Slamming the DOR on chemokine receptor signaling: heterodimerization silences ligand-occupied CXCR4 and delta-opioid receptors
- PMID: 18203136
- DOI: 10.1002/eji.200738101
Slamming the DOR on chemokine receptor signaling: heterodimerization silences ligand-occupied CXCR4 and delta-opioid receptors
Abstract
Dimerization has emerged as a common mechanism for regulating the function of G protein-coupled receptors (GPCR). Among these are chemokine receptors, which detect various chemokines and regulate a range of physiological process, including immune cell trafficking, cancer cell migration, and neuronal patterning. Homo- and heterodimerization in response to chemokine binding has been shown to be required for the initiation or alteration of signaling by a number of chemokine receptors. In this issue of the European Journal of Immunology, a new study indicates that the formation of heterodimers of chemokine receptor CXCR4 and the delta-opioid receptor (DOR) prevents each of them from actively signaling, suggesting a novel mechanism for silencing GPCR function.
Comment on
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Ligand stabilization of CXCR4/delta-opioid receptor heterodimers reveals a mechanism for immune response regulation.Eur J Immunol. 2008 Feb;38(2):537-49. doi: 10.1002/eji.200737630. Eur J Immunol. 2008. PMID: 18200497
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