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Volumn 283, Issue 7, 2016, Pages 1197-1217

Revealing G-protein-coupled receptor oligomerization at the single-molecule level through a nanoscopic lens: Methods, dynamics and biological function

Author keywords

actin cytoskeleton; G protein coupled receptor; oligomerization; photoactivated localization microscopy; single molecule microscopy; 2 adrenergic receptor

Indexed keywords

DIMER; G PROTEIN COUPLED RECEPTOR; OLIGOMER; PROTEIN BINDING;

EID: 84962960723     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13577     Document Type: Review
Times cited : (66)

References (115)
  • 1
    • 0037160105 scopus 로고    scopus 로고
    • 2-Adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • 2-Adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer. J Biol Chem 277, 44925-44931.
    • (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
  • 2
    • 33144473025 scopus 로고    scopus 로고
    • FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells
    • Meyer BH, Segura JM, Martinez KL, Hovius R, George N, Johnsson K, &, Vogel H, (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    Martinez, K.L.3    Hovius, R.4    George, N.5    Johnsson, K.6    Vogel, H.7
  • 3
    • 80053911537 scopus 로고    scopus 로고
    • Bright light, better labels
    • Baker M, (2011) Bright light, better labels. Nature 478, 137-142.
    • (2011) Nature , vol.478 , pp. 137-142
    • Baker, M.1
  • 4
    • 78650512639 scopus 로고    scopus 로고
    • Breaking the diffraction barrier: Super-resolution imaging of cells
    • Huang B, Babcock H, &, Zhuang X, (2010) Breaking the diffraction barrier: super-resolution imaging of cells. Cell 143, 1047-1058.
    • (2010) Cell , vol.143 , pp. 1047-1058
    • Huang, B.1    Babcock, H.2    Zhuang, X.3
  • 5
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • Rust MJ, Bates M, &, Zhuang X, (2006) Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat Methods 3, 793-795.
    • (2006) Nat Methods , vol.3 , pp. 793-795
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3
  • 7
    • 84907820473 scopus 로고    scopus 로고
    • Challenges in quantitative single molecule localization microscopy
    • Shivanandan A, Deschout H, Scarselli M, &, Radenovic A, (2014) Challenges in quantitative single molecule localization microscopy. FEBS Lett 588, 3595-3602.
    • (2014) FEBS Lett , vol.588 , pp. 3595-3602
    • Shivanandan, A.1    Deschout, H.2    Scarselli, M.3    Radenovic, A.4
  • 8
    • 79960806755 scopus 로고    scopus 로고
    • Quantitative photo activated localization microscopy: Unraveling the effects of photoblinking
    • Annibale P, Vanni S, Scarselli M, Rothlisberger U, &, Radenovic A, (2011a) Quantitative photo activated localization microscopy: unraveling the effects of photoblinking. PLoS One 6, e22678.
    • (2011) PLoS One , vol.6 , pp. e22678
    • Annibale, P.1    Vanni, S.2    Scarselli, M.3    Rothlisberger, U.4    Radenovic, A.5
  • 10
    • 33845360042 scopus 로고    scopus 로고
    • Ultra-high resolution imaging by fluorescence photoactivation localization microscopy
    • Hess ST, Girirajan TPK, &, Mason MD, (2006) Ultra-high resolution imaging by fluorescence photoactivation localization microscopy. Biophys J 91, 4258-4272.
    • (2006) Biophys J , vol.91 , pp. 4258-4272
    • Hess, S.T.1    Girirajan, T.P.K.2    Mason, M.D.3
  • 12
    • 69249158290 scopus 로고    scopus 로고
    • Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation
    • Han Y, Moreira IS, Urizar E, Weinstein H, &, Javitch JA, (2009) Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation. Nat Chem Biol 5, 688-695.
    • (2009) Nat Chem Biol , vol.5 , pp. 688-695
    • Han, Y.1    Moreira, I.S.2    Urizar, E.3    Weinstein, H.4    Javitch, J.A.5
  • 13
    • 84879121186 scopus 로고    scopus 로고
    • The prevalence, maintenance, and relevance of G protein-coupled receptor oligomerization
    • erratum appears in Molecular Pharmacology 84(2), 303
    • Milligan G, (2013) The prevalence, maintenance, and relevance of G protein-coupled receptor oligomerization. Mol Pharmacol 84, 158-169. (erratum appears in Molecular Pharmacology 84(2), 303).
