Lighting up multiprotein complexes: lessons from GPCR oligomerization

Trends Biotechnol. 2010 Aug;28(8):407-15. doi: 10.1016/j.tibtech.2010.05.002. Epub 2010 Jun 9.


Spatiotemporal characterization of protein-protein interactions (PPIs) is essential in determining the molecular mechanisms of intracellular signaling processes. In this review, we discuss how new methodological strategies derived from non-invasive fluorescence- and luminescence-based approaches (FRET, BRET, BiFC and BiLC), when applied to the study of G protein-coupled receptor (GPCR) oligomerization, can be used to detect specific PPIs in live cells. These technologies alone or in concert with complementary methods (SRET, BRET or BiFC, and SNAP-tag or TR-FRET) can be extremely powerful approaches for PPI visualization, even between more than two proteins. Here we provide a comprehensive update on all the biotechnological aspects, including the strengths and weaknesses, of new fluorescence- and luminescence-based methodologies, with a specific focus on their application for studying PPIs.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cytological Techniques
  • Fluorescence Resonance Energy Transfer
  • Humans
  • Luminescent Measurements / methods*
  • Multiprotein Complexes / chemistry*
  • Protein Binding
  • Protein Interaction Mapping / methods*
  • Receptors, G-Protein-Coupled / chemistry*


  • Multiprotein Complexes
  • Receptors, G-Protein-Coupled