메뉴 건너뛰기




Volumn 36, Issue 8, 2007, Pages 849-860

Functional membrane diffusion of G-protein coupled receptors

Author keywords

Cytoskeleton; FRAP; Membrane domain; Protein interactions; Signal transduction; SPT

Indexed keywords

G PROTEIN COUPLED RECEPTOR; LIGAND;

EID: 35748932049     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-007-0214-7     Document Type: Review
Times cited : (27)

References (76)
  • 1
    • 2142766875 scopus 로고    scopus 로고
    • Different structural states of the proteolipid membrane are produced by ligand binding to the human delta-opioid receptor as shown by plasmon-waveguide resonance spectroscopy
    • Alves ID, Cowell SM, Salamon Z, Devanathan S, Tollin G, Hruby VJ (2004) Different structural states of the proteolipid membrane are produced by ligand binding to the human delta-opioid receptor as shown by plasmon-waveguide resonance spectroscopy. Mol Pharmacol 65:1248-1257
    • (2004) Mol Pharmacol , vol.65 , pp. 1248-1257
    • Alves, I.D.1    Cowell, S.M.2    Salamon, Z.3    Devanathan, S.4    Tollin, G.5    Hruby, V.J.6
  • 3
    • 0031025764 scopus 로고    scopus 로고
    • Internal rafficking and surface mobility of a functionally intact beta2-adrenergic receptor-green fluorescent protein conjugate
    • Barak LS, Ferguson SS, Zhang J, Martenson C, Meyer T, Caron MG (1997) Internal rafficking and surface mobility of a functionally intact beta2-adrenergic receptor-green fluorescent protein conjugate. Mol Pharmacol 51:177-184
    • (1997) Mol Pharmacol , vol.51 , pp. 177-184
    • Barak, L.S.1    Ferguson, S.S.2    Zhang, J.3    Martenson, C.4    Meyer, T.5    Caron, M.G.6
  • 4
    • 33947382269 scopus 로고    scopus 로고
    • Investigating membrane protein dynamics in living cells
    • Bates IR, Wiseman PW, Hanrahan JW (2006) Investigating membrane protein dynamics in living cells. Biochem Cell Biol 84:825-831
    • (2006) Biochem Cell Biol , vol.84 , pp. 825-831
    • Bates, I.R.1    Wiseman, P.W.2    Hanrahan, J.W.3
  • 5
    • 0033118334 scopus 로고    scopus 로고
    • Molecular tinkering of G protein-coupled receptors: An evolutionary success
    • Bockaert J, Pin JP (1999) Molecular tinkering of G protein-coupled receptors: an evolutionary success. Embo J 18:1723-1729
    • (1999) Embo J , vol.18 , pp. 1723-1729
    • Bockaert, J.1    Pin, J.P.2
  • 6
    • 33846453991 scopus 로고    scopus 로고
    • Transient directed motions of GABA(A) receptors in growth cones detected by a speed correlation index
    • Bouzigues C, Dahan M (2007) Transient directed motions of GABA(A) receptors in growth cones detected by a speed correlation index. Biophys J 92:654-660
    • (2007) Biophys J , vol.92 , pp. 654-660
    • Bouzigues, C.1    Dahan, M.2
  • 7
    • 0034009390 scopus 로고    scopus 로고
    • Signal transduction: Hanging on a scaffold
    • Burack WR, Shaw AS (2000) Signal transduction: hanging on a scaffold. Curr Opin Cell Biol 12:211-216
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 211-216
    • Burack, W.R.1    Shaw, A.S.2
  • 9
    • 0032493759 scopus 로고    scopus 로고
    • Binding and phosphorylation of tubulin by G protein-coupled receptor kinases
    • Carman CV, Som T, Kim CM, Benovic JL (1998) Binding and phosphorylation of tubulin by G protein-coupled receptor kinases. J Biol Chem 273:20308-20316
    • (1998) J Biol Chem , vol.273 , pp. 20308-20316
    • Carman, C.V.1    Som, T.2    Kim, C.M.3    Benovic, J.L.4
  • 10
    • 7244250134 scopus 로고    scopus 로고
    • Dynamic confinement of NK2 receptors in the plasma membrane. Improved FRAP analysis and biological relevance
    • Cezanne L, Lecat S, Lagane B, Millot C, Vollmer JY, Matthes H, Galzi JL, Lopez A (2004) Dynamic confinement of NK2 receptors in the plasma membrane. Improved FRAP analysis and biological relevance. J Biol Chem 279:45057-45067