    • (2013) Mol Pharmacol , vol.84 , pp. 158-169
    • Milligan, G.1
  • 14
    • 34250666273 scopus 로고    scopus 로고
    • A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein
    • Whorton MR, Bokoch MP, Rasmussen SG, Huang B, Zare RN, Kobilka B, &, Sunahara RK, (2007) A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein. Proc Natl Acad Sci USA 104, 7682-7687.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7682-7687
    • Whorton, M.R.1    Bokoch, M.P.2    Rasmussen, S.G.3    Huang, B.4    Zare, R.N.5    Kobilka, B.6    Sunahara, R.K.7
  • 16
    • 51049112029 scopus 로고    scopus 로고
    • Dopamine D2 receptors form higher order oligomers at physiological expression levels
    • Guo W, Urizar E, Kralikova M, Mobarec JC, Shi L, Filizola M, &, Javitch JA, (2008) Dopamine D2 receptors form higher order oligomers at physiological expression levels. EMBO J 27, 2293-2304.
    • (2008) EMBO J , vol.27 , pp. 2293-2304
    • Guo, W.1    Urizar, E.2    Kralikova, M.3    Mobarec, J.C.4    Shi, L.5    Filizola, M.6    Javitch, J.A.7
  • 21
    • 42949083695 scopus 로고    scopus 로고
    • Live-cell photoactivated localization microscopy of nanoscale adhesion dynamics
    • Shroff H, Galbraith CG, Galbraith JA, &, Betzig E, (2008) Live-cell photoactivated localization microscopy of nanoscale adhesion dynamics. Nat Methods 5, 417-423.
    • (2008) Nat Methods , vol.5 , pp. 417-423
    • Shroff, H.1    Galbraith, C.G.2    Galbraith, J.A.3    Betzig, E.4
  • 27
    • 84949294350 scopus 로고    scopus 로고
    • Visualizing G protein-coupled receptor-receptor interactions in brain using proximity ligation in situ assay
    • Taura J, Fernández-Dueñas V, &, Ciruela F, (2015) Visualizing G protein-coupled receptor-receptor interactions in brain using proximity ligation in situ assay. Curr Protoc Cell Biol 67, 17.17.1-17.17.16.
    • (2015) Curr Protoc Cell Biol , vol.67 , pp. 17171-171716
    • Taura, J.1    Fernández-Dueñas, V.2    Ciruela, F.3
  • 31
    • 84923854268 scopus 로고    scopus 로고
    • The GPCR heterotetramer: Challenging classical pharmacology
    • Ferré S, (2015) The GPCR heterotetramer: challenging classical pharmacology. Trends Pharmacol Sci 36, 145-152.
    • (2015) Trends Pharmacol Sci , vol.36 , pp. 145-152
    • Ferré, S.1
  • 34
    • 67650364823 scopus 로고    scopus 로고
    • Chapter 22: Detection of GPCR/ß-arrestin interactions in live cells using bioluminescence resonance energy transfer technology
    • Wayne R. Leiffert (ed.), G Protein-Coupled Receptors in Drug Discovery, Humana Press
    • Kocan M, &, Pfleger KDG, (2009) Chapter 22: detection of GPCR/ß-arrestin interactions in live cells using bioluminescence resonance energy transfer technology (Wayne R. Leiffert (ed.), G Protein-Coupled Receptors in Drug Discovery, Humana Press. Methods Mol Biol 552, 305-317.
    • (2009) Methods Mol Biol , vol.552 , pp. 305-317
    • Kocan, M.1    Pfleger, K.D.G.2
  • 37
    • 28844437680 scopus 로고    scopus 로고
    • Inhibition of serotonin 5-Hydroxytryptamine2C receptor function through heterodimerization: Receptor dimers bind two molecules of ligand and one G-protein
    • Herrick-Davis K, Grinde E, Harrigan TJ, &, Mazurkiewicz JE, (2005) Inhibition of serotonin 5-Hydroxytryptamine2C receptor function through heterodimerization: receptor dimers bind two molecules of ligand and one G-protein. J Biol Chem 280, 40144-40151.
