메뉴 건너뛰기




Volumn 409, Issue 1, 2008, Pages 251-261

Functional complementation of high-efficiency resonance energy transfer: A new tool for the study of protein binding interactions in living cells

Author keywords

arrestin; Bioluminescence; Functional complementation; G protein coupled receptor; Renilla green fluorescent protein (RGFP); Resonance energy transfer

Indexed keywords

BIOASSAY; BIOCHEMISTRY; CELLS; PROTEINS; QUANTUM YIELD;

EID: 38149064653     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070803     Document Type: Article
Times cited : (59)

References (49)
  • 1
    • 84981779372 scopus 로고
    • Zwischenmolekulare energiewanderung und fluoreszenz
    • Förster, T. (1948) Zwischenmolekulare energiewanderung und fluoreszenz. Ann. Physik. 2, 55-75
    • (1948) Ann. Physik , vol.2 , pp. 55-75
    • Förster, T.1
  • 3
    • 0033823060 scopus 로고    scopus 로고
    • The renaissance of fluorescence resonance energy transfer
    • Selvin, P. R. (2000) The renaissance of fluorescence resonance energy transfer. Nat. Struct. Biol. 7, 730-734
    • (2000) Nat. Struct. Biol , vol.7 , pp. 730-734
    • Selvin, P.R.1
  • 4
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. (1998) The green fluorescent protein. Annu. Rev. Biochem. 67, 509-544
    • (1998) Annu. Rev. Biochem , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 5
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • Nguyen, A. W. and Daugherty, P. S. (2005) Evolutionary optimization of fluorescent proteins for intracellular FRET. Nat. Biotechnol. 23, 355-360
    • (2005) Nat. Biotechnol , vol.23 , pp. 355-360
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 6
    • 1542336956 scopus 로고    scopus 로고
    • The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins
    • Verkhusha, V. V. and Lukyanov, K. A. (2004) The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins. Nat. Biotechnol. 22, 289-296
    • (2004) Nat. Biotechnol , vol.22 , pp. 289-296
    • Verkhusha, V.V.1    Lukyanov, K.A.2
  • 7
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • Giepmans, B. N., Adams, S. R., Ellisman, M. H. and Tsien, R. Y. (2006) The fluorescent toolbox for assessing protein location and function. Science 312, 217-224
    • (2006) Science , vol.312 , pp. 217-224
    • Giepmans, B.N.1    Adams, S.R.2    Ellisman, M.H.3    Tsien, R.Y.4
  • 8
    • 0035318509 scopus 로고    scopus 로고
    • Oligomerization of G-protein-coupled transmitter receptors
    • Bouvier, M. (2001) Oligomerization of G-protein-coupled transmitter receptors. Nat. Rev. Neurosci. 2, 274-286
    • (2001) Nat. Rev. Neurosci , vol.2 , pp. 274-286
    • Bouvier, M.1
  • 9
    • 1442309077 scopus 로고    scopus 로고
    • Applications of bioluminescence- and fluorescence resonance energy transfer to drug discovery at G protein-coupled receptors
    • Milligan, G. (2004) Applications of bioluminescence- and fluorescence resonance energy transfer to drug discovery at G protein-coupled receptors. Eur. J. Pharm. Sci. 21, 397-405
    • (2004) Eur. J. Pharm. Sci , vol.21 , pp. 397-405
    • Milligan, G.1
  • 10
    • 13444269196 scopus 로고    scopus 로고
    • Monitoring the formation of dynamic G-protein-coupled receptor-protein complexes in living cells
    • Pfleger, K. D. and Eidne, K. A. (2005) Monitoring the formation of dynamic G-protein-coupled receptor-protein complexes in living cells. Biochem. J. 385, 625-637
    • (2005) Biochem. J , vol.385 , pp. 625-637
    • Pfleger, K.D.1    Eidne, K.A.2
  • 11
    • 33745911922 scopus 로고    scopus 로고
    • Application of bioluminescence resonance energy transfer (BRET) for biomolecular interaction studies