    • (2004) J Biol Chem , vol.279 , pp. 45057-45067
    • Cezanne, L.1    Lecat, S.2    Lagane, B.3    Millot, C.4    Vollmer, J.Y.5    Matthes, H.6    Galzi, J.L.7    Lopez, A.8
  • 11
    • 33746303104 scopus 로고    scopus 로고
    • Methods to measure the lateral diffusion of membrane lipids and proteins
    • Chen Y, Lagerholm BC, Yang B, Jacobson K (2006) Methods to measure the lateral diffusion of membrane lipids and proteins. Methods 39:147-153
    • (2006) Methods , vol.39 , pp. 147-153
    • Chen, Y.1    Lagerholm, B.C.2    Yang, B.3    Jacobson, K.4
  • 12
    • 0032030621 scopus 로고    scopus 로고
    • Rethinking receptor-G protein-effector interactions
    • Chidiac P (1998) Rethinking receptor-G protein-effector interactions. Biochem Pharmacol 55:549-556
    • (1998) Biochem Pharmacol , vol.55 , pp. 549-556
    • Chidiac, P.1
  • 13
    • 0038439320 scopus 로고    scopus 로고
    • The role of receptor diffusion in the organization of the postsynaptic membrane
    • Choquet D, Triller A (2003) The role of receptor diffusion in the organization of the postsynaptic membrane. Nat Rev Neurosci 4:251-265
    • (2003) Nat Rev Neurosci , vol.4 , pp. 251-265
    • Choquet, D.1    Triller, A.2
  • 14
    • 0036209874 scopus 로고    scopus 로고
    • Endocytosis of G protein-coupled receptors: Roles of G protein-coupled receptor kinases and beta-arrestin proteins
    • Claing A, Laporte SA, Caron MG, Lefkowitz RJ (2002) Endocytosis of G protein-coupled receptors: roles of G protein-coupled receptor kinases and beta-arrestin proteins. Prog Neurobiol 66:61-79
    • (2002) Prog Neurobiol , vol.66 , pp. 61-79
    • Claing, A.1    Laporte, S.A.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 15
    • 12244298862 scopus 로고    scopus 로고
    • Confined diffusion without fences of a g-protein-coupled receptor as revealed by single particle tracking
    • Daumas F, Destainville N, Millot C, Lopez A, Dean D, Salome L (2003) Confined diffusion without fences of a g-protein-coupled receptor as revealed by single particle tracking. Biophys J 84:356-366
    • (2003) Biophys J , vol.84 , pp. 356-366
    • Daumas, F.1    Destainville, N.2    Millot, C.3    Lopez, A.4    Dean, D.5    Salome, L.6
  • 17
    • 33646194548 scopus 로고    scopus 로고
    • Quantification and correction of systematic errors due to detector time-averaging in single-molecule tracking experiments
    • Destainville N, Salome L (2006) Quantification and correction of systematic errors due to detector time-averaging in single-molecule tracking experiments. Biophys J 90:L17-L19
    • (2006) Biophys J , vol.90
    • Destainville, N.1    Salome, L.2
  • 18
    • 0036214457 scopus 로고    scopus 로고
    • Relationship of lipid rafts to transient confinement zones detected by single particle tracking
    • Dietrich C, Yang B, Fujiwara T, Kusumi A, Jacobson K (2002) Relationship of lipid rafts to transient confinement zones detected by single particle tracking. Biophys J 82:274-284
    • (2002) Biophys J , vol.82 , pp. 274-284
    • Dietrich, C.1    Yang, B.2    Fujiwara, T.3    Kusumi, A.4    Jacobson, K.5
  • 19
  • 20
    • 28444437064 scopus 로고    scopus 로고
    • Membranes are more mosaic than fluid
    • Engelman DM (2005) Membranes are more mosaic than fluid. Nature 438:578-580
    • (2005) Nature , vol.438 , pp. 578-580
    • Engelman, D.M.1
  • 21
    • 0037054546 scopus 로고    scopus 로고
    • Phospholipids undergo hop diffusion in compartmentalized cell membrane
    • Fujiwara T, Ritchie K, Murakoshi H, Jacobson K, Kusumi A (2002) Phospholipids undergo hop diffusion in compartmentalized cell membrane. J Cell Biol 157:1071-1081
    • (2002) J Cell Biol , vol.157 , pp. 1071-1081
    • Fujiwara, T.1    Ritchie, K.2    Murakoshi, H.3    Jacobson, K.4    Kusumi, A.5
  • 24
    • 0036194867 scopus 로고    scopus 로고
