ArticleCellular and molecular life sciences : CMLS2026
Physical interaction with Ephrin B1 promotes CXCR4 intracellular localization and oncogenic potential.
Article in Cellular and molecular life sciences : CMLS, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Chemokine receptor 4 (CXCR4) is a member of the chemokine receptor family, exclusively activated by the chemokine CXCL12. While CXCR4 regulates numerous physiological processes associated with cell migration and embryogenesis, its overexpression has been involved in various cancer types. Studies suggest that intracellular CXCR4 rather than CXCL12-induced signaling at the plasma membrane contributes to its pro-tumorigenic functions. Given the role of GPCR-interacting proteins in their trafficking and subcellular localization, we characterized the CXCR4 interactome using an affinity purification coupled to mass spectrometry (AP-MS) strategy. The most abundant protein identified in the CXCR4 interactome is Ephrin B1, a member of the Ephrin protein family that shares several functions with CXCR4, such as the regulation of cell migration and proliferation. Further studies showed that the interaction between CXCR4 and Ephrin B1 is direct and enhanced upon CXCR4 activation by CXCL12. They also indicated that Ephrin B1 prevents CXCR4 N-glycosylation, decreases CXCR4 cell surface expression, and consistently inhibits CXCL12-induced CXCR4 coupling to G
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