Dataset related to article "CCR5 and ACKR2 show distinct constitutive and agonist-induced signaling properties"

This record contains raw data related to article "CCR5 and ACKR2 show distinct constitutive and agonist-induced signaling properties" ACKR2 is an atypical chemokine receptor structurally uncoupled from G proteins and unable to activate those signaling pathways used by conventional chemokine receptors to promote cell migration. Nevertheless, ACKR2 regulates inflammation and immune responses by shaping chemokine gradients in tissues by means scavenging inflammatory chemokines. To investigate the signaling pathways downstream ACKR2, a quantitative SILAC-based phosphoproteomic analysis was carried out in an inducible cell model expressing ACKR2 or its conventional counterpart CCR5, stimulated or not with the common agonist CCL3L1. A comparative analysis of the phosphoproteomes revealed unique constitutive and agonist-dependent phosphorylation signatures. ACKR2-responsive phosphosites were enriched for pathways involving mTOR signaling networks, which resulted unrelated to receptor scavenger properties. In conclusion, mapping of phosphorylation events indicated that conventional and atypical chemokine receptors differ for both constitutive and agonist-dependent signaling properties, and revealed that ACKR2 expression influences the mTOR pathway, suggesting its potential role in the regulation of cell metabolism