The DOI matches its Crossref record; 76 of the 76 references it cites were found in a registry or an index.
The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals
Open accessAbstract
β-arrestins are versatile adapter proteins that form complexes with most G-protein-coupled receptors (GPCRs) following agonist binding and phosphorylation of receptors by G-protein-coupled receptor kinases (GRKs). They play a central role in the interrelated processes of homologous desensitization and GPCR sequestration, which lead to the termination of G protein activation. β-arrestin binding to GPCRs both uncouples receptors from heterotrimeric G proteins and targets them to clathrin-coated pits for endocytosis. Recent data suggest that β-arrestins also function as GPCR signal transducers. They can form complexes with several signaling proteins,including Src family tyrosine kinases and components of the ERK1/2 and JNK3 MAP kinase cascades. By recruiting these kinases to agonist-occupied GPCRs,β-arrestins confer distinct signaling activities upon the receptor.β-arrestin-Src complexes have been proposed to modulate GPCR endocytosis,to trigger ERK1/2 activation and to mediate neutrophil degranulation. By acting as scaffolds for the ERK1/2 and JNK3 cascades, β-arrestins both facilitate GPCR-stimulated MAP kinase activation and target active MAP kinases to specific locations within the cell. Thus, their binding to GPCRs might initiate a second wave of signaling and represent a novel mechanism of GPCR signal transduction.
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Cites
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Conformational biosensors reveal GPCR signalling from endosomes
Irannejad, R., Tomshine, J. C., Tomshine, J. R., Chevalier, M., Mahoney, J. P., Steyaert, J., Rasmussen, S. G. F., Sunahara, R. K., El-Samad, H., Huang, B., et al. (2013) · Nature · doi:10.1038/nature12000 · Cited by 819
Metadata
- Authors
- Luttrell, L. M., & Lefkowitz, R. J.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2002-02-01
- Volume
- 115
- Issue
- 3
- Pages
- 455-465
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W1933410007
- Cited by
- 1,122
- References
- 76
- FWCI
- 21.81
- Type
- journal article
- Language
- en
- Open access
- green
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