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Volumn 3, Issue 12, 2006, Pages 1001-1006

A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID; BETA 2 ADRENERGIC RECEPTOR; DIMER; G PROTEIN COUPLED RECEPTOR; LUCIFERASE; MEMBRANE PROTEIN; MONOMER; OLIGOMER;

EID: 33751215258     PISSN: 15487091     EISSN: 15491676     Source Type: Journal    
DOI: 10.1038/nmeth978     Document Type: Article
Times cited : (274)

References (29)
  • 1
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
    • Xu, Y., Piston, D.W. & Johnson, C.H. A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins. Proc. Natl. Acad. Sci. USA 96, 151-156 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 2
    • 0018650688 scopus 로고
    • An analytic solution to the Forster energy transfer problem in two dimensions
    • Wolber, P.K. & Hudson, B.S. An analytic solution to the Forster energy transfer problem in two dimensions. Biophys. J. 28, 197-210 (1979).
    • (1979) Biophys. J. , vol.28 , pp. 197-210
    • Wolber, P.K.1    Hudson, B.S.2
  • 3
    • 0018278640 scopus 로고
    • Surface density determination in membranes by fluorescence energy transfer
    • Fung, B.K. & Stryer, L. Surface density determination in membranes by fluorescence energy transfer. Biochemistry 17, 5241-5248 (1978).
    • (1978) Biochemistry , vol.17 , pp. 5241-5248
    • Fung, B.K.1    Stryer, L.2
  • 4
    • 0017389386 scopus 로고
    • The dimeric nature of the gramicidin A transmembrane channel: Conductance and flourescence energy transfer studies of hybrid channels
    • Veatch, W. & Stryer, L. The dimeric nature of the gramicidin A transmembrane channel: Conductance and flourescence energy transfer studies of hybrid channels. J. Mol. Biol. 133, 89-102 (1977).
    • (1977) J. Mol. Biol. , vol.133 , pp. 89-102
    • Veatch, W.1    Stryer, L.2
  • 5
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 A using imaging flourescence resonance energy transfer
    • Kenworthy, A.K. & Edidin, M. Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 A using imaging flourescence resonance energy transfer. J. Cell Biol. 142, 69-84 (1998).
    • (1998) J. Cell Biol. , vol.142 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 6
    • 13444269196 scopus 로고    scopus 로고
    • Monitoring the formation of dynamic G-protein-coupled receptor-protein complexes in living cells
    • Pfleger, K.D. & Eidne, K.A. Monitoring the formation of dynamic G-protein-coupled receptor-protein complexes in living cells. Biochem. J. 385, 625-637 (2005).
    • (2005) Biochem. J. , vol.385 , pp. 625-637
    • Pfleger, K.D.1    Eidne, K.A.2
  • 7
    • 0026488252 scopus 로고
    • Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2
    • Jones, E.Y., Davis, S.J., Williams, A.F., Harlos, K. & Stuart, D.I. Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2. Nature 360, 232-239 (1992).
    • (1992) Nature , vol.360 , pp. 232-239
    • Jones, E.Y.1    Davis, S.J.2    Williams, A.F.3    Harlos, K.4    Stuart, D.I.5
  • 8
    • 0028774038 scopus 로고
    • Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution
    • Bodian, D.L., Jones, E.Y., Harlos, K., Stuart, D.I. & Davis, S.J. Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution. Structure 2, 755-766 (1994).
    • (1994) Structure , vol.2 , pp. 755-766
    • Bodian, D.L.1    Jones, E.Y.2    Harlos, K.3    Stuart, D.I.4    Davis, S.J.5
  • 9
    • 0036669785 scopus 로고    scopus 로고
    • The interaction properties of costimulatory molecules revisited
    • Collins, A.V. et al. The interaction properties of costimulatory molecules revisited. Immunity 17, 201-210 (2002).
