Use of Resonance Energy Transfer Techniques for In Vivo Detection of Chemokine Receptor Oligomerization

Methods Mol Biol. 2016;1407:341-59. doi: 10.1007/978-1-4939-3480-5_24.


Since the first reports on chemokine function, much information has been generated on the implications of these molecules in numerous physiological and pathological processes, as well as on the signaling events activated through their binding to receptors. As is the case for other G protein-coupled receptors, chemokine receptors are not isolated entities that are activated following ligand binding; rather, they are found as dimers and/or higher order oligomers at the cell surface, even in the absence of ligands. These complexes form platforms that can be modified by receptor expression and ligand levels, indicating that they are dynamic structures. The analysis of the conformations adopted by these receptors at the membrane and their dynamics is thus crucial for a complete understanding of the function of the chemokines. We focus here on the methodology insights of new techniques, such as those based on resonance energy transfer for the analysis of chemokine receptor conformations in living cells.

Keywords: BRET; BiFC; Chemokines; FRET; GPCR; Oligomerization; SRET.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bioluminescence Resonance Energy Transfer Techniques*
  • Chemokines / metabolism
  • Fluorescence Resonance Energy Transfer* / methods
  • Gene Expression
  • HEK293 Cells
  • Humans
  • Luminescent Proteins / genetics
  • Luminescent Proteins / metabolism
  • Protein Binding
  • Protein Multimerization*
  • Receptors, Chemokine / chemistry
  • Receptors, Chemokine / metabolism*
  • Receptors, G-Protein-Coupled / metabolism
  • Signal Transduction


  • Chemokines
  • Luminescent Proteins
  • Receptors, Chemokine
  • Receptors, G-Protein-Coupled