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Volumn 100, Issue 2, 2011, Pages 361-368

Organization of higher-order oligomers of the serotonin1A receptor explored utilizing homo-FRET in live cells

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EID: 78751700316     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.12.3692     Document Type: Article
Times cited : (82)

References (43)
  • 1
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum, D. M., S. G. F. Rasmussen, and B. K. Kobilka. 2009. The structure and function of G-protein-coupled receptors. Nature. 459:356-363.
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.F.2    Kobilka, B.K.3
  • 2
    • 61649096359 scopus 로고    scopus 로고
    • G-protein-coupled receptorfocused drug discovery using a target class platform approach
    • Heilker, R., M. Wolff,..., M. Bieler. 2009. G-protein-coupled receptorfocused drug discovery using a target class platform approach. Drug Discov. Today. 14:231-240.
    • (2009) Drug Discov. Today , vol.14 , pp. 231-240
    • Heilker, R.1    Wolff, M.2    Bieler, M.3
  • 3
    • 18044362857 scopus 로고    scopus 로고
    • The serotonin1A receptor: A representative member of the serotonin receptor family
    • Pucadyil, T. J., S. Kalipatnapu, and A. Chattopadhyay. 2005. The serotonin1A receptor: a representative member of the serotonin receptor family. Cell. Mol. Neurobiol. 25:553-580.
    • (2005) Cell. Mol. Neurobiol. , vol.25 , pp. 553-580
    • Pucadyil, T.J.1    Kalipatnapu, S.2    Chattopadhyay, A.3
  • 4
    • 3342944219 scopus 로고    scopus 로고
    • A new paradigm in the functioning of G-protein-coupled receptors
    • Shanti, K., and A. Chattopadhyay. 2000. A new paradigm in the functioning of G-protein-coupled receptors. Curr. Sci. 79:402-403.
    • (2000) Curr. Sci. , vol.79 , pp. 402-403
    • Shanti, K.1    Chattopadhyay, A.2
  • 5
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization: An emerging concept for G protein-coupled receptor ontogeny and function
    • Angers, S., A. Salahpour, and M. Bouvier. 2002. Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function. Annu. Rev. Pharmacol. Toxicol. 42:409-435.
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 409-435
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 6
    • 10844255797 scopus 로고    scopus 로고
    • Oligomerization of G protein-coupled receptors: Past, present, and future
    • Park, P. S., S. Filipek,..., K. Palczewski. 2004. Oligomerization of G protein-coupled receptors: past, present, and future. Biochemistry. 43:15643-15656.
    • (2004) Biochemistry , vol.43 , pp. 15643-15656
    • Park, P.S.1    Filipek, S.2    Palczewski, K.3
  • 7
    • 33947369500 scopus 로고    scopus 로고
    • G protein-coupled receptor dimerisation: Molecular basis and relevance to function
    • Milligan, G. 2007. G protein-coupled receptor dimerisation: molecular basis and relevance to function. Biochim. Biophys. Acta. 1768:825-835.
    • (2007) Biochim. Biophys. Acta. , vol.1768 , pp. 825-835
    • Milligan, G.1
  • 8
    • 72449147362 scopus 로고    scopus 로고
    • Dimerization in GPCR mobility and signaling
    • Lohse, M. J. 2010. Dimerization in GPCR mobility and signaling. Curr. Opin. Pharmacol. 10:53-58.
    • (2010) Curr. Opin. Pharmacol. , vol.10 , pp. 53-58
    • Lohse, M.J.1
  • 9
    • 0036780743 scopus 로고    scopus 로고
    • G-protein-coupled receptor oligomerization and its potential for drug discovery
    • George, S. R., B. F. O'Dowd, and S. P. Lee. 2002. G-protein-coupled receptor oligomerization and its potential for drug discovery. Nat. Rev. Drug Discov. 1:808-820.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 808-820
    • George, S.R.1    O'Dowd, B.F.2    Lee, S.P.3
  • 10
    • 33751215258 scopus 로고    scopus 로고
    • A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer
    • James, J. R., M. I. Oliveira,..., S. J. Davis. 2006. A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer. Nat. Methods. 3:1001-1006.
    • (2006) Nat. Methods , vol.3 , pp. 1001-1006
    • James, J.R.1    Oliveira, M.I.2    Davis, S.J.3
  • 11
    • 33144473025 scopus 로고    scopus 로고
    • FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells
    • Meyer, B. H., J.-M. Segura,..., H. Vogel. 2006. FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells. Proc. Natl. Acad. Sci. USA. 103:2138-2143.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2138-2143
    • Meyer, B.H.1    Segura, J.-M.2    Vogel, H.3
  • 12
    • 12244271469 scopus 로고    scopus 로고
    • Homo-FRET versus hetero-FRET to probe homodimers in living cells
    • Tramier, M., T. Piolot,..., M. Coppey-Moisan. 2003. Homo-FRET versus hetero-FRET to probe homodimers in living cells. Methods Enzymol. 360:580-597.
