Fluorescent protein FRET: the good, the bad and the ugly

Trends Biochem Sci. 2007 Sep;32(9):407-14. doi: 10.1016/j.tibs.2007.08.003. Epub 2007 Aug 30.

Abstract

Dynamic protein interactions play a significant part in many cellular processes. A technique that shows considerable promise in elucidating such interactions is Förster resonance energy transfer (FRET). When combined with multiple, colored fluorescent proteins, FRET permits high spatial resolution assays of protein-protein interactions in living cells. Because FRET signals are usually small, however, their measurement requires careful interpretation and several control experiments. Nevertheless, the use of FRET in cell biological experiments has exploded over the past few years. Here we describe the physical basis of FRET and the fluorescent proteins appropriate for these experiments. We also review the approaches that can be used to measure FRET, with particular emphasis on the potential artifacts associated with each approach.

Publication types

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

MeSH terms

  • Animals
  • Fluorescence Polarization
  • Fluorescence Resonance Energy Transfer*
  • Humans
  • Luminescent Proteins / metabolism*
  • Protein Folding

Substances

  • Luminescent Proteins