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. 2022 Nov 22;9:1060555. doi: 10.3389/fmolb.2022.1060555

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Copyright © 2022 Vacchini, Maffioli, Di Silvestre, Cancellieri, Milanesi, Nonnis, Badanai, Mauri, Negri, Locati, Tedeschi and Borroni.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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CCL3L1-induced phosphoproteome in ACKR2- and CCR5-expressing cells. (A–B) Number of distinct and shared phosphosites (A) and phosphoproteins (B) after ACKR2 and CCR5 short-term (T3) or extended activation (T30) activation with 100 nM CCL3L1. (C) Kinetics of up (black) and down (white) regulated phosphosites after ACKR2 (circle) and CCR5 (square) activation with 100 nM CCL3L1. (D–E) Kinetics of up and downregulated phosphoproteins after ACKR2 (D) and CCR5 (E) activation with 100 nM CCL3L1, distinct for kinases (white), phosphatases (black), and GTPase/ATPases activity (grey). (F–H) Candidate kinases (F) identified by sequence motif analysis in ACKR2 and CCR5 regulated phosphosites are shown as absolute counts of related phosphorylation sequence motifs at T3 (G) and T30 (H) time points. (I–L) ACKR2/CCR5 ratio of the percentage of phosphorylation sequence motif counts attributed to candidate kinases active at T3 (I) and T30 (L) time points after stimulation with 100 nM CCL3L1.