    • Prinz, A., Diskar, M. and Herberg, F. W. (2006) Application of bioluminescence resonance energy transfer (BRET) for biomolecular interaction studies. ChemBioChem 7, 1007-1012
    • (2006) ChemBioChem , vol.7 , pp. 1007-1012
    • Prinz, A.1    Diskar, M.2    Herberg, F.W.3
  • 12
    • 33646343978 scopus 로고    scopus 로고
    • Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET)
    • Pfleger, K. D. and Eidne, K. A. (2006) Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET). Nat. Methods 3, 165-174
    • (2006) Nat. Methods , vol.3 , pp. 165-174
    • Pfleger, K.D.1    Eidne, K.A.2
  • 13
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
    • Xu, Y., Piston, D. W. and Johnson, C. H. (1999) A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins. Proc. Natl. Acad. Sci. U.S.A. 96, 151-156
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 14
    • 24144488192 scopus 로고    scopus 로고
    • High-throughput screening of G protein-coupled receptor antagonists using a bioluminescence resonance energy transfer 1-based β-arrestin2 recruitment assay
    • Hamdan, F. F., Audet, M., Garneau, P., Pelletier, J. and Bouvier, M. (2005) High-throughput screening of G protein-coupled receptor antagonists using a bioluminescence resonance energy transfer 1-based β-arrestin2 recruitment assay. J. Biomol. Screen. 10, 463-475
    • (2005) J. Biomol. Screen , vol.10 , pp. 463-475
    • Hamdan, F.F.1    Audet, M.2    Garneau, P.3    Pelletier, J.4    Bouvier, M.5
  • 15
    • 0000263965 scopus 로고
    • In vitro energy transfer in Renilla bioluminescence
    • Ward, W. W. and Cormier, M. J. (1976) In vitro energy transfer in Renilla bioluminescence. J. Phys. Chem. 80, 2289-2291
    • (1976) J. Phys. Chem , vol.80 , pp. 2289-2291
    • Ward, W.W.1    Cormier, M.J.2
  • 16
    • 0015076612 scopus 로고
    • Energy transfer in a bioluminescent system
    • Morin, J. G. and Hastings, J. W. (1971) Energy transfer in a bioluminescent system. J. Cell. Physiol. 77, 313-318
    • (1971) J. Cell. Physiol , vol.77 , pp. 313-318
    • Morin, J.G.1    Hastings, J.W.2
  • 18
    • 0016156057 scopus 로고
    • Intermolecular energy transfer in the bioluminescent system of Aequorea
    • Morise, H., Shimomura, O., Johnson, F. H. and Winant, J. (1974) Intermolecular energy transfer in the bioluminescent system of Aequorea. Biochemistry 13, 2656-2662
    • (1974) Biochemistry , vol.13 , pp. 2656-2662
    • Morise, H.1    Shimomura, O.2    Johnson, F.H.3    Winant, J.4
  • 19
    • 0001605659 scopus 로고
    • Structure and chemical synthesis of a biologically active form of Renilla (sea pansy) Luciferin
    • Hori, K. and Cormier, M. J. (1973) Structure and chemical synthesis of a biologically active form of Renilla (sea pansy) Luciferin. Proc. Natl. Acad. Sci. U.S.A. 70, 120-123
    • (1973) Proc. Natl. Acad. Sci. U.S.A , vol.70 , pp. 120-123
    • Hori, K.1    Cormier, M.J.2
  • 20
    • 0015233810 scopus 로고
    • Structured bioluminescence. Two emitters during both the in vitro and the in vivo bioluminescence of the sea pansy, Renilla
    • Wampler, J. E., Hori, K., Lee, J. W. and Cormier, M. J. (1971) Structured bioluminescence. Two emitters during both the in vitro and the in vivo bioluminescence of the sea pansy, Renilla. Biochemistry 10, 2903-2909
    • (1971) Biochemistry , vol.10 , pp. 2903-2909
    • Wampler, J.E.1    Hori, K.2    Lee, J.W.3    Cormier, M.J.4
  • 21
    • 0018786147 scopus 로고
    • An energy transfer protein in coelenterate bioluminescence. Characterization of the Renilla green-fluorescent protein
    • Ward, W. W. and Cormier, M. J. (1979) An energy transfer protein in coelenterate bioluminescence. Characterization of the Renilla green-fluorescent protein. J. Biol. Chem. 254, 781-788
