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Volumn 16, Issue 7, 2015, Pages 14695-14716

Homo-FRET based biosensors and their application to multiplexed imaging of signalling events in live cells

Author keywords

FRET; Homo FRET; Multiplexed imaging; Time resolved fluorescence anisotropy imaging (TR FAIM)

Indexed keywords

CYAN FLUORESCENT PROTEIN; PHOSPHATIDYLINOSITIDE; PROTEIN KINASE B; CALCIUM; GREEN FLUORESCENT PROTEIN; PHOSPHATIDYLINOSITOL;

EID: 84936868588     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms160714695     Document Type: Article
Times cited : (44)

References (57)
  • 1
    • 67650302266 scopus 로고    scopus 로고
    • Simultaneous live cell imaging using dual FRET sensors with a single excitation light
    • Niino, Y.; Hotta, K.; Oka, K. Simultaneous live cell imaging using dual FRET sensors with a single excitation light. PLoS ONE 2009, 4, e6036, doi:10.1371/journal.pone.0006036.
    • (2009) Plos ONE , vol.4
    • Niino, Y.1    Hotta, K.2    Oka, K.3
  • 2
    • 42449154333 scopus 로고    scopus 로고
    • Simultaneous recording of multiple cellular events by FRET
    • Piljic, A.; Schultz, C. Simultaneous recording of multiple cellular events by FRET. ACS Chem. Biol. 2008, 3, 156-160.
    • (2008) ACS Chem. Biol , vol.3 , pp. 156-160
    • Piljic, A.1    Schultz, C.2
  • 4
    • 44449109239 scopus 로고    scopus 로고
    • Improving the photostability of bright monomeric orange and red fluorescent proteins
    • Shaner, N.; Lin, M.; McKeown, M.; Steinbach, P. Improving the photostability of bright monomeric orange and red fluorescent proteins. Nat. Methods 2008, 5, 545-551.
    • (2008) Nat. Methods , vol.5 , pp. 545-551
    • Shaner, N.1    Lin, M.2    McKeown, M.3    Steinbach, P.4
  • 6
    • 80052428624 scopus 로고    scopus 로고
    • Analysis of red-fluorescent proteins provides insight into dark-state conversion and photodegradation
    • Dean, K.M.; Lubbeck, J.L.; Binder, J.K.; Schwall, L.R.; Jimenez, R.; Palmer, A.E. Analysis of red-fluorescent proteins provides insight into dark-state conversion and photodegradation. Biophys. J. 2011, 101, 961-969.
    • (2011) Biophys. J , vol.101 , pp. 961-969
    • Dean, K.M.1    Lubbeck, J.L.2    Binder, J.K.3    Schwall, L.R.4    Jimenez, R.5    Palmer, A.E.6
  • 7
    • 66149096239 scopus 로고    scopus 로고
    • Fluorescence fluctuation spectroscopy of mCherry in living cells
    • Wu, B.; Chen, Y.; Müller, J.D. Fluorescence fluctuation spectroscopy of mCherry in living cells. Biophys. J. 2009, 96, 2391-2404.
    • (2009) Biophys. J , vol.96 , pp. 2391-2404
    • Wu, B.1    Chen, Y.2    Müller, J.D.3
  • 8
    • 43849083731 scopus 로고    scopus 로고
    • Dark states in monomeric red fluorescent proteins studied by fluorescence correlation and single molecule spectroscopy
    • Hendrix, J.; Flors, C.; Dedecker, P.; Hofkens, J.; Engelborghs, Y. Dark states in monomeric red fluorescent proteins studied by fluorescence correlation and single molecule spectroscopy. Biophys. J. 2008, 94, 4103-4113.
    • (2008) Biophys. J , vol.94 , pp. 4103-4113
    • Hendrix, J.1    Flors, C.2    Dedecker, P.3    Hofkens, J.4    Engelborghs, Y.5
  • 10
    • 0021454425 scopus 로고
    • Analysis of time-resolved fluorescence anisotropy decays
    • Cross, A.J.; Fleming, G.R. Analysis of time-resolved fluorescence anisotropy decays. Biophys. J. 1984, 46, 45-56.