    • (2002) Immunity , vol.17 , pp. 201-210
    • Collins, A.V.1
  • 10
    • 0033971597 scopus 로고    scopus 로고
    • Structure and dimerization of a soluble form of B7-1
    • Ikemizu, S. et al. Structure and dimerization of a soluble form of B7-1. Immunity 12, 51-60 (2000).
    • (2000) Immunity , vol.12 , pp. 51-60
    • Ikemizu, S.1
  • 11
    • 0035967146 scopus 로고    scopus 로고
    • Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses
    • Stamper, C.C. et al. Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses. Nature 410, 608-611 (2001).
    • (2001) Nature , vol.410 , pp. 608-611
    • Stamper, C.C.1
  • 13
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner, N.C. et al. Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 22, 1567-1572 (2004).
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1567-1572
    • Shaner, N.C.1
  • 14
    • 0037160105 scopus 로고    scopus 로고
    • Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • Mercier, J.F., Salahpour, A., Angers, S., Breit, A. & Bouvier, M. Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer. J. Biol. Chem. 277, 44925-44931 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 44925-44931
    • Mercier, J.F.1    Salahpour, A.2    Angers, S.3    Breit, A.4    Bouvier, M.5
  • 15
    • 27344439984 scopus 로고    scopus 로고
    • Different cell surface oligomeric states of B7-1 and B7-2: Implications for signaling
    • Bhatia, S., Edidin, M., Almo, S.C. & Nathenson, S.G. Different cell surface oligomeric states of B7-1 and B7-2: Implications for signaling. Proc. Natl. Acad. Sci. USA 102, 15569-15574 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15569-15574
    • Bhatia, S.1    Edidin, M.2    Almo, S.C.3    Nathenson, S.G.4
  • 16
    • 0034724192 scopus 로고    scopus 로고
    • Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • Angers, S. et al. Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl. Acad. Sci. USA 97, 3684-3689 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3684-3689
    • Angers, S.1
  • 17
    • 0037101774 scopus 로고    scopus 로고
    • Homo- and hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): Hetero-oligomers between receptors subtypes form more efficiently than between less closely related sequences
    • Ramsay, D., Kellett, E., McVey, M., Rees, S. & Milligan, G. Homo- and hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): Hetero-oligomers between receptors subtypes form more efficiently than between less closely related sequences. Biochem. J. 365, 429-440 (2002).
    • (2002) Biochem. J. , vol.365 , pp. 429-440
    • Ramsay, D.1    Kellett, E.2    McVey, M.3    Rees, S.4    Milligan, G.5
  • 18
    • 0026608605 scopus 로고
    • Solubilization and molecular characterization of active galamin receptors from rat brain
    • Chen, Y., Couvinea, A., Laburthe, M. & Amiranoff, B. Solubilization and molecular characterization of active galamin receptors from rat brain. Biochemistry 31, 2415-2422 (1992).
    • (1992) Biochemistry , vol.31 , pp. 2415-2422
    • Chen, Y.1    Couvinea, A.2    Laburthe, M.3    Amiranoff, B.4
  • 19
    • 17444380779 scopus 로고    scopus 로고
    • Heterodimerization is required for the formation of a functional GABA(B) receptor
    • White, J.H. et al. Heterodimerization is required for the formation of a functional GABA(B) receptor. Nature 396, 679-682 (1998).
    • (1998) Nature , vol.396 , pp. 679-682
    • White, J.H.1
  • 20
    • 0005169503 scopus 로고    scopus 로고
    • GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2
    • Jones, K.A. et al. GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2. Nature 396, 674-679 (1998).
    • (1998) Nature , vol.396 , pp. 674-679
    • Jones, K.A.1
  • 21
    • 0942265965 scopus 로고    scopus 로고
    • Homodimerization of adenosine A2A receptors: Qualitative and quantitative assessment by fluorescence and bioluminescence energy transfer
    • Canals, M. et al. Homodimerization of adenosine A2A receptors: qualitative and quantitative assessment by fluorescence and bioluminescence energy transfer. J. Neurochem. 88, 726-734 (2004).