    • (2005) J Biol Chem , vol.280 , pp. 40144-40151
    • Herrick-Davis, K.1    Grinde, E.2    Harrigan, T.J.3    Mazurkiewicz, J.E.4
  • 38
    • 84868114014 scopus 로고    scopus 로고
    • Plasticity of the asialoglycoprotein receptor deciphered by ensemble FRET imaging and single-molecule counting PALM imaging
    • Renz M, Daniels BR, Vámosi G, Arias IM, &, Lippincott-Schwartz J, (2012) Plasticity of the asialoglycoprotein receptor deciphered by ensemble FRET imaging and single-molecule counting PALM imaging. Proc Natl Acad Sci USA 109, 2989-2997.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 2989-2997
    • Renz, M.1    Daniels, B.R.2    Vámosi, G.3    Arias, I.M.4    Lippincott-Schwartz, J.5
  • 41
    • 36249020990 scopus 로고    scopus 로고
    • Old and new ways to calculate the affinity of agonists and antagonists interacting with G-protein-coupled monomeric and dimeric receptors: The receptor-dimer cooperativity index
    • Casadó V, Cortés A, Ciruela F, Mallol J, Ferré S, Lluis C, Canela EI, &, Franco R, (2007) Old and new ways to calculate the affinity of agonists and antagonists interacting with G-protein-coupled monomeric and dimeric receptors: the receptor-dimer cooperativity index. Pharmacol Ther 116, 343-354.
    • (2007) Pharmacol Ther , vol.116 , pp. 343-354
    • Casadó, V.1    Cortés, A.2    Ciruela, F.3    Mallol, J.4    Ferré, S.5    Lluis, C.6    Canela, E.I.7    Franco, R.8
  • 42
    • 84890612981 scopus 로고    scopus 로고
    • Single-molecule imaging revealed dynamic GPCR dimerization
    • erratum appears in Nature Methods 27, 144
    • Kasai RS, &, Kusumi A, (2014) Single-molecule imaging revealed dynamic GPCR dimerization. Curr Opin Cell Biol 27, 78-86. (erratum appears in Nature Methods 27, 144).
    • (2014) Curr Opin Cell Biol , vol.27 , pp. 78-86
    • Kasai, R.S.1    Kusumi, A.2
  • 44
    • 84863615246 scopus 로고    scopus 로고
    • 2C) receptor revealed by fluorescence correlation spectroscopy with photon counting histogram analysis: Evidence for homodimers without monomers or tetramers
    • 2C) receptor revealed by fluorescence correlation spectroscopy with photon counting histogram analysis: evidence for homodimers without monomers or tetramers. J Biol Chem 287, 23604-23614.
    • (2012) J Biol Chem , vol.287 , pp. 23604-23614
    • Herrick-Davis, K.1    Grinde, E.2    Lindsley, T.3    Cowan, A.4    Mazurkiewicz, J.E.5
  • 45
    • 84884683292 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy analysis of serotonin, adrenergic, muscarinic, and dopamine receptor dimerization: The oligomer number puzzle
    • Herrick-Davis K, Grinde E, Cowan A, &, Mazurkiewicz JE, (2013) Fluorescence correlation spectroscopy analysis of serotonin, adrenergic, muscarinic, and dopamine receptor dimerization: the oligomer number puzzle. Mol Pharmacol 84, 630-642.
    • (2013) Mol Pharmacol , vol.84 , pp. 630-642
    • Herrick-Davis, K.1    Grinde, E.2    Cowan, A.3    Mazurkiewicz, J.E.4
  • 48
    • 84922896573 scopus 로고    scopus 로고
    • Single molecule analysis of functionally asymmetric G Protein-coupled Receptor (GPCR) Oligomers reveals diverse spatial and structural assemblies
    • Jonas KC, Fanelli F, Huhtaniemi IT, &, Hanyaloglu AC, (2015) Single molecule analysis of functionally asymmetric G Protein-coupled Receptor (GPCR) Oligomers reveals diverse spatial and structural assemblies. J Biol Chem 290, 3875-3892.
    • (2015) J Biol Chem , vol.290 , pp. 3875-3892
    • Jonas, K.C.1    Fanelli, F.2    Huhtaniemi, I.T.3    Hanyaloglu, A.C.4
  • 49
    • 84919704267 scopus 로고    scopus 로고
    • Major ligand-induced rearrangement of the heptahelical domain interface in a GPCR dimer
    • Xue L, Rovira X, Scholler P, Zhao H, Liu J, Pin JP, &, Rondard P, (2015) Major ligand-induced rearrangement of the heptahelical domain interface in a GPCR dimer. Nat Chem Biol 11, 134-140.
    • (2015) Nat Chem Biol , vol.11 , pp. 134-140
    • Xue, L.1    Rovira, X.2    Scholler, P.3    Zhao, H.4    Liu, J.5    Pin, J.P.6    Rondard, P.7
  • 52
    • 33745934035 scopus 로고    scopus 로고
    • μ-δ Opioid receptor functional interaction: Insight using receptor-G protein fusions
    • Snook LA, Milligan G, Kieffer BL, &, Massotte D, (2006) μ-δ Opioid receptor functional interaction: insight using receptor-G protein fusions. J Pharmacol Exp Ther 318, 683-690.
