Creating new fluorescent probes for cell biology

Nature Reviews Molecular Cell Biology

Volumn 3, Issue 12, 2002, Pages 906-918

  Zhang, Jin ^a   Campbell, Robert E ^a   Ting, Alice Y ^a   Tsien, Roger Y ^a,b  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AEQUOREA FLUORESCENT PROTEIN; BIOCHEMICAL MARKER; FLUORESCENT DYE; RED FLUORESCENT PROTEIN; UNCLASSIFIED DRUG;

CELL STRUCTURE; CYTOLOGY; DIAGNOSTIC VALUE; ENZYME ACTIVATION; FLUORESCENCE; FLUORESCENE RESONANCE ENERGY TRANSFER; HUMAN; IMAGE ANALYSIS; MEASUREMENT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE IMAGING; POSITRON EMISSION TOMOGRAPHY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; REVIEW; SENSITIVITY AND SPECIFICITY; STRUCTURE ANALYSIS;

ANIMALS; BIOLOGICAL TRANSPORT; CELL PHYSIOLOGY; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENT DYES; GENES, REPORTER; LUMINESCENT PROTEINS; MICROSCOPY, FLUORESCENCE; MODELS, MOLECULAR; MOLECULAR PROBE TECHNIQUES; MOLECULAR STRUCTURE; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS;

AEQUOREA;

EID: 0036902813     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm976     Document Type: Review

References (153)

1. Tsien, R. Y. The green fluorescent protein. Annu. Rev. Biochem. 67, 509-544 (1998).
2. Sawano, A. & Miyawaki, A. Directed evolution of green fluorescent protein by a new versatile PCR strategy for site-directed and semi-random mutagenesis. Nucleic Acids Res. 28, E78 (2000).
3. Griesbeck, O., Baird, G. S., Campbell, R. E., Zacharias, D. A. & Tsien, R. Y. Reducing the environmental sensitivity of yellow fluorescent protein Mechanism and applications. J. Biol. Chem. 276, 29188-29194 (2001).
4. Nagai, T. et al. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nature Biotechnol. 20, 87-90 (2002).
5. Scholz, O., Thiel, A., Hillen, W. & Niederweis, M. Quantitative analysis of gene expression with an improved green fluorescent protein. Eur. J. Biochem. 267, 1565-1570 (2000).
6. Ormö, M. et al. Crystal structure of the Aequorea victoria green fluorescent protein. Science 273, 1392-1395 (1996).
7. Yokoe, H. & Meyer, T. Spatial dynamics of GFP-tagged proteins investigated by local fluorescence enhancement. Nature Biotechnol 14, 1252-1256 (1996).
8. Sawin, K. E. & Nurse, P. Photoactivation of green fluorescent protein. Curr. Biol. 7, R606-R607 (1997).
9. Elowitz, M. B., Surette, M. G., Wolf, P. E., Stock, J. & Leibler, S. Photoactivation turns green fluorescent protein red. Curr. Biol. 7, 809-812 (1997).
10. Patterson, G. H. & Lippincott-Schwartz, J. A photoactivatable GFP for selective photolabeling of proteins and cells. Science 297, 1873-1877 (2002).
11. Ando, R., Hama, H., Yamamoto-Hino, M., Mizuno, H. & Miyawaki, A. An optical marker based on the UV-induced green-to-red photoconversion of a fluorescent protein. Proc. Natl. Acad. Sci. USA 99, 12651-12656 (2002). References 10 and 11 describe a pair of photoactivatable fluorescent proteins that can be used as fluorescent 'highlighters' to mark specific organelles or protein subpopulations.
12. Lippincott-Schwartz, J., Snapp, E. & Kenworthy, A. Studying protein dynamics in living cells. Nature Rev. Mol. Cell Biol. 2, 444-456 (2001).
13. Zacharias, D. A., Violin, J. D., Newton, A. C. & Tsien, R. Y. Partitioning of lipid-modified monomric GFPs into membrane microdomains of live cells. Science 296, 913-916 (2002).
14. Ward, W. W., Prentice, H. J., Roth, A. F., Cody, C. W. & ves, S. C. Spectral perturbations of the Aequorea green-fluorescent protein. Photochem. Photobiol. 35, 803-808 (1982).
15. Yang, F., Moss, L. G. & Phillips, G. N. Jr. The molecular structure of green fluorescent protein. Nature Biotechnol. 14, 1246-1251 (1996).
