Detection of Protein‑protein Interactions by FRET and BRET Methods

Česká verzia

Authors: E. Matoulková; B. Vojtěšek
Authors place of work: Regionální centrum aplikované molekulární onkologie, Masarykův onkologický ústav, Brno
Published in the journal: Klin Onkol 2014; 27(Supplementum): 82-86

Summary

Nowadays, in vivo protein‑protein interaction studies have become preferable detecting methods that enable to show or specify (already known) protein interactions and discover their inhibitors. They also facilitate detection of protein conformational changes and discovery or specification of signaling pathways in living cells. One group of in vivo methods enabling these findings is based on fluorescent resonance energy transfer (FRET) and its bioluminescent modification (BRET). They are based on visualization of protein‑protein interactions via light or enzymatic excitation of fluorescent or bioluminescent proteins. These methods allow not only protein localization within the cell or its organelles (or small animals) but they also allow us to quantify fluorescent signals and to discover weak or strong interaction partners. In this review, we explain the principles of FRET and BRET, their applications in the characterization of protein‑protein interactions and we describe several findings using these two methods that clarify molecular and cellular mechanisms and signals related to cancer biology.

Key words:
FRET – BRET – imaging methods – protein‑protein interaction in vivo

This work was supported by the Czech Science Foundation projects P206/12/G151 and 13--00956S, by the European Regional Development Fund and the State Budget of the Czech Republic (RECAMO, CZ.1.05/2.1.00/03.0101) and by MH CZ – DRO (MMCI, 00209805).

The authors declare they have no potential conflicts of interest concerning drugs, products, or services used in the study.

The Editorial Board declares that the manuscript met the ICMJE “uniform requirements” for biomedical papers.

Submitted:
20. 1. 2014

Accepted:
31. 3. 2014

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