    • (2003) Methods Enzymol. , vol.360 , pp. 580-597
    • Tramier, M.1    Piolot, T.2    Coppey-Moisan, M.3
  • 13
    • 0029117442 scopus 로고
    • Theory and application of fluorescence homotransfer to melittin oligomerization
    • Runnels, L. W., and S. F. Scarlata. 1995. Theory and application of fluorescence homotransfer to melittin oligomerization. Biophys. J. 69:1569-1583.
    • (1995) Biophys. J. , vol.69 , pp. 1569-1583
    • Runnels, L.W.1    Scarlata, S.F.2
  • 14
    • 34247599842 scopus 로고    scopus 로고
    • Enumeration of oligomerization states of membrane proteins in living cells by homo-FRET spectroscopy and microscopy: Theory and application
    • Yeow, E. K. L., and A. H. A. Clayton. 2007. Enumeration of oligomerization states of membrane proteins in living cells by homo-FRET spectroscopy and microscopy: theory and application. Biophys. J. 92:3098-3104.
    • (2007) Biophys. J. , vol.92 , pp. 3098-3104
    • Yeow, E.K.L.1    Clayton, A.H.A.2
  • 15
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma, R., and S. Mayor. 1998. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature. 394:798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 16
    • 1942438090 scopus 로고    scopus 로고
    • Suppression of photobleaching-induced artifacts in frequency-domain FLIM by permutation of the recording order
    • van Munster, E. B., and T. W. J. Gadella, Jr. 2004. Suppression of photobleaching-induced artifacts in frequency-domain FLIM by permutation of the recording order. Cytometry A. 58:185-194.
    • (2004) Cytometry A , vol.58 , pp. 185-194
    • Van Munster, E.B.1    Gadella Jr., T.W.J.2
  • 17
    • 0000469474 scopus 로고    scopus 로고
    • Solvent dependence of the fluorescence lifetimes of xanthene dyes
    • Magde, D., G. E. Rojas, and P. G. Seybold. 1999. Solvent dependence of the fluorescence lifetimes of xanthene dyes. Photochem. Photobiol. 70:737-744.
    • (1999) Photochem. Photobiol. , vol.70 , pp. 737-744
    • Magde, D.1    Rojas, G.E.2    Seybold, P.G.3
  • 18
    • 0036708469 scopus 로고    scopus 로고
    • Dynamic fluorescence anisotropy imaging microscopy in the frequency domain (rFLIM)
    • Clayton, A. H. A., Q. S. Hanley,..., T. M. Jovin. 2002. Dynamic fluorescence anisotropy imaging microscopy in the frequency domain (rFLIM). Biophys. J. 83:1631-1649.
    • (2002) Biophys. J. , vol.83 , pp. 1631-1649
    • Clayton, A.H.A.1    Hanley, Q.S.2    Jovin, T.M.3
  • 20
    • 0142184429 scopus 로고    scopus 로고
    • Imaging molecular interactions in cells by dynamic and static fluorescence anisotropy (rFLIM and emFRET)
    • Lidke, D. S., P. Nagy,..., T. M. Jovin. 2003. Imaging molecular interactions in cells by dynamic and static fluorescence anisotropy (rFLIM and emFRET). Biochem. Soc. Trans. 31:1020-1027.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1020-1027
    • Lidke, D.S.1    Nagy, P.2    Jovin, T.M.3
  • 21
    • 0034633010 scopus 로고    scopus 로고
    • Förster distances between green fluorescent protein pairs
    • Patterson, G. H., D. W. Piston, and B. G. Barisas. 2000. Förster distances between green fluorescent protein pairs. Anal. Biochem. 284:438-440.
    • (2000) Anal. Biochem. , vol.284 , pp. 438-440
    • Patterson, G.H.1    Piston, D.W.2    Barisas, B.G.3
  • 22
    • 18644377743 scopus 로고    scopus 로고
    • Effects of refractive index and viscosity on fluorescence and anisotropy decays of enhanced cyan and yellow fluorescent proteins
    • Borst, J. W., M. A. Hink,..., A. J. Visser. 2005. Effects of refractive index and viscosity on fluorescence and anisotropy decays of enhanced cyan and yellow fluorescent proteins. J. Fluoresc. 15:153-160.
    • (2005) J. Fluoresc , vol.15 , pp. 153-160
    • Borst, J.W.1    Hink, M.A.2    Visser, A.J.3
  • 23
    • 0037763890 scopus 로고    scopus 로고
    • Intrasequence GFP in class I MHC molecules, a rigid probe for fluorescence anisotropy measurements of the membrane environment
    • Rocheleau, J. V., M. Edidin, and D. W. Piston. 2003. Intrasequence GFP in class I MHC molecules, a rigid probe for fluorescence anisotropy measurements of the membrane environment. Biophys. J. 84:4078-4086.
