Comparative analysis of fluorescence resonance energy transfer (FRET) and proximity ligation assay (PLA)

Proteomics

Volumn 11, Issue 10, 2011, Pages 2063-2070

  Mocanu, Maria Magdalena ^a,b   Váradi, Tímea ^a   Szöllosi, János ^a   Nagy, Peter ^a  

^a UNIVERSITY OF DEBRECEN   (Hungary)

^b CAROL DAVILA UNIVERSITY OF MEDICINE AND PHARMACY   (Romania)

Author keywords

Cell biology; Flow cytometry; Fluorescence resonance energy transfer; Protein associations; Proximity ligation assay

Indexed keywords

OLIGONUCLEOTIDE;

ANALYTIC METHOD; ARTICLE; FLOW CYTOMETRY; FLUORESCENCE RESONANCE ENERGY TRANSFER; INTERMETHOD COMPARISON; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROXIMITY LIGATION ASSAY; QUANTITATIVE ANALYSIS; SIGNAL TRANSDUCTION;

AFFINITY LABELS; ANTIBODIES; ANTIBODIES, MONOCLONAL; CARBOCYANINES; CELL LINE, TUMOR; FLOW CYTOMETRY; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMANS; LINEAR MODELS; NONLINEAR DYNAMICS; PROTEIN INTERACTION MAPPING;

EID: 79955757195     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201100028     Document Type: Article

References (33)