    • (1984) Biophys. J , vol.46 , pp. 45-56
    • Cross, A.J.1    Fleming, G.R.2
  • 11
    • 5644226253 scopus 로고    scopus 로고
    • Dynamic and static fluorescence anisotropy in biological microscopy (RFLIM and emFRET)
    • Periasamy, A., So, P.T.C., Eds.; International Society for Optics and Photonics: Bellingham, WA, USA
    • Jovin, T.M.; Lidke, D.S.; Post, J.N. Dynamic and static fluorescence anisotropy in biological microscopy (rFLIM and emFRET). In Biomedical Optics 2004; Periasamy, A., So, P.T.C., Eds.; International Society for Optics and Photonics: Bellingham, WA, USA, 2004; pp. 1-12.
    • (2004) Biomedical Optics 2004 , pp. 1-12
    • Jovin, T.M.1    Lidke, D.S.2    Post, J.N.3
  • 12
    • 37248999419 scopus 로고    scopus 로고
    • Fluorescence anisotropy imaging microscopy for homo-FRET in living cells
    • Tramier, M.; Coppey-Moisan, M. Fluorescence anisotropy imaging microscopy for homo-FRET in living cells. Methods Cell Biol. 2008, 85, 395-414.
    • (2008) Methods Cell Biol , vol.85 , pp. 395-414
    • Tramier, M.1    Coppey-Moisan, M.2
  • 13
    • 1942425048 scopus 로고    scopus 로고
    • Red-edge anisotropy microscopy enables dynamic imaging of homo-FRET between green fluorescent proteins in cells
    • Squire, A.; Verveer, P.J.; Rocks, O.; Bastiaens, P.I.H. Red-edge anisotropy microscopy enables dynamic imaging of homo-FRET between green fluorescent proteins in cells. J. Struct. Biol. 2004, 147, 62-69.
    • (2004) J. Struct. Biol , vol.147 , pp. 62-69
    • Squire, A.1    Verveer, P.J.2    Rocks, O.3    Bastiaens, P.4
  • 15
    • 0036708469 scopus 로고    scopus 로고
    • Dynamic fluorescence anisotropy imaging microscopy in the frequency domain (RFLIM)
    • Clayton, A.H.A.; Hanley, Q.S.; Arndt-Jovin, D.J.; Subramaniam, V.; Jovin, T.M. Dynamic fluorescence anisotropy imaging microscopy in the frequency domain (rFLIM). Biophys. J. 2002, 83, 1631-1649.
    • (2002) Biophys. J , vol.83 , pp. 1631-1649
    • Clayton, A.1    Hanley, Q.S.2    Arndt-Jovin, D.J.3    Subramaniam, V.4    Jovin, T.M.5
  • 16
    • 55349095832 scopus 로고    scopus 로고
    • The polarized AB plot for the frequency-domain analysis and representation of fluorophore rotation and resonance energy homotransfer
    • Clayton, A.H.A. The polarized AB plot for the frequency-domain analysis and representation of fluorophore rotation and resonance energy homotransfer. J. Microsc. 2008, 232, 306-312.
    • (2008) J. Microsc , vol.232 , pp. 306-312
    • Clayton, A.1
  • 17
    • 82955195098 scopus 로고    scopus 로고
    • Evidence for extended YFP-EGFR dimers in the absence of ligand on the surface of living cells
    • Kozer, N.; Henderson, C.; Jackson, J.T.; Nice, E.C.; Burgess, A.W.; Clayton, A.H.A. Evidence for extended YFP-EGFR dimers in the absence of ligand on the surface of living cells. Phys. Biol. 2011, 8, 066002, doi:10.1088/1478-3975/8/6/066002.
    • (2011) Phys. Biol , vol.8
    • Kozer, N.1    Henderson, C.2    Jackson, J.T.3    Nice, E.C.4    Burgess, A.W.5    Clayton, A.6
  • 18
    • 34249674419 scopus 로고    scopus 로고
    • Imaging of protein cluster sizes by means of confocal time-gated fluorescence anisotropy microscopy
    • Bader, A.N.; Hofman, E.G.; van Bergen en Henegouwen, P.M.; Gerritsen, H.C. Imaging of protein cluster sizes by means of confocal time-gated fluorescence anisotropy microscopy. Opt. Express 2007, 15, 6934-6945.