    • (1979) J. Biol. Chem , vol.254 , pp. 781-788
    • Ward, W.W.1    Cormier, M.J.2
  • 22
    • 0018803836 scopus 로고
    • Renilla reniformis bioluminescence: Luciferase-catalyzed production of nonradiating excited states from luciferin analogues and elucidation of the excited state species involved in energy transfer to Renilla green fluorescent protein
    • Hart, R. C., Matthews, J. C., Hori, K. and Cormier, M. J. (1979) Renilla reniformis bioluminescence: luciferase-catalyzed production of nonradiating excited states from luciferin analogues and elucidation of the excited state species involved in energy transfer to Renilla green fluorescent protein. Biochemistry 18, 2204-2210
    • (1979) Biochemistry , vol.18 , pp. 2204-2210
    • Hart, R.C.1    Matthews, J.C.2    Hori, K.3    Cormier, M.J.4
  • 23
    • 84981578054 scopus 로고
    • Energy transfer via protein-protein interaction in Renilla bioluminescence
    • Ward, W. W. and Cormier, M. J. (1978) Energy transfer via protein-protein interaction in Renilla bioluminescence. Photochem. Photobiol. 27, 389-396
    • (1978) Photochem. Photobiol , vol.27 , pp. 389-396
    • Ward, W.W.1    Cormier, M.J.2
  • 24
    • 0025212680 scopus 로고
    • Regions of the α1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function
    • Cotecchia, S., Exum, S., Caron, M. G. and Lefkowitz, R. J. (1990) Regions of the α1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function. Proc. Natl. Acad. Sci. U.S.A. 87, 2896-2900
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 2896-2900
    • Cotecchia, S.1    Exum, S.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 25
    • 0038521270 scopus 로고    scopus 로고
    • Promiscuous coupling at receptor-Gα fusion proteins. The receptor of one covalent complex interacts with the alpha-subunit of another
    • Molinari, P., Ambrosio, C., Riitano, D., Sbraccia, M., Gro, M. C. and Costa, T. (2003) Promiscuous coupling at receptor-Gα fusion proteins. The receptor of one covalent complex interacts with the alpha-subunit of another. J. Biol. Chem. 278, 15778-15788
    • (2003) J. Biol. Chem , vol.278 , pp. 15778-15788
    • Molinari, P.1    Ambrosio, C.2    Riitano, D.3    Sbraccia, M.4    Gro, M.C.5    Costa, T.6
  • 26
    • 0020669405 scopus 로고
    • Determination of total protein
    • Peterson, G. (1983) Determination of total protein. Methods Enzymol. 91, 95-119
    • (1983) Methods Enzymol , vol.91 , pp. 95-119
    • Peterson, G.1
  • 27
    • 38149071352 scopus 로고
    • Resolution of overlapping bands: Functions for simulating band shapes
    • Fraser, R. D. B. and Suzuki, E. (1969) Resolution of overlapping bands: functions for simulating band shapes. Anal. Chem. 41, 171-173
    • (1969) Anal. Chem , vol.41 , pp. 171-173
    • Fraser, R.D.B.1    Suzuki, E.2
  • 28
    • 33947087376 scopus 로고
    • Analytical moments of skewed Gaussian distribution functions
    • Rusch, P. F. and Lelieur, J. P. (1973) Analytical moments of skewed Gaussian distribution functions. Anal. Chem. 45, 1541-1543
    • (1973) Anal. Chem , vol.45 , pp. 1541-1543
    • Rusch, P.F.1    Lelieur, J.P.2
  • 29
    • 0034647238 scopus 로고    scopus 로고
    • Antiparallel leucine zipper-directed protein reassembly: Application to the green fluorescent protein
    • Ghosh, I., Hamilton, A. D. and Regan, L. (2000) Antiparallel leucine zipper-directed protein reassembly: application to the green fluorescent protein. J. Am. Chem. Soc. 122, 5658-5659
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 5658-5659
    • Ghosh, I.1    Hamilton, A.D.2    Regan, L.3
  • 30
    • 11844252081 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: Scope and mechanism