16. Matz, M. V. et al. Fluorescent proteins from nonbioluminescent Anthozoa species. Nature Biotechnol. 17, 969-973 (1999).
17. Tsien, R. Y. Rosy dawn for fluorescent proteins. Nature Biotechnol. 17, 956-957 (1999).
18. Zacharias, D. A. Sticky caveats in an otherwise glowing report: Oligomerizing fluorescent proteins and their use in cell biology. Sci. STKE. 2002, PE23 (2002).
19. Lauf, U., Lopez, P. & Falk, M. M. Expression of fluorescently tagged connexins: A novel approach to rescue function of oligomerc DsRed-tagged proteins. FEBS Lett. 498, 11-15 (2001).
20. Soling, A., Simm, A. & Rainov, N. Intracellular localization of Herpes simplex virus type 1 thymidine kinase fused to different fluorescent proteins depends on choice of fluorescent tag. FEBS Lett 527, 153 (2002).
21. Yanushevich, Y. G. et al. A strategy for the generation of non-aggregating mutants of Anthozoa fluorescent proteins. FEBS Lett. 511, 11-14 (2002).
22. Terskikh, A. V., Fradkov, A. F., Zaraisky, A. G., Kajava, A. V. & Angres, B. Analysis of DsRed mutants: Space around the fluorophore accelerates fluorescence development. J. Biol. Chem. 277, 7633-7636 (2002).
23. Bevis, B. J. & Glick, B. S. Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed). Nature Biotechnol. 20, 83-87 (2002).
24. Campbell, R. E. et al. A monomeric red fluorescent protein. Proc. Natl. Acad. Sci. USA 99, 7877-7882 (2002). This paper describes the directed evolution of a monomeric RFP that overcomes the problems associated with tetrameric DsRed.
25. Knop, M., Barr, F., Riedel, C. G., Heckel, T. & Reichel, C. Improved version of the red fluorescent protein (drFP583/DsRed/RFP). BioTechniques 33, 592, 594, 596-598 (20O2).
26. CLONTECH Laboratories Inc. Living Colors User Manual Vol. II. Red Fluorescent Protein 4 (Becton, Dickinson and Company, USA, 2002).
27. Fradkov, A. F. et al. Far-red fluorescent tag for protein labeling. Biochem. J. 388, 17-21 (2002).
28. Labas, Y. A. et al. Diversity and evolution of the green fluorescent protein family. Proc. Natl. Acad. Sci. USA 99, 4256-4261 (2002).
29. Matz, M. V. Lukyanov, K. A. & Lukyanov, S. A. Family of the green fluorescent protein: Journey to the end of the rainbow. Bioessays 24, 953-959 (2002).
30. Peelle, B., Gururaja, T. L., Payan, D. G. & Anderson, D. C. Characterization and use of green fluorescent proteins from Renilla mulleri and Ptilosarcus guernyi for the human cell display of functional peptides. J. Protein Chem. 20, 507-519 (2001).
31. Lukyanov, K. A. et al. Natural animal coloration can be determined by a non-fluorescent GFP homolog. J. Biol. Chem. 275, 25879-25882 (2000).
32. Fradkov, A. F. et al. Novel fluorescent protein from Discosoma coral and its mutants possesses a unique farred fluorescence. FEBS Lett. 479, 127-130 (2000).
33. Gurskaya, N. G. et al. GFP-like chromoproteins as a source of far-red fluorescent proteins. FEBS Lett. 507, 16-20 (2OO1).
34. Wiedenmann, J. et al. A far-red fluorescent protein with fast maturation and reduced oligomerization tendency from Entacmaea quadricolor (Anthozoa, Actinaria). Proc. Natl. Acad. Sci. USA 99, 11646-11651 (2002).
35. Griffin, B. A., Adams, S. R. & Tsien, R. Y. Specific covalent labeling of recombinant protein molecules inside live cells Science 281, 269-272 (1998).
36. Nakanishi, J. et al. Imaging of conformational changes of proteins with a new environment-sensitive fluorescent probe designed for site-specific labeling of recombinant proteins in live cells. Anal. Chem. 73, 2920-2928 (2001).
37. Adams, S. R. et al. New blarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications. J. Am. Chem. Soc. 124, 6063-6076 (2002).
38. Gaietta, G. et al. Multicolor and electron microscopic imaging of connexin trafficking. Science 296, 503-507 (2002). This paper describes the application of the tetracysteine-biarsenical system in pulse-chase labelling and electron microscopy.