    • Structure, composition, and peptide binding properties of detergent soluble bilayers and detergent resistant rafts
    • Gandhavadi M, Allende D, Vidal A, Simon SA, McIntosh TJ (2002) Structure, composition, and peptide binding properties of detergent soluble bilayers and detergent resistant rafts. Biophys J 82:1469-1482
    • (2002) Biophys J , vol.82 , pp. 1469-1482
    • Gandhavadi, M.1    Allende, D.2    Vidal, A.3    Simon, S.A.4    McIntosh, T.J.5
  • 25
    • 3242754218 scopus 로고    scopus 로고
    • Specific labeling of cell surface proteins with chemically diverse compounds
    • George N, Pick H, Vogel H, Johnsson N, Johnsson K (2004) Specific labeling of cell surface proteins with chemically diverse compounds. J Am Chem Soc 126:8896-8897
    • (2004) J Am Chem Soc , vol.126 , pp. 8896-8897
    • George, N.1    Pick, H.2    Vogel, H.3    Johnsson, N.4    Johnsson, K.5
  • 26
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman AG (1987) G proteins: transducers of receptor-generated signals. Annu Rev Biochem 56:615-649
    • (1987) Annu Rev Biochem , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 28
    • 12544257434 scopus 로고    scopus 로고
    • Differential effects of modification of membrane cholesterol and sphingolipids on the conformation, function, and trafficking of the G protein-coupled cholecystokinin receptor
    • Harikumar KG, Puri V, Singh RD, Hanada K, Pagano RE, Miller LJ (2005) Differential effects of modification of membrane cholesterol and sphingolipids on the conformation, function, and trafficking of the G protein-coupled cholecystokinin receptor. J Biol Chem 280:2176-2185
    • (2005) J Biol Chem , vol.280 , pp. 2176-2185
    • Harikumar, K.G.1    Puri, V.2    Singh, R.D.3    Hanada, K.4    Pagano, R.E.5    Miller, L.J.6
  • 31
    • 0033573876 scopus 로고    scopus 로고
    • Intrinsically fluorescent luteinizing hormone receptor demonstrates hormone-driven aggregation
    • Horvat RD, Nelson S, Clay CM, Barisas BG, Roess DA (1999) Intrinsically fluorescent luteinizing hormone receptor demonstrates hormone-driven aggregation. Biochem Biophys Res Commun 255:382-385
    • (1999) Biochem Biophys Res Commun , vol.255 , pp. 382-385
    • Horvat, R.D.1    Nelson, S.2    Clay, C.M.3    Barisas, B.G.4    Roess, D.A.5
  • 32
    • 33751211550 scopus 로고    scopus 로고
    • Analysis of transient behavior in complex trajectories: Application to secretory vesicle dynamics
    • Huet S, Karatekin E, Tran VS, Fanget I, Cribier S, Henry JP (2006) Analysis of transient behavior in complex trajectories: application to secretory vesicle dynamics. Biophys J 91:3542-3559
    • (2006) Biophys J , vol.91 , pp. 3542-3559
    • Huet, S.1    Karatekin, E.2    Tran, V.S.3    Fanget, I.4    Cribier, S.5    Henry, J.P.6
  • 33
    • 0036189809 scopus 로고    scopus 로고
    • G protein-coupled receptor signalling and cross-talk: Achieving rapidity and specificity
    • Hur EM, Kim KT (2002) G protein-coupled receptor signalling and cross-talk: achieving rapidity and specificity. Cell Signal 14:397-405
    • (2002) Cell Signal , vol.14 , pp. 397-405
    • Hur, E.M.1    Kim, K.T.2
  • 35
    • 33749243938 scopus 로고    scopus 로고
    • Visualizing odorant receptor trafficking in living cells down to the single-molecule level
    • Jacquier V, Prummer M, Segura JM, Pick H, Vogel H (2006) Visualizing odorant receptor trafficking in living cells down to the single-molecule level. Proc Natl Acad Sci USA 103:14325-14330
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 14325-14330
    • Jacquier, V.1    Prummer, M.2    Segura, J.M.3    Pick, H.4    Vogel, H.5
  • 36
    • 0025110290 scopus 로고
    • An inverse relationship between receptor internalization and the fraction of laterally mobile receptors for the vasopressin renal-type V2-receptor. An active role for receptor immobilization in down-regulation?
