The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Heterodimerization of Somatostatin and Opioid Receptors Cross-modulates Phosphorylation, Internalization, and Desensitization
Open accessAbstract
Heterodimerization has been shown to modulate the ligand binding, signaling, and trafficking properties of G protein-coupled receptors. However, to what extent heterodimerization may alter agonist-induced phosphorylation and desensitization of these receptors has not been documented. We have recently shown that heterodimerization of sst(2A) and sst(3) somatostatin receptors results in inactivation of sst(3) receptor function (Pfeiffer, M., Koch, T., Schröder, H., Klutzny, M., Kirscht, S., Kreienkamp, H. J., Höllt, V., and Schulz, S. (2001) J. Biol. Chem. 276, 14027-14036). Here we examine dimerization of the sst(2A) somatostatin receptor and the mu-opioid receptor, members of closely related G protein-coupled receptor families. In coimmunoprecipitation studies using differentially epitope-tagged receptors, we provide direct evidence for heterodimerization of sst(2A) and MOR1 in human embryonic kidney 293 cells. Unlike heteromeric assembly of sst(2A) and sst(3), sst(2A)-MOR1 heterodimerization did not substantially alter the ligand binding or coupling properties of these receptors. However, exposure of the sst(2A)-MOR1 heterodimer to the sst(2A)-selective ligand L-779,976 induced phosphorylation, internalization, and desensitization of sst(2A) as well as MOR1. Similarly, exposure of the sst(2A)-MOR1 heterodimer to the mu-selective ligand [d-Ala(2),Me-Phe(4),Gly(5)-ol]enkephalin induced phosphorylation and desensitization of both MOR1 and sst(2A) but not internalization of sst(2A). Cross-phosphorylation and cross-desensitization of the sst(2A)-MOR1 heterodimer were selective; they were neither observed with the sst(2A)-sst(3) heterodimer nor with the endogenously expressed lysophosphatidic acid receptor. Heterodimerization may thus represent a novel regulatory mechanism that could either restrict or enhance phosphorylation and desensitization of G protein-coupled receptors.
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Cites
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Weckbecker, G., Lewis, I., Albert, R., Schmid, H. A., Hoyer, D., & Bruns, C. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1255 · Cited by 559
Regulation and function of somatostatin receptors
Olias, G., Viollet, C., Kusserow, H., Epelbaum, J., & Meyerhof, W. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02402.x · Cited by 318
Unidirectional Cross-Activation of GRPR by MOR1D Uncouples Itch and Analgesia Induced by Opioids
Liu, X.-Y., Liu, Z.-C., Sun, Y.-G., Ross, M., Kim, S., Tsai, F.-F., Li, Q.-F., Jeffry, J., Kim, J.-Y., Loh, H. H., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.043 · Cited by 291
G protein-coupled receptor heteromers
Gomes, I., Ayoub, M. A., Fujita, W., Jaeger, W. C., Pfleger, K. D. G., & Devi, L. A. (2016) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011613-135952 · Cited by 262
Metadata
- Authors
- Pfeiffer, M., Koch, T., Schröder, H., Laugsch, M., Höllt, V., & Schulz, S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-05
- Volume
- 277
- Issue
- 22
- Pages
- 19762-19772
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2163240506
- Cited by
- 263
- References
- 27
- FWCI
- 8.53
- Type
- journal article
- Language
- en
- Open access
- hybrid
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