39. Lauf, U. et al. Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells. Proc. Natl. Acad. Sci. USA 99, 10446-10451 (2002).
40. Farinas, J. & Verkman, A. S. Receptor-mediated targeting of fluorescent probes in living cells. J. Biol. Chem. 274, 7603-7606 (1999).
41. Wu, M. M. et al. Organelle pH studies using targeted avidin and fluorescein-biotin. Chem. Biol. 7, 197-209 (2000).
42. Wu, M. M. et al. Studying organalle physiology using targeted avidin and fluorescein-biotin, Methods Enzymol. 327, 546-564 (2000).
43. Wu, M. M. et al. Mechanisms of pH regulation in the regulated secretory pathway. J. Biol. Chem. 276, 33027-33035 (2001).
44. Sano, T. & Cantor, C. R. Expression of a cloned streptavidin gene in Escherichia coli. Proc. Natl. Acad. Sci. USA 87, 142-146 (1990).
45. Gambetta, G. A. & Lagarias, J. C. Genetic engineering of phytochrome biosynthesis in bacteria. Proc. Natl. Acad. Sci. USA 98, 10566-10571 (2001).
46. Tooley, A. J., Cai, Y. A. & Glazer, A. N. Biosynthesis of a fluorescent cyanobacterial C-phycocyanin holo-α subunit in a heterologous host. Proc. Natl. Acad. Sci. USA 98, 10560-10565 (2001).
47. Tooley, A. J. & Glazer, A. N. Biosynthesis of the cyanobacterial light-harvesting polypeptide phycoerythrocyanin holo-α subunit in a heterologous host, J. Bacteriol. 184, 4666-4671 (2002).
48. Murphy, J. T. & Lagarias, J. C. The phytofluors: A new class of fluorescent protein probes. Curr. Biol. 7, 870-876 (1997).
49. Wildt, S. & Deuschle, U. cobA, a red fluorescent transcriptional reporter for Escherichia coli yeast, and mammalian cells. Nature Biotechnol. 17, 1175-1178 (1999).
50. Cubitt, A. B. et al. Understanding, using and improving green fluorescent protein. Trends Biochem. Sci. 20, 448-455 (1995).
51. Gonzalez, C. & Bejarano, L. A. Protein traps: Using intracellular localization for cloning. Trends Cell Biol. 10, 162-165 (2000).
52. Waterman-Storer, C. M., Desai, A., Bulinski, J. C. & Salmon, E. D. Fluorescent speckle microscopy, a method to visualize the dynamics of protein assemblies in living cells. Curr. Biol. 8, 1227-1230 (1998).
53. Watanabe, N. & Mitchison, T. J. Single-molecule speckle analysis of actin filament turnover in lamellipodia. Science 295, 1083-1086 (2002).
54. Bulinski, J. C., Odde, D. J., Howell, B. J., Salmon, T. D. & Waterman-Storer, C. M. Rapid dynamics of the microtubule binding of ensconsin in vivo. J. Cell Sci. 114, 3885-3897 (2001).
55. Watton, S. J. & Downward, J. Akt/PKB localisation and 3′ phosphoinositide generation at sites of epithelial cell-matrix and cell-cell interaction. Curr. Biol. 9, 433-436 (1999).
56. Oatey, P. B. et al. Confocal imaging of the subcellular distribution of phosphatidylinositol 3,4,5-trisphosphate in insulin- and PDGF-stimulated 3T3-L1 adipocytes. Biochem. J. 344, 511-518 (1999).
57. Gray, A., Van Der, K. J. & Downes, C. P. The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides·1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-trisphosphate in vivo. Biochem. J. 344, 929-936 (1999).
58. Servant, G. et al. Polarization of chemoattractant receptor signaling during neutrophil chemotaxis. Science 287, 1037-1040 (2000).
59. Meili, R. et al. Chemoattractant-mediated transient activation and membrane localization of Akt/PKB is required for efficient chemotaxis to cAMP in Dictyostelium. EMBO J. 18, 2092-2105 (1999).
60. 2 concentration monitored in living cells. Curr. Biol. 8, 343-346 (1998).
61. 2+ mobilization patterns. Science 284, 1527-1530 (1999).
62. Oancea, E., Teruel, M. N., Quest, A. F. G. & Meyer, T. Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells. J. Cell Biol. 140, 485-498 (1998).