    • (2006) J Pharmacol Exp Ther , vol.318 , pp. 683-690
    • Snook, L.A.1    Milligan, G.2    Kieffer, B.L.3    Massotte, D.4
  • 53
    • 42449147994 scopus 로고    scopus 로고
    • Co-expression of mu and delta opioid receptors as receptor-G protein fusions enhances both mu and delta signalling via distinct mechanisms
    • Snook LA, Milligan G, Kieffer BL, &, Massotte D, (2008) Co-expression of mu and delta opioid receptors as receptor-G protein fusions enhances both mu and delta signalling via distinct mechanisms. J Neurochem 105, 865-873.
    • (2008) J Neurochem , vol.105 , pp. 865-873
    • Snook, L.A.1    Milligan, G.2    Kieffer, B.L.3    Massotte, D.4
  • 54
    • 84902292100 scopus 로고    scopus 로고
    • CrossTalk opposing view: Weighing the evidence for class A GPCR dimers, the jury is still out
    • Lambert NA, &, Javitch JA, (2014) CrossTalk opposing view: weighing the evidence for class A GPCR dimers, the jury is still out. J Physiol 592, 2443-2445.
    • (2014) J Physiol , vol.592 , pp. 2443-2445
    • Lambert, N.A.1    Javitch, J.A.2
  • 59
    • 84863010954 scopus 로고    scopus 로고
    • Apo-Ghrelin receptor forms heteromers with DRD2 in hypothalamic neurons and is essential for anorexigenic effects of DRD2 agonism
    • Kern A, Albarran-Zeckler R, Walsh HE, &, Smith RG, (2012) Apo-Ghrelin receptor forms heteromers with DRD2 in hypothalamic neurons and is essential for anorexigenic effects of DRD2 agonism. Neuron 73, 317-332.
    • (2012) Neuron , vol.73 , pp. 317-332
    • Kern, A.1    Albarran-Zeckler, R.2    Walsh, H.E.3    Smith, R.G.4
  • 62
    • 84908338078 scopus 로고    scopus 로고
    • Family a GPCR heteromers in animal models
    • González-Maeso J, (2014) Family a GPCR heteromers in animal models. Front Pharmacol 5, 226.
    • (2014) Front Pharmacol , vol.5 , pp. 226
    • González-Maeso, J.1
  • 63
    • 84908352984 scopus 로고    scopus 로고
    • A peptide targeting an interaction interface disrupts the dopamine D1-D2 receptor heteromer to block signaling and function in vitro and in vivo: Effective selective antagonism
    • Hasbi A, Perreault ML, Shen MYF, Zhang L, To R, Fan T, Nguyen T, Ji X, O'Dowd BF, &, George SR, (2014) A peptide targeting an interaction interface disrupts the dopamine D1-D2 receptor heteromer to block signaling and function in vitro and in vivo: effective selective antagonism. FASEB J 28, 4806-4820.
    • (2014) FASEB J , vol.28 , pp. 4806-4820
    • Hasbi, A.1    Perreault, M.L.2    Shen, M.Y.F.3    Zhang, L.4    To, R.5    Fan, T.6    Nguyen, T.7    Ji, X.8    O'Dowd, B.F.9    George, S.R.10
  • 65
    • 84901853305 scopus 로고    scopus 로고
    • Transmembrane peptides as unique tools to demonstrate the in vivo action of a cross-class GPCR heterocomplex
    • Lee LTO, Ng SYL, Chu JYS, Sekar R, Harikumar KG, Miller LJ, &, Chow BKC, (2014) Transmembrane peptides as unique tools to demonstrate the in vivo action of a cross-class GPCR heterocomplex. FASEB J 28, 2632-2644.
    • (2014) FASEB J , vol.28 , pp. 2632-2644
    • Lee, L.T.O.1    Ng, S.Y.L.2    Chu, J.Y.S.3    Sekar, R.4    Harikumar, K.G.5    Miller, L.J.6    Chow, B.K.C.7
  • 66
    • 0016366591 scopus 로고
    • Fluorescence correlation spectroscopy II. An experimental realization
    • Magde D, Elson EL, &, Webb WW, (1974) Fluorescence correlation spectroscopy II. An experimental realization. Biopolymers 13, 29-61.
