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Slamming the DOR on chemokine receptor signaling: Heterodimerization silences ligand‐occupied CXCR4 and δ‐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 δ‐opioid receptor (DOR) prevents each of them from actively signaling, suggesting a novel mechanism for silencing GPCR function.