63. Teruel, M. N. & Meyer, T. Parallel single-cell monitoring of receptor-triggered membrane translocation of a calcium-sensing protein module. Science 295, 1910-1912 (2002).
64. 2+ and DAG signals.
65. Rizzo, M. A., Shome, K., Watkins, S. C. & Romero, G. The recruitment of Raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with Ras. J. Biol. Chem. 275, 23911-23918 (2000).
66. Dirks, R. W., Molenaar, C. & Tanke, H. J. Methods for visualizing RNA processing and transport pathways in living cells. Histochem. Cell. Biol. 115, 3-11 (2001).
67. Bassell, G. J., Oleynikov, Y. & Singer, R. H. The travels of mRNAs through all cells large and small. FASEB J. 13, 447-454 (1999).
68. Bertrand, E. et al. Localization of ASH1 mRNA particles in living yeast. Mol. Cell 2, 437-445 (1998).
69. Theurkauf, W. E. & Hazelrigg, T. I. In vivo analyses of cytoplasmic transport and cytoskeletal organization during Drosophila oogenesis: Haracterization of a multi-step anterior localization pathway. Development 25, 3655-3666 (1998).
70. Zhang, H. L. et al. Neurotrophin-induced transport of a β-actin mRNP complex increases β-actin levels and stimulates growth cone motility. Neuron 31, 261-275 (2001).
71. Muller, W. G., Walker, D., Hager, G. L. & McNally, J. G. Large-scale chromatin decondensation and recondensation regulated by transcription from a natural promoter J. Cell Biol. 154, 33-48 (2001).
72. Tsukamoto, T. et al. Visualization of gene activity in living cells. Nature Cell Biol. 2, 871-878 (2000).
73. Straight, A. F., Marshall, W. F., Sedat, J. W. & Murray, A. W. Mitosis in living budding yeast: Anaphase A but no metaphase plate. Science 277, 574-578 (1997).
74. Robinett, C. C. et al. In vivo localization of DNA sequences and visualization of large-scale chromatin organization using lac operator/repressor recognition. J. Cell Biol. 135, 1685-1700 (1996).
75. Hadjantonakis, A. K. & Nagy, A. The color of mice: In the light of GFP-variant reporters. Histochem. Cell Biol. 115, 49-58 (2001).
76. Zlokarnik, G. et al. Quantitation of transcription and clonal selection of single living cells using β-lactamase as reporter. Science 279, 84-88 (1998).
77. Li, X. et al. Generation of destabilized green fluorescent protein as a transcription reporter. J. Biol. Chem. 273, 34970-34975 (1998).
78. Terskikh, A. et al. 'Fluorescent timer': Protein that changes color with time. Science 290, 1585-1588 (2000). This paper describes a DsRed-derived transcriptional reporter that changes colour from green to red over a period of 24 h, thereby preserving the temporal history of promoter activation.
79. Dantuma, N. P., Lindsten, K., Glas, R., Jellne, M. & Masucci, M. G. Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells, Nature Biotechnol. 18, 538-543 (2000).
80. Kaether, C. & Gerdes, H. H. Visualization of protein transport along the secretory pathway using green fluorescent protein FEBS Lett. 369, 267-271 (1995).
81. Rudolf, R., Salm, T., Rustom, A. & Gerdes, H. H. Dynamics of immature secretory granules: Role of cytoskeletal elements during transport, cortical restriction, and F-actin-dependent tethering. Mol. Biol. Cell 12, 1353-1365 (2001).
82. Kneen, M., Farinas, J., Li, Y. & Verkman, A. S. Green flourescent protein as a noninvasive intracellular pH indicator. Biophys. J. 74, 1591-1599 (1998).
83. Llopis, J., McCaffery, J. M., Miyawaki, A., Farquhar, M. G. & Tsien, R. Y. Measurement of cytosolic, mitochondrial and Golgi pH in single living cells with green fluorescent protein. Proc. Natl. Acad. Sci. USA 95, 6803-6808 (1998).
84. Miesenböck, G., De Angelis, D. A. & Rothman, J. E. Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 394, 192-195 (1998). Reference 84 describes 'synapto-pHluorins' that report synaptic neurotransmitter secretion by detecting the abrupt pH change that occurs when the acidic interior of the vesicle (pH ∼5) is exposed to the outside of the cell (pH ∼7) on fusion to the plasma membrane.