    • (1974) Biopolymers , vol.13 , pp. 29-61
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 67
    • 36448965981 scopus 로고    scopus 로고
    • Pharmacology under the microscope: The use of fluorescence correlation spectroscopy to determine the properties of ligand-receptor complexes
    • Briddon SJ, &, Hill SJ, (2007) Pharmacology under the microscope: the use of fluorescence correlation spectroscopy to determine the properties of ligand-receptor complexes. Trends Pharmacol Sci 28, 637-645.
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 637-645
    • Briddon, S.J.1    Hill, S.J.2
  • 69
    • 40449125151 scopus 로고    scopus 로고
    • 3 adenosine receptors exist within heterogeneous complexes in membrane microdomains of individual living cells
    • 3 adenosine receptors exist within heterogeneous complexes in membrane microdomains of individual living cells. FASEB J 22, 850-860.
    • (2008) FASEB J , vol.22 , pp. 850-860
    • Cordeaux, Y.1    Briddon, S.J.2    Alexander, S.P.3    Kellam, B.4    Hill, S.J.5
  • 70
    • 84907692805 scopus 로고    scopus 로고
    • 3 receptors within membrane microdomains of individual cells provides evidence of receptor dimerization and allosterism
    • 3 receptors within membrane microdomains of individual cells provides evidence of receptor dimerization and allosterism. FASEB J 28, 4211-4222.
    • (2014) FASEB J , vol.28 , pp. 4211-4222
    • Corriden, R.1    Kilpatrick, L.E.2    Kellam, B.3    Briddon, S.J.4    Hill, S.J.5
  • 72
    • 84902265013 scopus 로고    scopus 로고
    • Time-resolved fluorescence spectroscopy measures clustering and mobility of a G protein-coupled receptor Opsin in live cell membranes
    • Comar WD, Schubert SM, Jastrzebska B, Palczewski K, &, Smith AW, (2014) Time-resolved fluorescence spectroscopy measures clustering and mobility of a G protein-coupled receptor Opsin in live cell membranes. J Am Chem Soc 136, 8342-8349.
    • (2014) J Am Chem Soc , vol.136 , pp. 8342-8349
    • Comar, W.D.1    Schubert, S.M.2    Jastrzebska, B.3    Palczewski, K.4    Smith, A.W.5
  • 73
    • 0036220117 scopus 로고    scopus 로고
    • Molecular brightness characterization of EGFP in vivo by fluorescence fluctuation spectroscopy
    • Chen Y, Muller JD, Ruan Q, &, Gratton E, (2002) Molecular brightness characterization of EGFP in vivo by fluorescence fluctuation spectroscopy. Biophys J 82, 133-144.
    • (2002) Biophys J , vol.82 , pp. 133-144
    • Chen, Y.1    Muller, J.D.2    Ruan, Q.3    Gratton, E.4
  • 74
    • 84885899008 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy and photon-counting histogram analysis of receptor-receptor interactions
    • Herrick-Davis K, &, Mazurkiewicz JE, (2013) Fluorescence correlation spectroscopy and photon-counting histogram analysis of receptor-receptor interactions. Methods Cell Biol 117, 181-196.
    • (2013) Methods Cell Biol , vol.117 , pp. 181-196
    • Herrick-Davis, K.1    Mazurkiewicz, J.E.2
  • 75
    • 84872195772 scopus 로고    scopus 로고
    • Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization
    • Calebiro D, Rieken F, Wagner J, Sungkaworn T, Zabel U, Borzi A, Cocucci E, Zürn A, &, Lohse MJ, (2013) Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization. Proc Natl Acad Sci USA 110, 743-748.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 743-748
    • Calebiro, D.1    Rieken, F.2    Wagner, J.3    Sungkaworn, T.4    Zabel, U.5    Borzi, A.6    Cocucci, E.7    Zürn, A.8    Lohse, M.J.9
  • 76
    • 66749160501 scopus 로고    scopus 로고
    • Analysis of membrane protein cluster densities and sizes in situ by image correlation spectroscopy
    • discussion 331-243.
    • Petersen NO, Brown C, Kaminski A, Rocheleau J, Srivastava M, &, Wiseman PW, (1998) Analysis of membrane protein cluster densities and sizes in situ by image correlation spectroscopy. Faraday Discuss 28, 9-305. discussion 331-243.
