{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kim HT"],"funding":["National Research Foundation of Korea"],"pagination":["111"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11863771"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(1)"],"pubmed_abstract":["<h4>Background</h4>The trafficking of immune cells between lymphoid organs and circulation depends on gradients of CXCL12 and sphingosine-1-phosphate (S1P), mediated through their cognate receptors C-X-C chemokine receptor type 4 (CXCR4) and S1P receptor type 1 (S1P<sub>1</sub>). S1P<sub>1</sub> facilitates the egress of hematopoietic stem cells and lymphocytes by counteracting CXCR4-mediated retention signals. However, the molecular mechanisms underlying this interplay remain poorly understood. In this study, we uncover CXCR4-S1P<sub>1</sub> heteromerization and explore their functional interactions.<h4>Methods</h4>Bimolecular fluorescence complementation (BiFC) assay, proximity ligation assay (PLA), and quantitative bioluminescence resonance energy transfer (BRET) assay were employed to "],"journal":["Cell communication and signaling : CCS"],"pubmed_title":["Regulation of CXCR4 function by S1P&lt;sub&gt;1&lt;/sub&gt; through heteromerization."],"pmcid":["PMC11863771"],"funding_grant_id":["2020R1A5A1018081"],"pubmed_authors":["Jeong JY","Huh WK","Kim HT"],"additional_accession":[]},"is_claimable":false,"name":"Regulation of CXCR4 function by S1P&lt;sub&gt;1&lt;/sub&gt; through heteromerization.","description":"<h4>Background</h4>The trafficking of immune cells between lymphoid organs and circulation depends on gradients of CXCL12 and sphingosine-1-phosphate (S1P), mediated through their cognate receptors C-X-C chemokine receptor type 4 (CXCR4) and S1P receptor type 1 (S1P<sub>1</sub>). S1P<sub>1</sub> facilitates the egress of hematopoietic stem cells and lymphocytes by counteracting CXCR4-mediated retention signals. However, the molecular mechanisms underlying this interplay remain poorly understood. In this study, we uncover CXCR4-S1P<sub>1</sub> heteromerization and explore their functional interactions.<h4>Methods</h4>Bimolecular fluorescence complementation (BiFC) assay, proximity ligation assay (PLA), and quantitative bioluminescence resonance energy transfer (BRET) assay were employed to ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2026-06-02T18:16:36.404Z","creation":"2025-04-07T11:30:18.825Z"},"accession":"S-EPMC11863771","cross_references":{"pubmed":["40012038"],"doi":["10.1186/s12964-025-02099-x"]}}