85. Matsuyama, S., Llopis, J., Deveraux, Q. L., Tsien, R. Y. & Reed, J. C. Changes in intramitochondrial and cytosolic pH: Early events that modulate caspase activation during apoptosis. Nature Cell Biol. 2, 318-325 (2000).
86. Wachter, R. M. & Remington, S. J. Sensitivity of the yellow variant of green fluorescent protein to halides and nitrate. Curr. Biol. 9, R62B-R629 (1999).
87. Wachter, R. M., Yarbrough, D., Kallio, K. & Remington, S. J. Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein. J. Mol. Biol. 301, 157-171 (2000).
88. Jayaraman, S., Haggie, R., Wachter R. M., Remington, S. J. & Verkman, A. S. Mechanism and cellular applications of a green fluorescent protein-based halide sensor. J. Biol. Chem. 275, 6047-6050 (2000).
89. Eisliger, M.-A., Wachter, R. M., Hanson, G. T., Kallio, K. & Remington, S. J. Structural and spectral response of green fluorescent protein variants to changes in pH, Biochemistry 38, 5296-5301 (1999).
90. Kuner, T. & Augustine, G. J. A genetically encoded ratiometric neurotechnique indicator for chloride capturing chloride transients in cultured hippocampal neurons. Neuron 27, 447-459 (2000).
91. Barondeau, D. P., Kassmann, C. J., Tainer, J. A. & Getzoff, E. D. Structural chemistry of a green fluorescent protein Zn biosensor. J. Am. Chem. Soc. 124, 3522-3524 (2002).
92. Ostergaard, H., Hennksen, A., Hansen, F. G. & Winther, J. R. Shedding light on disulfide bond formation: Engineering a redox switch in green fluorescent protein. EMBO J. 20, 5853-5862 (2001).
93. Baird, G. S., Zacharias, D. A. & Tsian, R., Y. Circular permutation and receptor insertion within green fluorescent proteins. Proc. Natl. Acad. Sci, USA 96, 11241-11246 (1999).
94. 2- microdomains to mitochondria. J. Cell. Biol. (in the press)
95. Yu, D., Baird, G., Tsien, R. Y. & Davis, R. L. Detection of calcium transient in Drosophila mushroom body neurons with camgaroo. Neurosci. (in the press).
96. Slegel, M. S. & Isacoff, E. Y. A genetically encoded optical probe of membrane voltage. Neuron 19, 735-741 (1997).
97. Ataka, K. & Pieribone, V. A. A genetically targetable fluorescent probe of channel gating with rapid kinetics. Biophys. J. 82, 509-516 (2002).
98. 2+ probe composed of a single green fluorescent protein Nature Biotechnol. 19, 137-141 (2001).
99. 2+ indicators that have been dubbed 'GCaMP' and 'pericams', respectively.
100. Helm, R. & Tsien, R. Y. Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence energy transfer. Curr. Biol. 6, 178-182 (1996).
101. Mitre, R. D., Silva, C. M. & Youvan, D. C. Fluorescence resonance energy transfer between blue-emitting and redshifted excitation derivatives of the green fluorescent protein. Gene 173, 13-17 (1996).
102. Mahajan, N. P., Harrison-Shostak, D. C., Michaux, J. & Herman, B. Novel mutant green fluorescent protein protease substrates reveal the activation of specific caspases during apoptosis. Chem. Biol. 6, 401-409 (1999).
103. Luo, K. Q., Yu, V. C., Pu, Y. & Chang, D. C. Application of the fluorescence resonance energy transfer method for studying the dynamics of caspase-3 activation during UV-induced apoptosi1s in living HeLa cells. Biochem. Biophys. Res. Commun. 283, 1054-1060 (2001).
104. Rehm, M. et al. Singre-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process. Role of caspase-3. J. Biol. Chem. 277, 24506-24514 (2002).
105. 2- based on green fluorescent proteins and calmodulin. Nature 388, 882-887 (1997).
106. 2- measurements using improved cameleons. Proc. Natl. Acad. Sci. USA 96, 2135-2140 (1999).
107. Miyawaki, A. & Tsien, R. Y. Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein Methods Enzymol. 327, 472-500 (2000).
108. 2+ imaging by a new calmodulin-GFP fusion molecule. Nature Struct. Biol. 8, 1069-1073 (2001).