    • (2007) Opt. Express , vol.15 , pp. 6934-6945
    • Bader, A.N.1    Hofman, E.G.2    Gerritsen, H.C.3
  • 19
    • 72249114997 scopus 로고    scopus 로고
    • Homo-FRET imaging enables quantification of protein cluster sizes with subcellular resolution
    • Bader, A.N.; Hofman, E.G.; Voortman, J.; en Henegouwen, P.M.; Gerritsen, H.C. Homo-FRET imaging enables quantification of protein cluster sizes with subcellular resolution. Biophys. J. 2009, 97, 2613-2622.
    • (2009) Biophys. J , vol.97 , pp. 2613-2622
    • Bader, A.N.1    Hofman, E.G.2    Voortman, J.3    En Henegouwen, P.M.4    Gerritsen, H.C.5
  • 21
    • 0029117442 scopus 로고
    • Theory and application of fluorescence homotransfer to melittin oligomerization
    • Runnels, L.W.; Scarlata, S.F. Theory and application of fluorescence homotransfer to melittin oligomerization. Biophys. J. 1995, 69, 1569-1583.
    • (1995) Biophys. J , vol.69 , pp. 1569-1583
    • Runnels, L.W.1    Scarlata, S.F.2
  • 23
    • 0031000601 scopus 로고    scopus 로고
    • Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: Cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion
    • Swaminathan, R.; Hoang, C.P.; Verkman, A.S. Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: Cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion. Biophys. J. 1997, 72, 1900-1907.
    • (1997) Biophys. J , vol.72 , pp. 1900-1907
    • Swaminathan, R.1    Hoang, C.P.2    Verkman, A.S.3
  • 24
    • 38549132277 scopus 로고    scopus 로고
    • Inositol derivatives: Evolution and functions
    • Michell, R.H. Inositol derivatives: Evolution and functions. Nat. Rev. Mol. Cell Biol. 2008, 9, 151-161.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 151-161
    • Michell, R.H.1
  • 27
    • 42149177825 scopus 로고    scopus 로고
    • The regulation of cell motility and chemotaxis by phospholipid signaling
    • Kölsch, V.; Charest, P.G.; Firtel, R.A. The regulation of cell motility and chemotaxis by phospholipid signaling. J. Cell Sci. 2008, 121, 551-559.
    • (2008) J. Cell Sci , vol.121 , pp. 551-559
    • Kölsch, V.1    Charest, P.G.2    Firtel, R.A.3
  • 28
    • 0034635513 scopus 로고    scopus 로고
    • Polarization of chemoattractant receptor signaling during neutrophil chemotaxis
    • Servant, G. Polarization of chemoattractant receptor signaling during neutrophil chemotaxis. Science 2000, 287, 1037-1040.
    • (2000) Science , vol.287 , pp. 1037-1040
    • Servant, G.1
  • 29
    • 0033617576 scopus 로고    scopus 로고
    • A cell’s sense of direction
    • Parent, C.A. A cell’s sense of direction. Science 1999, 284, 765-770.
    • (1999) Science , vol.284 , pp. 765-770
    • Parent, C.A.1
  • 30
    • 0037205265 scopus 로고    scopus 로고
    • Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis
    • Funamoto, S.; Meili, R.; Lee, S.; Parry, L.; Firtel, R.A. Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis. Cell 2002, 109, 611-623.
    • (2002) Cell , vol.109 , pp. 611-623
    • Funamoto, S.1    Meili, R.2    Lee, S.3    Parry, L.4    Firtel, R.A.5
  • 31
    • 0037205230 scopus 로고    scopus 로고
    • Tumor suppressor PTEN mediates sensing of chemoattractant gradients
    • Iijima, M.; Devreotes, P. Tumor suppressor PTEN mediates sensing of chemoattractant gradients. Cell 2002, 109, 599-610.
    • (2002) Cell , vol.109 , pp. 599-610
    • Iijima, M.1    Devreotes, P.2
  • 32
    • 0037415640 scopus 로고    scopus 로고
    • Rac and Cdc42 play distinct roles in regulating PI(3,4,5)P3 and polarity during neutrophil chemotaxis
    • Srinivasan, S.; Wang, F.; Glavas, S.; Ott, A.; Hofmann, F.; Aktories, K.; Kalman, D.; Bourne, H.R. Rac and Cdc42 play distinct roles in regulating PI(3,4,5)P3 and polarity during neutrophil chemotaxis. J. Cell Biol. 2003, 160, 375-385.
