메뉴 건너뛰기




Volumn 109, Issue 9, 2015, Pages 1798-1806

Referenced Single-Molecule Measurements Differentiate between GPCR Oligomerization States

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID B RECEPTOR; BETA 2 ADRENERGIC RECEPTOR; CD28 ANTIGEN; CD86 ANTIGEN;

EID: 84947465922     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2015.09.004     Document Type: Article
Times cited : (28)

References (49)
  • 1
    • 33748926752 scopus 로고    scopus 로고
    • Stoichiometry and turnover in single, functioning membrane protein complexes
    • M.C. Leake, and J.H. Chandler J.P. Armitage Stoichiometry and turnover in single, functioning membrane protein complexes Nature 443 2006 355 358
    • (2006) Nature , vol.443 , pp. 355-358
    • Leake, M.C.1    Chandler, J.H.2    Armitage, J.P.3
  • 2
    • 84872195772 scopus 로고    scopus 로고
    • Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization
    • D. Calebiro, and F. Rieken M.J. Lohse Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization Proc. Natl. Acad. Sci. USA 110 2013 743 748
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 743-748
    • Calebiro, D.1    Rieken, F.2    Lohse, M.J.3
  • 3
    • 79551711208 scopus 로고    scopus 로고
    • Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging
    • R.S. Kasai, and K.G.N. Suzuki A. Kusumi Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging J. Cell Biol. 192 2011 463 480
    • (2011) J. Cell Biol. , vol.192 , pp. 463-480
    • Kasai, R.S.1    Suzuki, K.G.N.2    Kusumi, A.3
  • 5
    • 29744438833 scopus 로고    scopus 로고
    • Thinning out clusters while conserving stoichiometry of labeling
    • M. Moertelmaier, and M. Brameshuber H. Stockinger Thinning out clusters while conserving stoichiometry of labeling Appl. Phys. Lett. 87 2005 263903
    • (2005) Appl. Phys. Lett. , vol.87 , pp. 263903
    • Moertelmaier, M.1    Brameshuber, M.2    Stockinger, H.3
  • 6
    • 77249150932 scopus 로고    scopus 로고
    • Formation and dissociation of M1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules
    • J.A. Hern, and A.H. Baig N.J.M. Birdsall Formation and dissociation of M1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules Proc. Natl. Acad. Sci. USA 107 2010 2693 2698
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 2693-2698
    • Hern, J.A.1    Baig, A.H.2    Birdsall, N.J.M.3
  • 7
    • 69349092619 scopus 로고    scopus 로고
    • DySCo: Quantitating associations of membrane proteins using two-color single-molecule tracking
    • P.D. Dunne, and R.A. Fernandes D. Klenerman DySCo: quantitating associations of membrane proteins using two-color single-molecule tracking Biophys. J. 97 2009 L5 L7
    • (2009) Biophys. J. , vol.97 , pp. L5-L7
    • Dunne, P.D.1    Fernandes, R.A.2    Klenerman, D.3
  • 8
    • 12244298862 scopus 로고    scopus 로고
    • Confined diffusion without fences of a G-protein-coupled receptor as revealed by single particle tracking
    • F. Daumas, and N. Destainville L. Salomé Confined diffusion without fences of a G-protein-coupled receptor as revealed by single particle tracking Biophys. J. 84 2003 356 366
    • (2003) Biophys. J. , vol.84 , pp. 356-366
    • Daumas, F.1    Destainville, N.2    Salomé, L.3
  • 11
    • 84890612981 scopus 로고    scopus 로고
    • Single-molecule imaging revealed dynamic GPCR dimerization
    • R.S. Kasai, and A. Kusumi Single-molecule imaging revealed dynamic GPCR dimerization Curr. Opin. Cell Biol. 27 2014 78 86
    • (2014) Curr. Opin. Cell Biol. , vol.27 , pp. 78-86
    • Kasai, R.S.1    Kusumi, A.2
  • 12
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • T.H. Bayburt, and A.J. Leitz S.G. Sligar Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins J. Biol. Chem. 282 2007 14875 14881
    • (2007) J. Biol. Chem. , vol.282 , pp. 14875-14881
    • Bayburt, T.H.1    Leitz, A.J.2    Sligar, S.G.3
  • 13
    • 34250666273 scopus 로고    scopus 로고
    • A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein
    • M.R. Whorton, and M.P. Bokoch R.K. Sunahara A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein Proc. Natl. Acad. Sci. USA 104 2007 7682 7687
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7682-7687
    • Whorton, M.R.1    Bokoch, M.P.2    Sunahara, R.K.3
  • 14
    • 70350381113 scopus 로고    scopus 로고
    • Purification and functional reconstitution of monomeric μ-opioid receptors: Allosteric modulation of agonist binding by Gi2
    • A.J. Kuszak, and S. Pitchiaya R.K. Sunahara Purification and functional reconstitution of monomeric μ-opioid receptors: allosteric modulation of agonist binding by Gi2 J. Biol. Chem. 284 2009 26732 26741
    • (2009) J. Biol. Chem. , vol.284 , pp. 26732-26741
    • Kuszak, A.J.1    Pitchiaya, S.2    Sunahara, R.K.3
  • 16
    • 33751215258 scopus 로고    scopus 로고
    • A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer
    • J.R. James, and M.I. Oliveira S.J. Davis A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer Nat. Methods 3 2006 1001 1006
    • (2006) Nat. Methods , vol.3 , pp. 1001-1006
    • James, J.R.1    Oliveira, M.I.2    Davis, S.J.3
  • 17
    • 62949087122 scopus 로고    scopus 로고
    • The apparent cooperativity of some GPCRs does not necessarily imply dimerization
    • M. Chabre, P. Deterre, and B. Antonny The apparent cooperativity of some GPCRs does not necessarily imply dimerization Trends Pharmacol. Sci. 30 2009 182 187
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 182-187
    • Chabre, M.1    Deterre, P.2    Antonny, B.3
  • 18
    • 21844441860 scopus 로고    scopus 로고
    • Monomeric G-protein-coupled receptor as a functional unit
    • M. Chabre, and M. le Maire Monomeric G-protein-coupled receptor as a functional unit Biochemistry 44 2005 9395 9403
    • (2005) Biochemistry , vol.44 , pp. 9395-9403
    • Chabre, M.1    Le Maire, M.2
  • 20
    • 77953672210 scopus 로고    scopus 로고
    • GPCR dimers fall apart
    • N.A. Lambert GPCR dimers fall apart Sci. Signal. 3 2010 pe12
    • (2010) Sci. Signal. , vol.3 , pp. pe12
    • Lambert, N.A.1
  • 21
    • 0029031518 scopus 로고
    • Binding stoichiometry of the cytotoxic T lymphocyte-associated molecule-4 (CTLA-4). A disulfide-linked homodimer binds two CD86 molecules
    • P.S. Linsley, and S.G. Nadler S.-Y. Shaw Binding stoichiometry of the cytotoxic T lymphocyte-associated molecule-4 (CTLA-4). A disulfide-linked homodimer binds two CD86 molecules J. Biol. Chem. 270 1995 15417 15424
    • (1995) J. Biol. Chem. , vol.270 , pp. 15417-15424
    • Linsley, P.S.1    Nadler, S.G.2    Shaw, S.-Y.3
  • 22
    • 84878523000 scopus 로고    scopus 로고
    • A quantitative comparison of single-dye tracking analysis tools using Monte Carlo simulations
    • L. Weimann, and K.A. Ganzinger D. Klenerman A quantitative comparison of single-dye tracking analysis tools using Monte Carlo simulations PLoS One 8 2013 e64287
    • (2013) PLoS One , vol.8 , pp. e64287
    • Weimann, L.1    Ganzinger, K.A.2    Klenerman, D.3
  • 23
    • 78049321005 scopus 로고    scopus 로고
    • Membrane molecules mobile even after chemical fixation
    • K.A.K. Tanaka, and K.G.N. Suzuki A. Kusumi Membrane molecules mobile even after chemical fixation Nat. Methods 7 2010 865 866
    • (2010) Nat. Methods , vol.7 , pp. 865-866
    • Tanaka, K.A.K.1    Suzuki, K.G.N.2    Kusumi, A.3
  • 24
    • 20544457766 scopus 로고    scopus 로고
    • Fluorescence imaging for monitoring the colocalization of two single molecules in living cells
    • I. Koyama-Honda, and K. Ritchie A. Kusumi Fluorescence imaging for monitoring the colocalization of two single molecules in living cells Biophys. J. 88 2005 2126 2136
    • (2005) Biophys. J. , vol.88 , pp. 2126-2136
    • Koyama-Honda, I.1    Ritchie, K.2    Kusumi, A.3
  • 25
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • A. Keppler, and S. Gendreizig K. Johnsson A general method for the covalent labeling of fusion proteins with small molecules in vivo Nat. Biotechnol. 21 2003 86 89