109. 2+-dependent changes in the fluorescence emission of an indicator composed of two green fluorescent protein variants linked by a calmodulin-binding sequence. J. Biol. Chem. 272, 13270-13274 (1997). References 105 and 109 describe the first genetically encoded indicators to be composed of conformationally responsive elements sandwiched between two fluorescent proteins that can undergo FRET - A design that has since been extended to many other systems.
110. 2--calmodulin in intact cells J. Biol. Chem. 274, 6827-6830 (1999).
111. Sato, M., Hida, N., Ozawa, T. & Umezawa, Y. Fluorescent indicators for cyclic GMP based on cyclic GMP-dependent protein kinase I α and green fluorescent proteins. Anal. Chem. 72, 5918-5924 (2000).
112. Honda, A. et al. Spatiotemporal dynamics of guanosine 3′,5′-cyclic monophosphate revealed by a genetically encoded, fluorescent indicator. Proc. Natl. Acad. Sci. USA 98, 2437-2442 (2001).
113. Mochizuki, N. et al. Spatio-temporal images of growth-factor-induced activation of Ras and Rap1. Nature 411, 1065-1068 (2001).
114. Kalab, P., Weis, K. & Heald, R. Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts Science 295, 2452-2456 (2002).
115. Kurokawa, K. et al. A pair of FRET-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo. J. Biol. Chem 276, 31305-31310 (2001).
116. Ting, A. Y., Kan, K. H., Kemke, R. L. & Tsien, R. Y. Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells, Proc. Natl. Acad. Sci. USA 98, 15003-15008 (2001).
117. Sato, M., Ozawa, T., Inukal, K., Asano, T. & Umezawa, Y. Fluorescent indicators for imaging protein phosphorylation in single living cells. Nature Biotechnol. 20, 287-294 (2002).
118. Zhang, J., Ma, Y., Taylor, S. S. & Tsien, R. Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering. Proc. Natl. Acad. Sci. USA 98, 14997-15002 (2001). References 116 and 118 describe a general strategy for non-destructively imaging kinase activities in living cells using FRET-based reporters.
119. Sakai, R., Repunte-Canonigo, V., Raj, C. D. & Knopfel, T. Design and characterization of a DNA-encoded, voltage-sensitive fluorescent protein. Eur. J. Neurosci 13, 2314-2318 (2001).
120. Adams, S. R., Harootunian, A. T., Buechler, Y. J., Taylor S. S. & Tsien, R. Y. Fluorescence ratio imaging of cyclic AMP in single cells. Nature 349, 694-697 (1991).
121. Zaccolo, M. et al. A genetically encoded, fluorescent indicator for cyclic AMP in living cells. Nature Cell Biol. 2, 25-29 (2000).
122. Zaccolo, M. & Pozzan, T. Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes. Science 295, 1711-1715 (2002). The use of a genetically encodable intermolecular FRET-based cAMP indicator in cardiac myocytes showed an unusual compartmentalization of cAMP.
123. Bacskai, B. J. et al. Spatially resolved dynamics of cAMP and protein kinase A subunits in Aplysia sensory neurons. Science 260, 222-226 (1993).
124. Hempel, C. M., Vincent, P., Adams, S. R., Tsien, R. Y. & Selverston, A. I. Spatio-temporal dynamics of cAMP signals in an intact neural circuit. Nature 384, 166-169 (1996).
125. Periasamy, A., Kay, S. A. & Day, R. N. in Functional Imaging and Optical Manipulation of Living Cells. SPIE Proc. Vol. 2983 (eds Farkas, D. L. & Tromberg, B. J.) (The International Society for Optical Engineers, USA, 1997).
126. Llopis, J. et al. Ligand-dependent interactions of coactivators SRC-1 and PBP with nuclear hormone receptors can be imaged in live cells and are required for transcription. Proc. Natl. Acad. Sci. USA 97, 4363-4368 (2000).
127. Janetopoulos, C., Jin, T. & Devreotes, P. Receptor-mediated activation of heterotrimeric G proteins in living cells. Science 291, 2408-2411 (2001).
128. Damelin, M. & Silver, P. A. Mapping interactions between nuclear transport factors in living cells reveals pathways through the nuclear pore complex. Mol. Cell 5, 133-140 (2000).
129. Ruehr, M. L., Zakhary, D. R., Damron, D. S. & Bond, M. Cyclic AMP-dependent protein kinase binding to A-kinase anchoring proteins in living cells by fluorescence resonance energy transfer of green fluorescent protein fusion proteins. J. Biol. Chem. 274, 33092-33096 (1999).
