Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052981 | FEBS Letters | 2006 | 5 Pages |
Abstract
Fluorescence resonance energy transfer (FRET) is a powerful technique to reveal interactions between membrane proteins in live cells. Fluorescence labeling for FRET is typically performed by fusion with fluorescent proteins (FP) with the drawbacks of a limited choice of fluorophores, an arduous control of donor–acceptor ratio and high background fluorescence arising from intracellular FPs. Here we show that these shortcomings can be overcome by using the acyl carrier protein labeling technique. FRET revealed interactions between cell-surface neurokinin-1 receptors simultaneously labeled with a controlled ratio of donors and acceptors. Moreover, using FRET the specific binding of fluorescent agonists could be monitored.
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Authors
Bruno H. Meyer, Karen L. Martinez, Jean-Manuel Segura, Pedro Pascoal, Ruud Hovius, Nathalie George, Kai Johnsson, Horst Vogel,