    • (2003) Nat. Biotechnol. , vol.21 , pp. 86-89
    • Keppler, A.1    Gendreizig, S.2    Johnsson, K.3
  • 26
    • 48049092838 scopus 로고    scopus 로고
    • HaloTag: A novel protein labeling technology for cell imaging and protein analysis
    • G.V. Los, and L.P. Encell K.V. Wood HaloTag: a novel protein labeling technology for cell imaging and protein analysis ACS Chem. Biol. 3 2008 373 382
    • (2008) ACS Chem. Biol. , vol.3 , pp. 373-382
    • Los, G.V.1    Encell, L.P.2    Wood, K.V.3
  • 27
    • 84902982983 scopus 로고    scopus 로고
    • Type-3 BRET, an improved competition-based bioluminescence resonance energy transfer assay
    • J.H. Felce, R.G. Knox, and S.J. Davis Type-3 BRET, an improved competition-based bioluminescence resonance energy transfer assay Biophys. J. 106 2014 L41 L43
    • (2014) Biophys. J. , vol.106 , pp. L41-L43
    • Felce, J.H.1    Knox, R.G.2    Davis, S.J.3
  • 28
    • 0030609874 scopus 로고    scopus 로고
    • 2-adrenergic receptor sequestration: Intracellular complement of β-adrenergic receptor kinase and β-arrestin determine kinetics of internalization
    • 2-adrenergic receptor sequestration: intracellular complement of β-adrenergic receptor kinase and β-arrestin determine kinetics of internalization Mol. Pharmacol. 51 1997 800 808
    • (1997) Mol. Pharmacol. , vol.51 , pp. 800-808
    • Ménard, L.1    Ferguson, S.S.G.2    Barak, L.S.3
  • 29
    • 84860877718 scopus 로고    scopus 로고
    • 2-adrenergic receptor clusters identified using photoactivated localization microscopy are not lipid raft related, but depend on actin cytoskeleton integrity
    • 2-adrenergic receptor clusters identified using photoactivated localization microscopy are not lipid raft related, but depend on actin cytoskeleton integrity J. Biol. Chem. 287 2012 16768 16780
    • (2012) J. Biol. Chem. , vol.287 , pp. 16768-16780
    • Scarselli, M.1    Annibale, P.2    Radenovic, A.3
  • 30
    • 78650861408 scopus 로고    scopus 로고
    • Live-cell dSTORM with SNAP-tag fusion proteins
    • T. Klein, and A. Löschberger M. Sauer Live-cell dSTORM with SNAP-tag fusion proteins Nat. Methods 8 2011 7 9
    • (2011) Nat. Methods , vol.8 , pp. 7-9
    • Klein, T.1    Löschberger, A.2    Sauer, M.3
  • 31
    • 33750612930 scopus 로고    scopus 로고
    • Understanding the folding of GFP using biophysical techniques
    • S.E. Jackson, T.D. Craggs, and J.R. Huang Understanding the folding of GFP using biophysical techniques Expert Rev. Proteomics 3 2006 545 559
    • (2006) Expert Rev. Proteomics , vol.3 , pp. 545-559
    • Jackson, S.E.1    Craggs, T.D.2    Huang, J.R.3
  • 32
    • 0034724192 scopus 로고    scopus 로고
    • 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET) Proc. Natl. Acad. Sci. USA 97 2000 3684 3689
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3684-3689
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 33
    • 11244294831 scopus 로고    scopus 로고
    • The composition of the β-2 adrenergic receptor oligomer affects its membrane trafficking after ligand-induced endocytosis
    • T.T. Cao, A. Brelot, and M. von Zastrow The composition of the β-2 adrenergic receptor oligomer affects its membrane trafficking after ligand-induced endocytosis Mol. Pharmacol. 67 2005 288 297
    • (2005) Mol. Pharmacol. , vol.67 , pp. 288-297
    • Cao, T.T.1    Brelot, A.2    Von Zastrow, M.3
  • 34
    • 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 receptor subtypes form more efficiently than between less closely related sequences
    • D. Ramsay, and E. Kellett G. Milligan 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 receptor subtypes form more efficiently than between less closely related sequences Biochem. J. 365 2002 429 440
    • (2002) Biochem. J. , vol.365 , pp. 429-440
    • Ramsay, D.1    Kellett, E.2    Milligan, G.3
  • 38
    • 33745511381 scopus 로고    scopus 로고
    • 2-adrenergic receptors utilizing self-assembling Nanodisc technology
    • 604, 606 passim