    • (2004) J. Neurochem. , vol.88 , pp. 726-734
    • Canals, M.1
  • 22
    • 0344875553 scopus 로고    scopus 로고
    • Adenosine A2A-dopamine D2 receptor-receptor heteromerization: Qualitative and quantitative assessment by fluorescence and bioluminescence energy transfer
    • Canals, M. et al. Adenosine A2A-dopamine D2 receptor-receptor heteromerization: Qualitative and quantitative assessment by fluorescence and bioluminescence energy transfer. J. Biol. Chem. 278, 46741-46749 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 46741-46749
    • Canals, M.1
  • 23
    • 15444377047 scopus 로고    scopus 로고
    • Bioluminescence resonance energy transfer reveals ligand-induced conformational changes in CXCR4 homo- and heterodimers
    • Percherancier, Y. et al. Bioluminescence resonance energy transfer reveals ligand-induced conformational changes in CXCR4 homo- and heterodimers. J. Biol. Chem. 280, 9895-9903 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 9895-9903
    • Percherancier, Y.1
  • 24
    • 3142617997 scopus 로고    scopus 로고
    • Hetero-oligomerization between beta2-and beta3-adrenergic receptors generates a beta-adrenergic signaling unit with distinct functional properties
    • Breit, A., Lagace, M. Bouvier, M. Hetero-oligomerization between beta2-and beta3-adrenergic receptors generates a beta-adrenergic signaling unit with distinct functional properties. J. Biol. Chem. 279, 28756-28765 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 28756-28765
    • Breit, A.1    Lagace, M.2    Bouvier, M.3
  • 25
    • 33644822831 scopus 로고    scopus 로고
    • Coupling of GABAB receptor GABAB2 subunit to G proteins: Evidence from Xenopus oocyte and baby hamster kidney cell expression system
    • Uezono, Y. et al. Coupling of GABAB receptor GABAB2 subunit to G proteins: Evidence from Xenopus oocyte and baby hamster kidney cell expression system. Am. J. Physiol. Cell Physiol. 290, C200-C207 (2006).
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290
    • Uezono, Y.1
  • 26
    • 0024723988 scopus 로고
    • Lateral diffusion in an archipelago. Distance dependence of the diffusion coefficient
    • Saxton, M.J. Lateral diffusion in an archipelago. Distance dependence of the diffusion coefficient. Biophys. J. 56, 615-622 (1989).
    • (1989) Biophys. J. , vol.56 , pp. 615-622
    • Saxton, M.J.1
  • 27
    • 0242708772 scopus 로고    scopus 로고
    • Scaffolding of antigen receptors for immunogenic versus tolerogenic signaling
    • Jun, J.E. & Goodnow, C.C. Scaffolding of antigen receptors for immunogenic versus tolerogenic signaling. Nat. Immunol. 4, 1057-1064 (2003).
    • (2003) Nat. Immunol. , vol.4 , pp. 1057-1064
    • Jun, J.E.1    Goodnow, C.C.2
  • 28
    • 0029930984 scopus 로고    scopus 로고
    • The structure and ligand interactions of CD2: Implications for T-cell function
    • Davis, S.J. & van der Merwe, P.A. The structure and ligand interactions of CD2: Implications for T-cell function. Immunol. Today 17, 177-187 (1996).
    • (1996) Immunol. Today , vol.17 , pp. 177-187
    • Davis, S.J.1    van der Merwe, P.A.2
  • 29
    • 2342566929 scopus 로고    scopus 로고
    • What is the importance of the immunological synapse?
    • Davis, D.M. & Dustin, M.L. What is the importance of the immunological synapse? Trends Immunol. 25, 323-327 (2004).
    • (2004) Trends Immunol. , vol.25 , pp. 323-327
    • Davis, D.M.1    Dustin, M.L.2


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