    • (2003) J. Cell Biol , vol.160 , pp. 375-385
    • Srinivasan, S.1    Wang, F.2    Glavas, S.3    Ott, A.4    Hofmann, F.5    Aktories, K.6    Kalman, D.7    Bourne, H.R.8
  • 33
    • 33748376922 scopus 로고    scopus 로고
    • Regulation of chemotaxis by the orchestrated activation of Ras, PI3K, and TOR
    • Sasaki, A.T.; Firtel, R. Regulation of chemotaxis by the orchestrated activation of Ras, PI3K, and TOR. Eur. J. Cell Biol. 2006, 85, 873-895.
    • (2006) Eur. J. Cell Biol , vol.85 , pp. 873-895
    • Sasaki, A.T.1    Firtel, R.2
  • 34
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley, L.C. The phosphoinositide 3-kinase pathway. Science 2002, 296, 1655-1657.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 35
    • 0024509946 scopus 로고
    • Role of phosphatidylinositol kinase in PDGF receptor signal transduction
    • Escobedo, J.; Williams, L. Role of phosphatidylinositol kinase in PDGF receptor signal transduction. Science 1989, 243, 1191-1194.
    • (1989) Science , vol.243 , pp. 1191-1194
    • Escobedo, J.1    Williams, L.2
  • 36
    • 1542793153 scopus 로고
    • Platelet-derived growth factor (PDGF) binding promotes physical association of PDGF receptor with phospholipase C
    • Kumjian, D.A.; Wahl, M.I.; Rhee, S.G.; Daniel, T.O. Platelet-derived growth factor (PDGF) binding promotes physical association of PDGF receptor with phospholipase C. Proc. Natl. Acad. Sci. USA 1989, 86, 8232-8236.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8232-8236
    • Kumjian, D.A.1    Wahl, M.I.2    Rhee, S.G.3    Daniel, T.O.4
  • 37
    • 34547897405 scopus 로고    scopus 로고
    • IP3 receptor/Ca2+ channel: From discovery to new signaling concepts
    • Mikoshiba, K. IP3 receptor/Ca2+ channel: From discovery to new signaling concepts. J. Neurochem. 2007, 102, 1426-1446.
    • (2007) J. Neurochem , vol.102 , pp. 1426-1446
    • Mikoshiba, K.1
  • 39
    • 37049035944 scopus 로고    scopus 로고
    • Phospholipase C regulation of phosphatidylinositol 3,4,5-trisphosphate-mediated chemotaxis
    • Kortholt, A.; King, J.S.; Keizer-Gunnink, I.; Harwood, A.J.; van Haastert, P.J.M. Phospholipase C regulation of phosphatidylinositol 3,4,5-trisphosphate-mediated chemotaxis. Mol. Biol. Cell 2007, 18, 4772-4779.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4772-4779
    • Kortholt, A.1    King, J.S.2    Keizer-Gunnink, I.3    Harwood, A.J.4    Van Haastert, P.5
  • 40
    • 0029791504 scopus 로고    scopus 로고
    • Mutation of a Src phosphorylation site in the PDGF β-receptor leads to increased PDGF-stimulated chemotaxis but decreased mitogenesis
    • Hansen, K.; Johnell, M.; Siegbahn, A.; Rorsman, C.; Engström, U.; Wernstedt, C.; Heldin, C.H.; Rönnstrand, L. Mutation of a Src phosphorylation site in the PDGF β-receptor leads to increased PDGF-stimulated chemotaxis but decreased mitogenesis. EMBO J. 1996, 15, 5299-5313.
    • (1996) EMBO J , vol.15 , pp. 5299-5313
    • Hansen, K.1    Johnell, M.2    Siegbahn, A.3    Rorsman, C.4    Engström, U.5    Wernstedt, C.6    Heldin, C.H.7    Rönnstrand, L.8
  • 42
    • 84882894978 scopus 로고    scopus 로고
    • The interaction between pseudopods and extracellular signalling during chemotaxis and directed migration
    • Insall, R. The interaction between pseudopods and extracellular signalling during chemotaxis and directed migration. Curr. Opin. Cell Biol. 2013, 25, 526-531.