    • (2003) Biophys. J. , vol.84 , pp. 4078-4086
    • Rocheleau, J.V.1    Edidin, M.2    Piston, D.W.3
  • 24
    • 0034625458 scopus 로고    scopus 로고
    • Structural dynamics of green fluorescent protein alone and fused with a single chain Fv protein
    • Hink, M. A., R. A. Griep,..., A. J. Visser. 2000. Structural dynamics of green fluorescent protein alone and fused with a single chain Fv protein. J. Biol. Chem. 275:17556-17560.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17556-17560
    • Hink, M.A.1    Griep, R.A.2    Visser, A.J.3
  • 25
    • 37249047410 scopus 로고    scopus 로고
    • Anomalous negative fluorescence anisotropy in yellow fluorescent protein (YFP 10C): Quantitative analysis of FRET in YFP dimers
    • Shi, X., J. Basran,..., S. G. Boxer. 2007. Anomalous negative fluorescence anisotropy in yellow fluorescent protein (YFP 10C): quantitative analysis of FRET in YFP dimers. Biochemistry. 46:14403-14417.
    • (2007) Biochemistry , vol.46 , pp. 14403-14417
    • Shi, X.1    Basran, J.2    Boxer, S.G.3
  • 26
    • 72249114997 scopus 로고    scopus 로고
    • Homo-FRET imaging enables quantification of protein cluster sizes with subcellular resolution
    • Bader, A. N., E. G. Hofman,..., H. C. Gerritsen. 2009. Homo-FRET imaging enables quantification of protein cluster sizes with subcellular resolution. Biophys. J. 97:2613-2622.
    • (2009) Biophys. J. , vol.97 , pp. 2613-2622
    • Bader, A.N.1    Hofman, E.G.2    Gerritsen, H.C.3
  • 27
    • 0018389150 scopus 로고
    • Carbocyanine dye orientation in red cell membrane studied by microscopic fluorescence polarization
    • Axelrod, D. 1979. Carbocyanine dye orientation in red cell membrane studied by microscopic fluorescence polarization. Biophys. J. 26:557-573.
    • (1979) Biophys. J. , vol.26 , pp. 557-573
    • Axelrod, D.1
  • 28
    • 37249032741 scopus 로고    scopus 로고
    • FRET by fluorescence polarization microscopy
    • Piston, D. W., and M. A. Rizzo. 2008. FRET by fluorescence polarization microscopy. Methods Cell Biol. 85:415-430.
    • (2008) Methods Cell. Biol. , vol.85 , pp. 415-430
    • Piston, D.W.1    Rizzo, M.A.2
  • 29
    • 23044445764 scopus 로고    scopus 로고
    • 2 adrenoceptor in detergent micelles
    • 2 adrenoceptor in detergent micelles. Anal. Biochem. 343:344-346.
    • (2005) Anal. Biochem. , vol.343 , pp. 344-346
    • Yao, Z.1    Kobilka, B.2
  • 34
    • 0001363954 scopus 로고
    • Time-resolved fluorescence techniques: Methods and applications in biology
    • Prendergast, F. G. 1991. Time-resolved fluorescence techniques: methods and applications in biology. Curr. Opin. Struct. Biol. 1:1054-1059.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 1054-1059
    • Prendergast, F.G.1
  • 35
    • 58149469939 scopus 로고    scopus 로고
    • Membrane lipid domains and rafts: Current applications of fluorescence lifetime spectroscopy and imaging
    • de Almeida, R. F., L. M. Loura, and M. Prieto. 2009. Membrane lipid domains and rafts: current applications of fluorescence lifetime spectroscopy and imaging. Chem. Phys. Lipids. 157:61-77.
    • (2009) Chem. Phys. Lipids , vol.157 , pp. 61-77
    • De Almeida, R.F.1    Loura, L.M.2    Prieto, M.3
  • 37
    • 38349093022 scopus 로고    scopus 로고
    • Dipolar relaxation within the protein matrix of the green fluorescent protein: A red edge excitation shift study
    • Haldar, S., and A. Chattopadhyay. 2007. Dipolar relaxation within the protein matrix of the green fluorescent protein: a red edge excitation shift study. J. Phys. Chem. B. 111:14436-14439.
    • (2007) J. Phys. Chem. B. , vol.111 , pp. 14436-14439
    • Haldar, S.1    Chattopadhyay, A.2
  • 38
    • 0037013265 scopus 로고    scopus 로고
    • Oligomerization of G-protein-coupled receptors shown by selective co-immunoprecipitation
    • Salim, K., T. Fenton,..., P. C. Guest. 2002. Oligomerization of G-protein-coupled receptors shown by selective co-immunoprecipitation. J. Biol. Chem. 277:15482-15485.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15482-15485
    • Salim, K.1    Fenton, T.2    Guest, P.C.3
  • 41
    • 57249084132 scopus 로고    scopus 로고
    • Predominance of activated EGFR higher-order oligomers on the cell surface
    • Clayton, A. H. A., S. G. Orchard,..., A. W. Burgess. 2008. Predominance of activated EGFR higher-order oligomers on the cell surface. Growth Factors. 26:316-324.
    • (2008) Growth Factors , vol.26 , pp. 316-324
    • Clayton, A.H.A.1    Orchard, S.G.2    Burgess, A.W.3
  • 43
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: At a crossroad between cell biology and physics
    • Jacobson, K., O. G. Mouritsen, and R. G. W. Anderson. 2007. Lipid rafts: at a crossroad between cell biology and physics. Nat. Cell Biol. 9:7-14.
    • (2007) Nat. Cell. Biol. , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.W.3


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