期刊
JOURNAL OF IMMUNOLOGY
卷 183, 期 11, 页码 7337-7346出版社
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.0901802
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资金
- European Union [LSHB-CT-2005-518167, LSHG-CT-2003-503259]
- Spanish Ministry of Science and Innovation [SAF2005-03388, SAF2008-02175]
- Madrid Regional Government [CCG07-CSIC/SAL-1904]
- Redes tematicas de Investigacion Cooperativa Sanitaria Program [RD08/0075 RIER]
Although homo- and heterodimerization are reported for some chemokine receptors, it remains unclear whether these functional states are in dynamic equilibrium and how receptor/ligand levels influence oligomerization. In human neutrophils and in cell lines that coexpress the chemokine receptors CXCR1 and CXCR2, we used fluorescence resonance energy transfer techniques to show that these two receptors form homo- and heterodimers. Receptor expression and ligand activation were found to regulate the balance between these complexes, adapting the response to changes in the milieu. CXCL8, a ligand for both receptors, alters heterodimeric complexes, whereas it stabilizes homodimers and promotes receptor internalization. Oligomerization of receptors, together with the regulation of their expression and desensitization, could thus contribute to the fine control of chemokine functions. The Journal of Immunology, 2009, 183: 7337-7346.
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