    • (1998) Faraday Discuss , vol.28 , pp. 9-305
    • Petersen, N.O.1    Brown, C.2    Kaminski, A.3    Rocheleau, J.4    Srivastava, M.5    Wiseman, P.W.6
  • 77
    • 34548364156 scopus 로고    scopus 로고
    • NHERF-1 and the cytoskeleton regulate the traffic and membrane dynamics of g protein-coupled receptors
    • Wheeler D, Sneddon WB, Wang B, Friedman PA, &, Romero G, (2007) NHERF-1 and the cytoskeleton regulate the traffic and membrane dynamics of g protein-coupled receptors. J Biol Chem 282, 25076-25087.
    • (2007) J Biol Chem , vol.282 , pp. 25076-25087
    • Wheeler, D.1    Sneddon, W.B.2    Wang, B.3    Friedman, P.A.4    Romero, G.5
  • 78
    • 79959854835 scopus 로고    scopus 로고
    • Identification of clustering artifacts in photoactivated localization microscopy
    • Annibale P, Vanni S, Scarselli M, Rothlisberger U, &, Radenovic A, (2011b) Identification of clustering artifacts in photoactivated localization microscopy. Nat Methods 8, 527-528.
    • (2011) Nat Methods , vol.8 , pp. 527-528
    • Annibale, P.1    Vanni, S.2    Scarselli, M.3    Rothlisberger, U.4    Radenovic, A.5
  • 80
    • 84860877718 scopus 로고    scopus 로고
    • Cell type-specific β2-Adrenergic receptor clusters identified using photoactivated localization microscopy are not lipid raft related, but depend on actin cytoskeleton integrity
    • Scarselli M, Annibale P, &, Radenovic A, (2012) Cell type-specific β2-Adrenergic receptor clusters identified using photoactivated localization microscopy are not lipid raft related, but depend on actin cytoskeleton integrity. J Biol Chem 287, 16768-16780.
    • (2012) J Biol Chem , vol.287 , pp. 16768-16780
    • Scarselli, M.1    Annibale, P.2    Radenovic, A.3
  • 81
    • 84873123405 scopus 로고    scopus 로고
    • Enlightening G-protein-coupled receptors on the plasma membrane using super-resolution photoactivated localization microscopy
    • Scarselli M, Annibale P, Gerace C, &, Radenovic A, (2013) Enlightening G-protein-coupled receptors on the plasma membrane using super-resolution photoactivated localization microscopy. Biochem Soc Trans 41, 191-196.
    • (2013) Biochem Soc Trans , vol.41 , pp. 191-196
    • Scarselli, M.1    Annibale, P.2    Gerace, C.3    Radenovic, A.4
  • 82
    • 0035254167 scopus 로고    scopus 로고
    • Differential effects of carvedilol and metoprolol on isoprenaline-induced changes in β-adrenoceptor density and systolic function in rat cardiac myocytes
    • Flesch M, Ettelbrück S, Rosenkranz S, Maack C, Cremers B, Schlüter KD, Zolk O, &, Böhm M, (2001) Differential effects of carvedilol and metoprolol on isoprenaline-induced changes in β-adrenoceptor density and systolic function in rat cardiac myocytes. Cardiovasc Res 49, 371-380.
    • (2001) Cardiovasc Res , vol.49 , pp. 371-380
    • Flesch, M.1    Ettelbrück, S.2    Rosenkranz, S.3    Maack, C.4    Cremers, B.5    Schlüter, K.D.6    Zolk, O.7    Böhm, M.8
  • 84
    • 84919681704 scopus 로고    scopus 로고
    • Dynamics and modulation of metabotropic glutamate receptors
    • Rondard P, &, Pin JP, (2015) Dynamics and modulation of metabotropic glutamate receptors. Curr Opin Pharmacol 20, 95-101.
    • (2015) Curr Opin Pharmacol , vol.20 , pp. 95-101
    • Rondard, P.1    Pin, J.P.2
  • 86
    • 63649098654 scopus 로고    scopus 로고
    • Constitutive internalization of G protein-coupled receptors and G proteins via clathrin-independent endocytosis
    • Scarselli M, &, Donaldson JG, (2009) Constitutive internalization of G protein-coupled receptors and G proteins via clathrin-independent endocytosis. J Biol Chem 284, 3577-3585.
    • (2009) J Biol Chem , vol.284 , pp. 3577-3585
    • Scarselli, M.1    Donaldson, J.G.2
  • 87
    • 41149090339 scopus 로고    scopus 로고
    • Regulation of GPCRs by endocytic membrane trafficking and its potential implications
    • Hanyaloglu AC, &, von Zastrow M, (2008) Regulation of GPCRs by endocytic membrane trafficking and its potential implications. Annu Rev Pharmacol Toxicol 48, 537-568.
