Bimolecular fluorescence complementation

Navarro, G., Carriba, P., Gandia, J., Ciruela, F., Casado, V., Cortes, A., Mallol, J., Canela, E.I. et al. (2008) Detection of heteromers formed by cannabinoid CBl, dopamine D2, and adenosine A2A G-protein-coupled receptors by combining bimolecular fluorescence complementation and bioluminescence energy transfer. Scientific World Journal, 8, 1088-1097. 

This system is organized in vascular plants as a 30 nm diameter plasma membrane complex, known as the rosette TC, that was first described by Mueller and Brown more than 25 years ago [42]. The rosette is composed of an estimated 36 subunits comprising at least three types of cellulose synthase A proteins. All three components have been shown to be essential for correct assembly and enzymatic activity of the complex in Arabidopsis [43, 44]. The physical interaction of these three components has recently been demonstrated by bimolecular fluorescence complementation [45]. The system also offers a beautiful example of the functional aspects of this organization, as cortical microtubules guide the movement of cellulose synthase complexes through the plasma membrane during cell wall biosynthesis [46,47],... 

Type 1 Forster (or fluorescent) resonance energy transfer (FRET)-based biosensors Type 2 Bimolecular fluorescence complementation (BiFC)-based biosensors Type 3 Single FP-based biosensors... 

Bimolecular Fluorescence Complementation (BiFC)-based biosensors... 

Bimolecular fluorescence complementation (BiFC)-based biosensors have been used to visualize a variety of protein—protein interactions in live cells. In this type of biosensor, the FP that is split up and MRE are linked to one portion and the analyte protein is linked to the other portion. When the two proteins interact, the two fragments fuse together, refolding properly into its three-dimensional structure and producing a fluorescence signal. 

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