    • (2013) Curr. Opin. Cell Biol , vol.25 , pp. 526-531
    • Insall, R.1
  • 43
    • 33748333139 scopus 로고    scopus 로고
    • Live cell imaging of phosphoinositide dynamics with fluorescent protein domains
    • Várnai, P.; Balla, T. Live cell imaging of phosphoinositide dynamics with fluorescent protein domains. Biochim. Biophys. Acta 2006, 1761, 957-967.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 957-967
    • Várnai, P.1    Balla, T.2
  • 45
    • 80052275615 scopus 로고    scopus 로고
    • PI3K/Akt signaling requires spatial compartmentalization in plasma membrane microdomains
    • Gao, X.; Lowry, P.R.; Zhou, X.; Depry, C.; Wei, Z.; Wong, G.W.; Zhang, J. PI3K/Akt signaling requires spatial compartmentalization in plasma membrane microdomains. Proc. Natl. Acad. Sci. USA 2011, 108, 14509-14514.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 14509-14514
    • Gao, X.1    Lowry, P.R.2    Zhou, X.3    Depry, C.4    Wei, Z.5    Wong, G.W.6    Zhang, J.7
  • 46
    • 0035805510 scopus 로고    scopus 로고
    • Monitoring agonist-induced phospholipase C activation in live cells by fluorescence resonance energy transfer
    • Van der Wal, J.; Habets, R.; Várnai, P.; Balla, T.; Jalink, K. Monitoring agonist-induced phospholipase C activation in live cells by fluorescence resonance energy transfer. J. Biol. Chem. 2001, 276, 15337-15344.
    • (2001) J. Biol. Chem , vol.276 , pp. 15337-15344
    • Van Der Wal, J.1    Habets, R.2    Várnai, P.3    Balla, T.4    Jalink, K.5
  • 48
    • 84869021496 scopus 로고    scopus 로고
    • The impact of heterogeneity and dark acceptor states on FRET: Implications for using fluorescent protein donors and acceptors
    • Vogel, S.S.; Nguyen, T.A.; van der Meer, B.W.; Blank, P.S. The impact of heterogeneity and dark acceptor states on FRET: Implications for using fluorescent protein donors and acceptors. PLoS ONE 2012, 7, e49593.
    • (2012) Plos ONE , vol.7
    • Vogel, S.S.1    Nguyen, T.A.2    Van Der Meer, B.W.3    Blank, P.S.4
  • 49
    • 84869044166 scopus 로고    scopus 로고
    • Fluorescence lifetime readouts of troponin-C-based calcium FRET sensors: A quantitative comparison of CFP and mTFP1 as donor fluorophores
    • Laine, R.; Stuckey, D.W.; Manning, H.; Warren, S.C.; Kennedy, G.; Carling, D.; Dunsby, C.; Sardini, A.; French, P.M.W. Fluorescence lifetime readouts of troponin-C-based calcium FRET sensors: A quantitative comparison of CFP and mTFP1 as donor fluorophores. PLoS ONE 2012, 7, e49200.
    • (2012) Plos ONE , vol.7
    • Laine, R.1    Stuckey, D.W.2    Manning, H.3    Warren, S.C.4    Kennedy, G.5    Carling, D.6    Dunsby, C.7    Sardini, A.8    French, P.9
  • 51
    • 80455137048 scopus 로고    scopus 로고
    • DNA multiphoton absorption generates localized damage for studying repair dynamics in live cells
    • Daddysman, M.K.; Fecko, C.J. DNA multiphoton absorption generates localized damage for studying repair dynamics in live cells. Biophys. J. 2011, 101, 2294-2303.
    • (2011) Biophys. J , vol.101 , pp. 2294-2303
    • Daddysman, M.K.1    Fecko, C.J.2
  • 55
    • 0025720541 scopus 로고
    • Maximum likelihood method for the analysis of time-resolved fluorescence decay curves
    • Bajzer, Ž.; Therneau, T.M.; Sharp, J.C.; Prendergast, F.G. Maximum likelihood method for the analysis of time-resolved fluorescence decay curves. Eur. Biophys. J. 1991, 20, 247-262.
    • (1991) Eur. Biophys. J , vol.20 , pp. 247-262
    • Bajzer, Ž.1    Therneau, T.M.2    Sharp, J.C.3    Prendergast, F.G.4
  • 56
  • 57
    • 84936878589 scopus 로고    scopus 로고
    • accessed on 20 November
    • Tsien, R.Y. Tsien Lab Website. Available online: http://http://www.tsienlab.ucsd.edu/ (accessed on 20 November 2014).
    • (2014) Tsien Lab Website
    • Tsien, R.Y.1


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