    • (2008) Annu Rev Pharmacol Toxicol , vol.48 , pp. 537-568
    • Hanyaloglu, A.C.1    Von Zastrow, M.2
  • 88
    • 80052787459 scopus 로고    scopus 로고
    • Measuring spatiotemporal dynamics of cyclic AMP signaling in real-time using FRET-based biosensors
    • Gesellchen F, Stangherlin A, Surdo N, Terrin A, Zoccarato A, &, Zaccolo M, (2011) Measuring spatiotemporal dynamics of cyclic AMP signaling in real-time using FRET-based biosensors. Methods Mol Biol 746, 297-316.
    • (2011) Methods Mol Biol , vol.746 , pp. 297-316
    • Gesellchen, F.1    Stangherlin, A.2    Surdo, N.3    Terrin, A.4    Zoccarato, A.5    Zaccolo, M.6
  • 89
    • 48449092211 scopus 로고    scopus 로고
    • Using plasma membrane nanoclusters to build better signaling circuits
    • Harding AS, &, Hancock JF, (2008) Using plasma membrane nanoclusters to build better signaling circuits. Trends Cell Biol 18, 364-371.
    • (2008) Trends Cell Biol , vol.18 , pp. 364-371
    • Harding, A.S.1    Hancock, J.F.2
  • 90
    • 77955825161 scopus 로고    scopus 로고
    • Spatial organization of transmembrane receptor signalling
    • Bethani I, Skånland SS, Dikic I, &, Acker-Palmer A, (2010) Spatial organization of transmembrane receptor signalling. EMBO J 29, 2677-2688.
    • (2010) EMBO J , vol.29 , pp. 2677-2688
    • Bethani, I.1    Skånland, S.S.2    Dikic, I.3    Acker-Palmer, A.4
  • 91
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: At a crossroad between cell biology and physics
    • Jacobson K, Mouritsen OG, &, Anderson RG, (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.3
  • 92
    • 49049108218 scopus 로고    scopus 로고
    • G-protein-coupled receptor-signaling components in membrane raft and caveolae microdomains
    • E. Klussmann, J. Scott (eds.) Protein-Protein Interactions as New Drug Targets, Springer-Verlag
    • Patel HH, Murray F, &, Insel PA, (2008) G-protein-coupled receptor-signaling components in membrane raft and caveolae microdomains (E. Klussmann, J. Scott (eds.) Protein-Protein Interactions as New Drug Targets, Springer-Verlag). Handb Exp Pharmacol 186, 167-184.
    • (2008) Handb Exp Pharmacol , vol.186 , pp. 167-184
    • Patel, H.H.1    Murray, F.2    Insel, P.A.3
  • 93
    • 54049106162 scopus 로고    scopus 로고
    • 2-Adrenergic receptor from its partners determines signaling efficacy: Insight into nanoscale organization of signal transduction
    • 2-Adrenergic receptor from its partners determines signaling efficacy: insight into nanoscale organization of signal transduction. J Biol Chem 283, 24659-24672.
    • (2008) J Biol Chem , vol.283 , pp. 24659-24672
    • Pontier, S.M.1    Percherancier, Y.2    Galandrin, S.3    Breit, A.4    Galés, C.5    Bouvier, M.6
  • 94
  • 96
    • 2342451911 scopus 로고    scopus 로고
    • G-protein coupled receptors in lipid rafts and caveolae: How, when and why do they go there?
    • Chini B, &, Parenti M, (2004) G-protein coupled receptors in lipid rafts and caveolae: how, when and why do they go there? J Mol Endocrinol 32, 325-338.
    • (2004) J Mol Endocrinol , vol.32 , pp. 325-338
    • Chini, B.1    Parenti, M.2
  • 100
    • 79955865307 scopus 로고    scopus 로고
    • Reorganization of the actin cytoskeleton upon G-protein coupled receptor signaling
    • Ganguly S, Saxena R, &, Chattopadhyay A, (2011) Reorganization of the actin cytoskeleton upon G-protein coupled receptor signaling. Biochim Biophys Acta 1808, 1921-1929.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 1921-1929
    • Ganguly, S.1    Saxena, R.2    Chattopadhyay, A.3
  • 101
    • 80051695489 scopus 로고    scopus 로고
    • 2-adrenergic receptors in the plasma membrane of cardiomyocyte-like H9c2 cells is mediated by selective interactions with PDZ domain and A-kinase anchoring proteins but not caveolae
    • 2-adrenergic receptors in the plasma membrane of cardiomyocyte-like H9c2 cells is mediated by selective interactions with PDZ domain and A-kinase anchoring proteins but not caveolae. Mol Biol Cell 22, 2970-2982.
