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Differential activity and selectivity of N‐terminal modified CXCL12 chemokines at the CXCR4 and ACKR3 receptors

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Jaracz-Ros, Agnieszka | Bernadat, Guillaume | Cutolo, Pasquale | Gallego, Carmen | Gustavsson, Martin | Cecon, Erika | Baleux, Françoise | Kufareva, Irina | Handel, Tracy, M | Bachelerie, Françoise | Levoye, Angélique

Edité par CCSD ; Society for Leukocyte Biology -

International audience. Chemokines play critical roles in numerous physiological and pathological processes through their action on seven-transmembrane (TM) receptors. The N-terminal domain of chemokines, which is a key determinant of signaling via its binding within a pocket formed by receptors' TM helices, can be the target of proteolytic processing. An illustrative case of this regulatory mechanism is the natural processing of CXCL12 that generates chemokine variants lacking the first two N-terminal residues. While such truncated variants behave as antagonists of CXCR4, the canonical G proteincoupled receptor of CXCL12, they are agonists of the atypical chemokine receptor 3 (ACKR3/

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