    • 2-adrenergic receptors utilizing self-assembling Nanodisc technology Biotechniques 40 2006 601 602 604, 606 passim
    • (2006) Biotechniques , vol.40 , pp. 601-602
    • Leitz, A.J.1    Bayburt, T.H.2    Sligar, S.G.3
  • 39
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the β2 adrenergic receptor-Gs protein complex
    • S.G.F. Rasmussen, and B.T. DeVree B.K. Kobilka Crystal structure of the β2 adrenergic receptor-Gs protein complex Nature 477 2011 549 555
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.F.1    DeVree, B.T.2    Kobilka, B.K.3
  • 40
    • 3142617997 scopus 로고    scopus 로고
    • 3-adrenergic receptors generates a β-adrenergic signaling unit with distinct functional properties
    • 3-adrenergic receptors generates a β-adrenergic signaling unit with distinct functional properties J. Biol. Chem. 279 2004 28756 28765
    • (2004) J. Biol. Chem. , vol.279 , pp. 28756-28765
    • Breit, A.1    Lagacé, M.2    Bouvier, M.3
  • 41
    • 0037144542 scopus 로고    scopus 로고
    • 2-adrenergic receptor internalization and ERK signaling efficacy
    • 2-adrenergic receptor internalization and ERK signaling efficacy J. Biol. Chem. 277 2002 35402 35410
    • (2002) J. Biol. Chem. , vol.277 , pp. 35402-35410
    • Lavoie, C.1    Mercier, J.F.2    Hébert, T.E.3
  • 42
    • 84875430188 scopus 로고    scopus 로고
    • Stoichiometric analysis of oligomerization of membrane proteins on living cells using coiled-coil labeling and spectral imaging
    • K. Kawano, and Y. Yano K. Matsuzaki Stoichiometric analysis of oligomerization of membrane proteins on living cells using coiled-coil labeling and spectral imaging Anal. Chem. 85 2013 3454 3461
    • (2013) Anal. Chem. , vol.85 , pp. 3454-3461
    • Kawano, K.1    Yano, Y.2    Matsuzaki, K.3
  • 44
    • 84883148197 scopus 로고    scopus 로고
    • Segregation of family A GPCR protomers in the plasma membrane
    • A. Gavalas, and T.-H. Lan N.A. Lambert Segregation of family A GPCR protomers in the plasma membrane Mol. Pharmacol. 84 2013 346 352
    • (2013) Mol. Pharmacol. , vol.84 , pp. 346-352
    • Gavalas, A.1    Lan, T.-H.2    Lambert, N.A.3
  • 45
    • 84873685831 scopus 로고    scopus 로고
    • Molecular signatures of G-protein-coupled receptors
    • A.J. Venkatakrishnan, and X. Deupi M.M. Babu Molecular signatures of G-protein-coupled receptors Nature 494 2013 185 194
    • (2013) Nature , vol.494 , pp. 185-194
    • Venkatakrishnan, A.J.1    Deupi, X.2    Babu, M.M.3
  • 46
    • 85027927015 scopus 로고    scopus 로고
    • Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists
    • B. Wu, and E.Y.T. Chien R.C. Stevens Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists Science 330 2010 1066 1071
    • (2010) Science , vol.330 , pp. 1066-1071
    • Wu, B.1    Chien, E.Y.T.2    Stevens, R.C.3
  • 47
    • 84856511452 scopus 로고    scopus 로고
    • Domain coupling in GPCRs: The engine for induced conformational changes
    • H. Unal, and S.S. Karnik Domain coupling in GPCRs: the engine for induced conformational changes Trends Pharmacol. Sci. 33 2012 79 88
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 79-88
    • Unal, H.1    Karnik, S.S.2
  • 48
    • 17644405396 scopus 로고    scopus 로고
    • G protein-coupled receptors show unusual patterns of intrinsic unfolding
    • V.P. Jaakola, and J. Prilusky A. Goldman G protein-coupled receptors show unusual patterns of intrinsic unfolding Protein Eng. Des. Sel. 18 2005 103 110
    • (2005) Protein Eng. Des. Sel. , vol.18 , pp. 103-110
    • Jaakola, V.P.1    Prilusky, J.2    Goldman, A.3
  • 49
    • 13444269196 scopus 로고    scopus 로고
    • Monitoring the formation of dynamic G-protein-coupled receptor-protein complexes in living cells
    • K.D.G. Pfleger, and K.A. Eidne Monitoring the formation of dynamic G-protein-coupled receptor-protein complexes in living cells Biochem. J. 385 2005 625 637
    • (2005) Biochem. J. , vol.385 , pp. 625-637
    • Pfleger, K.D.G.1    Eidne, K.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.