    • (2011) Mol Biol Cell , vol.22 , pp. 2970-2982
    • Valentine, C.D.1    Haggie, P.M.2
  • 103
    • 38049110263 scopus 로고    scopus 로고
    • Dual-color superresolution imaging of genetically expressed probes within individual adhesion complexes
    • rratum appears in Proceedings of the National Academy of Sciences of the United States of America (PNAS) 105(39), 15220
    • Shroff H, Galbraith CG, Galbraith JA, White H, Gillette J, Olenych S, Davidson MW, &, Betzig E, (2007) Dual-color superresolution imaging of genetically expressed probes within individual adhesion complexes. Proc Natl Acad Sci USA 104, 20308-20313. (erratum appears in Proceedings of the National Academy of Sciences of the United States of America (PNAS) 105(39), 15220).
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20308-20313
    • Shroff, H.1    Galbraith, C.G.2    Galbraith, J.A.3    White, H.4    Gillette, J.5    Olenych, S.6    Davidson, M.W.7    Betzig, E.8
  • 104
    • 84884212705 scopus 로고    scopus 로고
    • Identification of the factors affecting co-localization precision for quantitative multicolor localization microscopy
    • Annibale P, Scarselli M, Greco M, &, Radenovic A, (2012) Identification of the factors affecting co-localization precision for quantitative multicolor localization microscopy. Opt Nanoscopy 1.
    • (2012) Opt Nanoscopy , vol.1
    • Annibale, P.1    Scarselli, M.2    Greco, M.3    Radenovic, A.4
  • 105
    • 84896638753 scopus 로고    scopus 로고
    • Superresolution imaging of biological systems using photoactivated localization microscopy
    • Sengupta P, van Engelenburg SB, &, Lippincott-Schwartz J, (2014) Superresolution imaging of biological systems using photoactivated localization microscopy. Chem Rev 114, 3189-31202.
    • (2014) Chem Rev , vol.114 , pp. 3189-31202
    • Sengupta, P.1    Van Engelenburg, S.B.2    Lippincott-Schwartz, J.3
  • 106
    • 33749079184 scopus 로고    scopus 로고
    • CargoRegulates Clathrin-Coated pit dynamics
    • Puthenveedu MA, &, von Zastrow M, (2006) CargoRegulates Clathrin-Coated pit dynamics. Cell 127, 113-124.
    • (2006) Cell , vol.127 , pp. 113-124
    • Puthenveedu, M.A.1    Von Zastrow, M.2
  • 107
    • 59349110743 scopus 로고    scopus 로고
    • Photoactivatable mCherry for high-resolution two-color fluorescence microscopy
    • erratum appears in Nature Methods 6(4), 311
    • Subach FV, Patterson GH, Manley S, Gillette JM, Lippincott-Schwartz J, &, Verkhusha VV, (2009) Photoactivatable mCherry for high-resolution two-color fluorescence microscopy. Nat Methods 6, 153-159. (erratum appears in Nature Methods 6(4), 311).
    • (2009) Nat Methods , vol.6 , pp. 153-159
    • Subach, F.V.1    Patterson, G.H.2    Manley, S.3    Gillette, J.M.4    Lippincott-Schwartz, J.5    Verkhusha, V.V.6
  • 108
    • 77952059303 scopus 로고    scopus 로고
    • Bright monomeric photoactivatable red fluorescent protein for two-color super-resolution sptPALM of live cells
    • Subach FV, Patterson GH, Renz M, Lippincott-Schwartz J, &, Verkhusha VV, (2010) Bright monomeric photoactivatable red fluorescent protein for two-color super-resolution sptPALM of live cells. J Am Chem Soc 132, 6481-6491.
    • (2010) J Am Chem Soc , vol.132 , pp. 6481-6491
    • Subach, F.V.1    Patterson, G.H.2    Renz, M.3    Lippincott-Schwartz, J.4    Verkhusha, V.V.5
  • 114
    • 84861085223 scopus 로고    scopus 로고
    • Multicolor single molecule tracking of stochastically active synthetic dyes
    • Benke A, Olivier N, Gunzenhäuser J, &, Manley S, (2012) Multicolor single molecule tracking of stochastically active synthetic dyes. Nano Lett 12, 2619-2624.
    • (2012) Nano Lett , vol.12 , pp. 2619-2624
    • Benke, A.1    Olivier, N.2    Gunzenhäuser, J.3    Manley, S.4


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