130. Siegel, R. M. et al. Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations. Science 288, 2354-2357 (2000).
131. Xia, Z., Zhou, Q., Lin, J. & Liu, Y. Stable SNARE complex prior to evoked synaptic vesicle fusion revealed by fluorescence resonance energy transfer. J. Biol. Chem. 276, 1766-1771 (2001).
132. Li, H. Y. et al. Protein-protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET). J. Cell Biochem. 80, 293-303 (2001).
133. Mas, R., Devlin, P. F., Panda, S. & Kay, S. A Functional interaction of phytochrome B and cryptochrome 2. Nature 408, 207-211 (2000).
134. Tertoolen, L. G. et al. Dimerization of receptor protein-tyrosine phosphatase α in living cells. B.M.C. Cell Biol. 2, 8 (2001).
135. Ghosh, I., Hamilton, A. D. & Regan, L. Antiarale eucine zipper-directed protein reassembly: Application to the green fluorescent protein. J. Am. Chem. Soc. 122, 5658-5659 (2000).
136. Hu, C.-D., Chinenov, Y. & Kerppola, T. K. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell. 9, 789-798 2002).
137. Rossi, F., Charlton, C. A. & Blau, H. M. Monitoring protein-protein interactions in intact eukaryotic cells by β-galactosidase complementation. Proc. Natl. Acad. Sci. USA 94, 8405-8410 (1997).
138. Michnick, S. W., Remy, I., Campbell-Valois, F. X., Vallee-Belisle, A. & Pelletier, J. N. Detection of protein-protein interactions by protein fragment complementation strategies. Methods Enzymol. 328, 208-230 (2000).
139. Wehrman, T., Kleaveland, B., Her, J. H., Balint, R. F. & Blau, H. M. Protein-protein interactions monitored in mammalian cells via complementation of β-lactamase enzyme fragments Proc. Natl. Acad. Sci. USA 99, 3469-3474 (2002).
140. Galarneau, A., Primeau, M., Trudeau, L. E. & Michnick, S. W. β-lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions Nature Biotechnol. 20, 619-622 (2002).
141. Gordon, G. W., Berry, G., Liang, X. H., Levine, B. & Herman, B. Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys. J. 74, 2702-2713 (1998).
142. Sorkin, A., McClure, M., Huang, F. & Carter, R. Interaction of EGF receptor and grb2 in living cells visualized by fluorescence resonance energy transfer (FRET) microscopy. Curr. Biol. 10, 1395-1398 (2000).
143. 2-) channels revealed by FRET in single living cells. Neuron 31, 973-985 (2001).
144. Chan, F. K. et al. Fluorescence resonance energy transfer analysis of cell surface receptor interactions and signaling using spectral variants of the green fluorescent protein. Cytometry 44, 361-368 (2001).
145. Ng, T. et al. Imaging protein kinase Cα activation in cells. Science 283, 2085-2089 (1999).
146. Verveer, P. J., Wouters, F. S., Reynolds, A. R. & Bastiaens, P. I. Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane. Science 290, 1567-1570 (2000).
147. Harpur, A. G., Wouters, F. S. & Bastiaens, P. I. Imaging FRET between spectrally similar GFP molecules in single cells. Nature Biotechnol. 19, 167-169 (2001).
148. Weiss, S. Fluorescence spectroscopy of single biomolecules. Science 283, 1676-1683 (1999).
149. Sako, Y., Minoguchi, S. & Yanagida, T. Single-molecule imaging of EGFR signalling on the surface of living cells. Nature Cell Biol. 2, 168-172 (2000).
150. Sonnleitner, A., Mannuzzu, L. M., Terakawa, S. & Isacoff, E. Y. Structural rearrangements in single ion channels detected optically in living cells. Proc. Natl. Acad. Sci. USA 99, 12759-12764 (2002).
151. 2+) channels in live cells. Biophys J. 81, 2639-2646 (2001).
152. Ito, S. et al. Real-time observation of micrometastasis formation in the living mouse liver using a green fluorescent protein gene-tagged rat tongue carcinoma cell line. Int. J. Cancer 93, 212-217 (2001).
153. Brown, E. B. et al. In vivo measurement of gene expression, angiogenesis and physiological function in tumors using multiphoton laser scanning microscopy. Nature Med. 7, 864-868 (2001).