Slamming the DOR on chemokine receptor signaling: heterodimerization silences ligand-occupied CXCR4 and delta-opioid receptors.
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.
Hereld
Dale
D
Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, NIH, Rockville, MD 20852, USA.
Jin
Tian
T
D000818:Animals; D019281:Dimerization; D006801:Humans; D008024:Ligands; D019718:Receptors, CXCR4 / Q000037:antagonists & inhibitors* / Q000096:biosynthesis / Q000378:metabolism* / Q000502:physiology; D017465:Receptors, Opioid, delta / Q000037:antagonists & inhibitors* / Q000096:biosynthesis / Q000378:metabolism* / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology*
D008024:Ligands; D019718:Receptors, CXCR4; D017465:Receptors, Opioid, delta