    • Magliery, T. J., Wilson, C. G., Pan, W., Mishler, D., Ghosh, I., Hamilton, A. D. and Regan, L. (2005) Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism. J. Am. Chem. Soc. 127, 146-157
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 146-157
    • Magliery, T.J.1    Wilson, C.G.2    Pan, W.3    Mishler, D.4    Ghosh, I.5    Hamilton, A.D.6    Regan, L.7
  • 31
    • 0029026320 scopus 로고
    • Determinants of thrombin receptor cleavage. Receptor domains involved, specificity, and role of the P3 aspartate
    • Ishii, K., Gerszten, R., Zheng, Y. W., Welsh, J. B., Turck, C. W. and Coughlin, S. R. (1995) Determinants of thrombin receptor cleavage. Receptor domains involved, specificity, and role of the P3 aspartate. J. Biol. Chem. 270, 16435-16440
    • (1995) J. Biol. Chem , vol.270 , pp. 16435-16440
    • Ishii, K.1    Gerszten, R.2    Zheng, Y.W.3    Welsh, J.B.4    Turck, C.W.5    Coughlin, S.R.6
  • 32
    • 0034595860 scopus 로고    scopus 로고
    • Differential affinities of visual arrestin, β-arrestin1, and β-arrestin2 for G protein-coupled receptors delineate two major classes of receptors
    • Oakley, R. H., Laporte, S. A., Holt, J. A., Caron, M. G. and Barak, L. S. (2000) Differential affinities of visual arrestin, β-arrestin1, and β-arrestin2 for G protein-coupled receptors delineate two major classes of receptors. J. Biol. Chem. 275, 17201-17210
    • (2000) J. Biol. Chem , vol.275 , pp. 17201-17210
    • Oakley, R.H.1    Laporte, S.A.2    Holt, J.A.3    Caron, M.G.4    Barak, L.S.5
  • 33
    • 0034724192 scopus 로고    scopus 로고
    • Detection of β2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • Angers, S., Salahpour, A., Joly, E., Hilairet, S., Chelsky, D., Dennis, M. and Bouvier, M. (2000) Detection of β2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl. Acad. Sci. U.S.A. 97, 3684-3689
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 3684-3689
    • Angers, S.1    Salahpour, A.2    Joly, E.3    Hilairet, S.4    Chelsky, D.5    Dennis, M.6    Bouvier, M.7
  • 34
    • 2542437470 scopus 로고    scopus 로고
    • Development of a BRET2 screening assay using β-arrestin 2 mutants
    • Vrecl, M., Jorgensen, R., Pogacnik, A. and Heding, A. (2004) Development of a BRET2 screening assay using β-arrestin 2 mutants. J. Biomol. Screen. 9, 322-333
    • (2004) J. Biomol. Screen , vol.9 , pp. 322-333
    • Vrecl, M.1    Jorgensen, R.2    Pogacnik, A.3    Heding, A.4
  • 35
    • 0015935504 scopus 로고
    • Lumisomes, the cellular site of bioluminescence in coelenterates
    • Anderson, J. M. and Cormier, M. J. (1973) Lumisomes, the cellular site of bioluminescence in coelenterates. J. Biol. Chem. 248, 2937-2943
    • (1973) J. Biol. Chem , vol.248 , pp. 2937-2943
    • Anderson, J.M.1    Cormier, M.J.2
  • 36
    • 0035140197 scopus 로고    scopus 로고
    • A study of protein-protein interaction in living cells using luminescence resonance energy transfer (LRET) from Renilla luciferase to Aequorea GFP
    • Wang, Y., Wang, G., O'Kane, D. J. and Szalay, A. A. (2001) A study of protein-protein interaction in living cells using luminescence resonance energy transfer (LRET) from Renilla luciferase to Aequorea GFP. Mol. Gen. Genet. 264, 578-587
    • (2001) Mol. Gen. Genet , vol.264 , pp. 578-587
    • Wang, Y.1    Wang, G.2    O'Kane, D.J.3    Szalay, A.A.4
  • 37
    • 0035984722 scopus 로고    scopus 로고
    • β-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions
    • Galarneau, A., Primeau, M., Trudeau, L. E. and Michnick, S. W. (2002) β-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions. Nat. Biotechnol. 20, 619-622
    • (2002) Nat. Biotechnol , vol.20 , pp. 619-622
