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Remodeling our concept of chemokine receptor function: From monomers to oligomers
Author(s) -
MartínezMuñoz Laura,
Villares Ricardo,
RodríguezFernández José Luis,
RodríguezFrade José Miguel,
Mellado Mario
Publication year - 2018
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.2mr1217-503r
Subject(s) - chemokine receptor , chemokine , biology , ccr3 , ccr1 , microbiology and biotechnology , receptor , ccr10 , cxc chemokine receptors , immune system , neuroscience , immunology , biochemistry
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.

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