4.7 Review

Lighting up multiprotein complexes: lessons from GPCR oligomerization

Journal

TRENDS IN BIOTECHNOLOGY
Volume 28, Issue 8, Pages 407-415

Publisher

ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibtech.2010.05.002

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Funding

  1. Ministerio de Ciencia e Innovacion [SAF2008-01462, CSD2008-00005]
  2. National Institutes of Health [DK087688]

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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.

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