Förster Resonance Energy Transfer (FRET) Microscopy for Monitoring Biomolecular Interactions
Förster or Fluorescence resonance energy transfer (FRET) can be used to detect protein-protein interactions. When combined with microscopy, FRET has high temporal and spatial resolution, allowing the interaction dynamics of proteins within specific subcellular compartments to be detected in cells. FRET microscopy has become a powerful technique to assay the direct binding interaction of two proteins in vivo. Here, we describe a sensitized emission method to determine the presence and dynamics of protein-protein interactions in living cells.
Key wordsFluorescence FRET Sensitized emission Dynamics Microscopy Live cell imaging
The authors thank Dr. Claire E. Atkinson for critical reading of the manuscript. This work was supported by NIH grant 1RO1CA142858 awarded to A.I.M. and NIH grant 1R21AR066920 awarded to A.L.M.