Plant Molecular Biology

, Volume 50, Issue 6, pp 871–883

Imaging protein-protein interactions in living cells


  • Mark A. Hink
    • MicroSpectroscopy CentreWageningen University
  • Ton Bisseling
    • MicroSpectroscopy CentreWageningen University
  • Antonie J.W.G. Visser
    • MicroSpectroscopy CentreWageningen University
    • Department of Structural Biology, Faculty of Earth and Life SciencesVrije Universiteit

DOI: 10.1023/A:1021282619035

Cite this article as:
Hink, M.A., Bisseling, T. & Visser, A.J. Plant Mol Biol (2002) 50: 871. doi:10.1023/A:1021282619035


The complex organization of plant cells makes it likely that the molecular behaviour of proteins in the test tube and the cell is different. For this reason, it is essential though a challenge to study proteins in their natural environment. Several innovative microspectroscopic approaches provide such possibilities, combining the high spatial resolution of microscopy with spectroscopic techniques to obtain information about the dynamical behaviour of molecules. Methods to visualize interaction can be based on FRET (fluorescence detected resonance energy transfer), for example in fluorescence lifetime imaging microscopy (FLIM). Another method is based on fluorescence correlation spectroscopy (FCS) by which the diffusion rate of single molecules can be determined, giving insight into whether a protein is part of a larger complex or not. Here, both FRET- and FCS-based approaches to study protein-protein interactions in vivo are reviewed.

cellsFCSfluorescence spectroscopyFRETprotein-protein interactions

Copyright information

© Kluwer Academic Publishers 2002