverse effects and creating therapeutic benefits
Camilleri, M., Lembo, A., & Katzka, D. A. (2017) · Clinical Gastroenterology and Hepatology · doi:10.1016/j.cgh.2017.05.014 · Cited by 176 · see citing works
Similarities between the Hedgehog and Wnt signaling pathways
Kalderon, D. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(02)02388-7 · Cited by 141 · see citing works
Wu, G., Zhao, G., & He, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305707200 · Cited by 103 · see citing works
Insights of Endocytosis Signaling in Health and Disease
Pathak, C., Vaidya, F. U., Waghela, B. N., Jaiswara, P. K., Gupta, V. K., Kumar, A., Rajendran, B. K., & Ranjan, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032971 · Cited by 59 · see citing works
“In brief, the activation of receptors promotes the posttranslational modification (PTM) of IChs and recruitment of mediators including ubiquitin ligases and β-arrestins, which are the key components of ion channel endocytosis [92,93].”
BackgroundG-protein-coupled receptor controls steroid hormone signaling in cell membrane
Wang, D., Zhao, W.-L., Cai, M.-J., Wang, J.-X., & Zhao, X.-F. (2015) · Scientific Reports · doi:10.1038/srep08675 · Cited by 35 · see citing works
- Authors
- Claing, A.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Claing, A
- ORCID
- Claing, A
- Venue
- Progress in Neurobiology
- Publisher
- Elsevier BV
- Published
- 2002-02
- Volume
- 66
- Issue
- 2
- Pages
- 61-79
- ISSN
- 0301-0082 (ISSN-L)
- OpenAlex
- W2038594983
- Cited by
- 519
- References
- 2
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 10 · 2023: 5 · 2022: 11 · 2021: 6 · 2020: 9 · 2019: 16 · 2018: 8 · 2017: 18 · 2016: 19 · 2015: 23 · 2014: 17 · 2013: 17 · 2012: 8
- FWCI
- 17.68
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Progress in Neurobiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- G protein-coupled receptors, receptor internalization, endocytosis, G protein-coupled receptor kinases, beta-arrestin, receptor desensitization, receptor resensitization, signal transduction, signaling crosstalk, protein-protein interaction
- MeSH terms
- beta-Arrestins, Animals, Endocytosis, Humans, Receptors, Cell Surface, Signal Transduction, GTP-Binding Proteins, Arrestins, Receptor Protein-Tyrosine Kinases
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