    • Galarneau, A.1    Primeau, M.2    Trudeau, L.E.3    Michnick, S.W.4
  • 38
    • 14744281422 scopus 로고    scopus 로고
    • Firefly luciferase enzyme fragment complementation for imaging in cells and living animals
    • Paulmurugan, R. and Gambhir, S. S. (2005) Firefly luciferase enzyme fragment complementation for imaging in cells and living animals. Anal. Chem. 77, 1295-1302
    • (2005) Anal. Chem , vol.77 , pp. 1295-1302
    • Paulmurugan, R.1    Gambhir, S.S.2
  • 39
    • 13244296604 scopus 로고    scopus 로고
    • Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein
    • Cabantous, S., Terwilliger, T. C. and Waldo, G. S. (2005) Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nat. Biotechnol. 23, 102-107
    • (2005) Nat. Biotechnol , vol.23 , pp. 102-107
    • Cabantous, S.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 40
    • 18144394763 scopus 로고    scopus 로고
    • Capturing protein interactions in the secretory pathway of living cells
    • Nyfeler, B., Michnick, S. W. and Hauri, H. P. (2005) Capturing protein interactions in the secretory pathway of living cells. Proc. Natl. Acad. Sci. U.S.A. 102, 6350-6355
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 6350-6355
    • Nyfeler, B.1    Michnick, S.W.2    Hauri, H.P.3
  • 41
    • 0033197614 scopus 로고    scopus 로고
    • Cameleon calcium indicator reports cytoplasmic calcium dynamics in Arabidopsis guard cells
    • Allen, G. J., Kwak, J. M., Chu, S. P., Llopis, J., Tsien, R. Y., Harper, J. F. and Schroeder, J. I. (1999) Cameleon calcium indicator reports cytoplasmic calcium dynamics in Arabidopsis guard cells. Plant J. 19, 735-747
    • (1999) Plant J , vol.19 , pp. 735-747
    • Allen, G.J.1    Kwak, J.M.2    Chu, S.P.3    Llopis, J.4    Tsien, R.Y.5    Harper, J.F.6    Schroeder, J.I.7
  • 44
    • 4444377903 scopus 로고    scopus 로고
    • Novel single chain cAMP sensors for receptor-induced signal propagation
    • Nikolaev, V. O., Bunemann, M., Hein, L., Hannawacker, A. and Lohse, M. J. (2004) Novel single chain cAMP sensors for receptor-induced signal propagation. J. Biol. Chem. 279, 37215-37218
    • (2004) J. Biol. Chem , vol.279 , pp. 37215-37218
    • Nikolaev, V.O.1    Bunemann, M.2    Hein, L.3    Hannawacker, A.4    Lohse, M.J.5
  • 46
    • 0035424506 scopus 로고    scopus 로고
    • Measurement of proteases using chemiluminescence-resonance-energy-transfer chimaeras between green fluorescent protein and aequorin
    • Waud, J. P., Bermudez Fajardo, A., Sudhaharan, T., Trimby, A. R., Jeffery, J., Jones, A. and Campbell, A. K. (2001) Measurement of proteases using chemiluminescence-resonance-energy-transfer chimaeras between green fluorescent protein and aequorin. Biochem. J. 357, 687-697
    • (2001) Biochem. J , vol.357 , pp. 687-697
    • Waud, J.P.1    Bermudez Fajardo, A.2    Sudhaharan, T.3    Trimby, A.R.4    Jeffery, J.5    Jones, A.6    Campbell, A.K.7
  • 47
    • 33748101201 scopus 로고    scopus 로고
    • Consensus guided mutagenesis of Renilla luciferase yields enhanced stability and light output
    • Loening, A. M., Fenn, T. D., Wu, A. M. and Gambhir, S. S. (2006) Consensus guided mutagenesis of Renilla luciferase yields enhanced stability and light output. Protein Eng. Des. Sel. 19, 391-400
    • (2006) Protein Eng. Des. Sel , vol.19 , pp. 391-400
    • Loening, A.M.1    Fenn, T.D.2    Wu, A.M.3    Gambhir, S.S.4
  • 48
    • 33751215258 scopus 로고    scopus 로고
    • A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer
    • James, J. R., Oliveira, M. I., Carmo, A. M., Iaboni, A. and Davis, S. J. (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    Carmo, A.M.3    Iaboni, A.4    Davis, S.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.