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J Leukoc Biol. 2018 Aug;104(2):323-331. doi: 10.1002/JLB.2MR1217-503R. Epub 2018 May 2.

Remodeling our concept of chemokine receptor function: From monomers to oligomers.

Author information

1
Department of Cell Signaling, Centro Andaluz de Biología Molecular y Medicina Regenerativa (CABIMER-CSIC), Seville, Spain.
2
Department of Immunology and Oncology, Centro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain.
3
Department of Molecular Microbiology and Infection Biology, Centro de Investigaciones Biológicas (CIB/CSIC), Madrid, Spain.

Abstract

The chemokines direct leukocyte recruitment in both homeostatic and inflammatory conditions, and are therefore critical for immune reactions. By binding to members of the class A G protein-coupled receptors, the chemokines play an essential role in numerous physiological and pathological processes. In the last quarter century, the field has accumulated much information regarding the implications of these molecules in different immune processes, as well as mechanistic insight into the signaling events activated through their binding to their receptors. Here, we will focus on chemokine receptors and how new methodological approaches have underscored the role of their conformations in chemokine functions. Advances in biophysical-based techniques show that chemokines and their receptors act in very complex networks and therefore should not be considered isolated entities. In this regard, the chemokine receptors can form homo- and heterodimers as well as oligomers at the cell surface. These findings are changing our view as to how chemokines influence cell biology, identify partners that regulate chemokine function, and open new avenues for therapeutic intervention.

KEYWORDS:

cell signaling; chemokine receptors; imaging-based approaches; receptor conformations

PMID:
29719064
DOI:
10.1002/JLB.2MR1217-503R

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