CXCR7 heterodimerizes with CXCR4 and regulates CXCL12-mediated G protein signaling.

By A. Levoye, K. Balabanian, F. Baleux, F. Bachelerie, B. Lagane. Blood, 2009

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International Union of Basic and Clinical Pharmacology. LXXXIX. Update on the Extended Family of Chemokine Receptors and Introducing a New Nomenclature for Atypical Chemokine Receptors (2014, neutral): “…of CXCR4 and ACKR3, which seems to depend on the expression levels of both receptors, indicates a negative cooperative effect of ACKR3 on CXCR4-G protein coupling (Levoye et al., 2009) and a shift in biased signaling toward the arrestin axis (Rajagopal et al., 2010; Decaillot et al., 2011).”
HMGB1 promotes recruitment of inflammatory cells to damaged tissues by forming a complex with CXCL12 and signaling via CXCR4 (2012, methodology): “In accordance with previous FRET studies (Percherancier et al., 2005; Levoye et al., 2009), we observed that addition of CXCL12 increased the maximal FRET signal, whereas the FRET 50 value was not significantly affected.”
CXCL12/CXCR4/CXCR7 Chemokine Axis and Cancer Progression (2010, background): “Another role for the receptor is that it may serve as a co-receptor for CXCR4 [59, 60] and enhance CXCL12mediate G-protein signaling [59], as the two receptors form heterodimers in the context of overexpression in transiently transfected cells.”