1. Williamson, M. P., Sutcliffe, M. J., Protein-protein interactions. Biochem. Soc. Trans. 2010, 38, 875-878.
2. Hu, C. D., Kerppola, T. K., Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat. Biotechnol. 2003, 21, 539-545.
3. Jares-Erijman, E. A., Jovin, T. M., FRET imaging. Nat. Biotechnol. 2003, 21, 1387-1395.
4. Haustein, E., Schwille, P., Fluorescence correlation spectroscopy: novel variations of an established technique. Annu. Rev. Biophys. Biomol. Struct. 2007, 36, 151-169.
5. Digman, M. A., Dalal, R., Horwitz, A. F., Gratton, E., Mapping the number of molecules and brightness in the laser scanning microscope. Biophys. J. 2008, 94, 2320-2332.
6. Shi, Y., Huang, W., Tan, Y., Jin, X. et al., A novel proximity assay for the detection of proteins and protein complexes: quantitation of HER1 and HER2 total protein expression and homodimerization in formalin-fixed, paraffin-embedded cell lines and breast cancer tissue. Diagn. Mol. Pathol. 2009, 18, 11-21.
7. Weibrecht, I., Leuchowius, K. J., Clausson, C. M., Conze, T. et al., Proximity ligation assays: a recent addition to the proteomics toolbox. Expert. Rev. Proteomics 2010, 7, 401-409.
8. Söderberg, O., Gullberg, M., Jarvius, M., Ridderstrale, K. et al., Direct observation of individual endogenous protein complexes in situ by proximity ligation. Nat. Methods 2006, 3, 995-1000.
9. Yarden, Y., Sliwkowski, M. X., Untangling the ErbB signalling network. Nat. Rev. Mol. Cell Biol. 2001, 2, 127-137.
10. Lemmon, M. A., Ligand-induced ErbB receptor dimerization. Exp. Cell. Res. 2009, 315, 638-648.
11. Nagy, P., Claus, J., Jovin, T. M., Arndt-Jovin, D. J., Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysis. Proc. Natl. Acad. Sci. USA 2010, 107, 16524-16529.
12. Szabó, Á., Horváth, G., Szöllösi, J., Nagy, P., Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements. Biophys. J. 2008, 95, 2086-2096.
13. Clayton, A. H., Tavarnesi, M. L., Johns, T. G., Unligated epidermal growth factor receptor forms higher order oligomers within microclusters on A431 cells that are sensitive to tyrosine kinase inhibitor binding. Biochemistry 2007, 46, 4589-4597.
14. Chung, I., Akita, R., Vandlen, R., Toomre, D. et al., Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 2010, 464, 783-787.
15. Leuchowius, K. J., Weibrecht, I., Landegren, U., Gedda, L., Soderberg, O., Flow cytometric in situ proximity ligation analyses of protein interactions and post-translational modification of the epidermal growth factor receptor family. Cytometry A 2009, 75, 833-839.
16. Szentesi, G., Horváth, G., Bori, I., Vámosi, G. et al., Computer program for determining fluorescence resonance energy transfer efficiency from flow cytometric data on a cell-by-cell basis. Comput. Methods Programs Biomed. 2004, 75, 201-211.
17. Nagy, P., Vereb, G., Damjanovich, S., Mátyus, L., Szöllösi, J., in: Robinson, J. P. (Ed.), Current Protocols in Cytometry, John Wiley & Sons, New York, 2006, pp. 12.18.11-12.18.13.
18. Szöllösi, J., Damjanovich, S., Nagy, P., Vereb, G., Mátyus, L., in: Robinson, J. P. (Ed.), Current Protocols in Cytometry, John Wiley & Sons, New York, 2006, pp. 1.12.11-1.12.16.
19. Kenworthy, A. K., Edidin, M., Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of<100Å using imaging fluorescence resonance energy transfer. J. Cell. Biol. 1998, 142, 69-84.
20. Nagy, P., Vereb, G., Sebestyén, Z., Horváth, G. et al., Lipid rafts and the local density of ErbB proteins influence the biological role of homo- and heteroassociations of ErbB2. J. Cell. Sci. 2002, 115, 4251-4262.
21. Gustafsdottir, S. M., Schallmeiner, E., Fredriksson, S., Gullberg, M. et al., Proximity ligation assays for sensitive and specific protein analyses. Anal. Biochem. 2005, 345, 2-9.
22. Clayton, A. H., Walker, F., Orchard, S. G., Henderson, C. et al., Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-A multidimensional microscopy analysis. J. Biol. Chem. 2005, 280, 30392-30399.
23. Liu, P., Sudhaharan, T., Koh, R. M., Hwang, L. C. et al., Investigation of the dimerization of proteins from the epidermal growth factor receptor family by single wavelength fluorescence cross-correlation spectroscopy. Biophys. J. 2007, 93, 684-698.
24. McLaughlin, S., Smith, S. O., Hayman, M. J., Murray, D., An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ErbB) family. J. Gen. Physiol. 2005, 126, 41-53.
25. Tzahar, E., Waterman, H., Chen, X., Levkowitz, G. et al., A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor. Mol. Cell. Biol. 1996, 16, 5276-5287.
26. Nagy, P., Bene, L., Balázs, M., Hyun, W. C. et al., EGF-induced redistribution of erbB2 on breast tumor cells: flow and image cytometric energy transfer measurements. Cytometry 1998, 32, 120-131.
27. Nagy, P., Friedländer, E., Tanner, M., Kapanen, A. I. et al., Decreased accessibility and lack of activation of ErbB2 in JIMT-1, a herceptin-resistant, MUC4-expressing breast cancer cell line. Cancer Res. 2005, 65, 473-482.
28. Stryer, L., Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 1978, 47, 819-846.
29. Szabó, A., Szöllösi, J., Nagy, P., Coclustering of ErbB1 and ErbB2 revealed by FRET-sensitized acceptor bleaching. Biophys. J. 2010, 99, 105-114.
30. Anikovsky, M., Dale, L., Ferguson, S., Petersen, N., Resonance energy transfer in cells: a new look at fixation effect and receptor aggregation on cell membrane. Biophys. J. 2008, 95, 1349-1359.
31. Yeow, E. K., Clayton, A. H., Enumeration of oligomerization states of membrane proteins in living cells by homo-FRET spectroscopy and microscopy: theory and application. Biophys. J. 2007, 92, 3098-3104.
32. Beutler, M., Makrogianneli, K., Vermeij, R. J., Keppler, M. et al., satFRET: estimation of Förster resonance energy transfer by acceptor saturation. Eur. Biophys. J. 2008, 38, 69-82.
33. Koushik, S. V., Blank, P. S., Vogel, S. S., Anomalous surplus energy transfer observed with multiple FRET acceptors. PLoS One 2009, 4, e8031.