    • Jans DA, Peters R, Fahrenholz F (1990a) An inverse relationship between receptor internalization and the fraction of laterally mobile receptors for the vasopressin renal-type V2-receptor. An active role for receptor immobilization in down-regulation? FEBS Lett 274:223-226
    • (1990) FEBS Lett , vol.274 , pp. 223-226
    • Jans, D.A.1    Peters, R.2    Fahrenholz, F.3
  • 37
    • 0025182369 scopus 로고
    • Lateral mobility of the phospholipase C-activating vasopressin V1-type receptor in A7r5 smooth muscle cells: A comparison with the adenylate cyclase-coupled V2-receptor
    • Jans DA, Peters R, Fahrenholz F (1990b) Lateral mobility of the phospholipase C-activating vasopressin V1-type receptor in A7r5 smooth muscle cells: a comparison with the adenylate cyclase-coupled V2-receptor. Embo J 9:2693-2699
    • (1990) Embo J , vol.9 , pp. 2693-2699
    • Jans, D.A.1    Peters, R.2    Fahrenholz, F.3
  • 38
    • 0024456622 scopus 로고
    • The adenylate cyclase-coupled vasopressin V2-receptor is highly laterally mobile in membranes of LLC-PK1 renal epithelial cells at physiological temperature
    • Jans DA, Peters R, Zsigo J, Fahrenholz F (1989) The adenylate cyclase-coupled vasopressin V2-receptor is highly laterally mobile in membranes of LLC-PK1 renal epithelial cells at physiological temperature. Embo J 8:2481-2488
    • (1989) Embo J , vol.8 , pp. 2481-2488
    • Jans, D.A.1    Peters, R.2    Zsigo, J.3    Fahrenholz, F.4
  • 39
    • 20744433934 scopus 로고    scopus 로고
    • Ligand-induced partitioning of human CXCR1 chemokine receptors with lipid raft microenvironments facilitates G-protein-dependent signaling
    • Jiao X, Zhang N, Xu X, Oppenheim JJ, Jin T (2005) Ligand-induced partitioning of human CXCR1 chemokine receptors with lipid raft microenvironments facilitates G-protein-dependent signaling. Mol Cell Biol 25:5752-5762
    • (2005) Mol Cell Biol , vol.25 , pp. 5752-5762
    • Jiao, X.1    Zhang, N.2    Xu, X.3    Oppenheim, J.J.4    Jin, T.5
  • 40
    • 0034193130 scopus 로고    scopus 로고
    • Using green fluorescent proteins to study G-protein-coupled receptor localization and trafficking
    • Kallal L, Benovic JL (2000) Using green fluorescent proteins to study G-protein-coupled receptor localization and trafficking. Trends Pharmacol Sci 21:175-180
    • (2000) Trends Pharmacol Sci , vol.21 , pp. 175-180
    • Kallal, L.1    Benovic, J.L.2
  • 41
    • 0036463901 scopus 로고    scopus 로고
    • Efficacy at G-protein-coupled receptors
    • Kenakin T (2002) Efficacy at G-protein-coupled receptors. Nat Rev 11:103-110
    • (2002) Nat Rev , vol.11 , pp. 103-110
    • Kenakin, T.1
  • 42
    • 3042798261 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function
    • Kristiansen K (2004) Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: molecular modeling and mutagenesis approaches to receptor structure and function. Pharmacol Ther 103:21-80
    • (2004) Pharmacol Ther , vol.103 , pp. 21-80
    • Kristiansen, K.1
  • 43
    • 0345564815 scopus 로고    scopus 로고
    • Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin
    • Kwik J, Boyle S, Fooksman D, Margolis L, Sheetz MP, Edidin M (2003) Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin. Proc Natl Acad Sci USA 100:13964-13969
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13964-13969
    • Kwik, J.1    Boyle, S.2    Fooksman, D.3    Margolis, L.4    Sheetz, M.P.5    Edidin, M.6
  • 45
    • 23944505054 scopus 로고    scopus 로고
    • Kinetics of the initial steps of g protein-coupled receptor-mediated cellular signaling revealed by single-molecule imaging
    • Lill Y, Martinez KL, Lill MA, Meyer BH, Vogel H, Hecht B (2005) Kinetics of the initial steps of g protein-coupled receptor-mediated cellular signaling revealed by single-molecule imaging. Chemphyschem 6:1633-1640
    • (2005) Chemphyschem , vol.6 , pp. 1633-1640
    • Lill, Y.1    Martinez, K.L.2    Lill, M.A.3    Meyer, B.H.4    Vogel, H.5    Hecht, B.6
  • 46
    • 33747591249 scopus 로고    scopus 로고
    • Dynamics in the plasma membrane: How to combine fluidity and order
    • Marguet D, Lenne PF, Rigneault H, He HT (2006) Dynamics in the plasma membrane: how to combine fluidity and order. Embo J 25:3446-3457
    • (2006) Embo J , vol.25 , pp. 3446-3457
    • Marguet, D.1    Lenne, P.F.2    Rigneault, H.3    He, H.T.4
  • 48
    • 0037452553 scopus 로고    scopus 로고
    • Lateral mobility and specific binding to GABA(A) receptors on hippocampal neurons monitored by fluorescence correlation spectroscopy
    • Meissner O, Haberlein H (2003) Lateral mobility and specific binding to GABA(A) receptors on hippocampal neurons monitored by fluorescence correlation spectroscopy. Biochemistry 42:1667-1672
    • (2003) Biochemistry , vol.42 , pp. 1667-1672
    • Meissner, O.1    Haberlein, H.2
  • 49
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • Munro S (2003) Lipid rafts: elusive or illusive? Cell 115:377-388
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 50
    • 0032961873 scopus 로고    scopus 로고
    • Characterization of an intrinsically fluorescent gonadotropin-releasing hormone receptor and effects of ligand binding on receptor lateral diffusion
    • Nelson S, Horvat RD, Malvey J, Roess DA, Barisas BG, Clay CM (1999) Characterization of an intrinsically fluorescent gonadotropin-releasing hormone receptor and effects of ligand binding on receptor lateral diffusion. Endocrinology 140:950-957
    • (1999) Endocrinology , vol.140 , pp. 950-957
    • Nelson, S.1    Horvat, R.D.2    Malvey, J.3    Roess, D.A.4    Barisas, B.G.5    Clay, C.M.6
  • 51
    • 0027936892 scopus 로고
    • Membrane organization in G-protein mechanisms
    • Neubig RR (1994) Membrane organization in G-protein mechanisms. FASEB J 8:939-946
    • (1994) FASEB J , vol.8 , pp. 939-946
    • Neubig, R.R.1
  • 52
    • 0022005299 scopus 로고
    • Differences in the lateral mobility of receptors for luteinizing hormone (LH) in the luteal cell plasma membrane when occupied by ovine LH versus human chorionic gonadotropin
    • Niswender GD, Roess DA, Sawyer HR, Silvia WJ, Barisas BG (1985) Differences in the lateral mobility of receptors for luteinizing hormone (LH) in the luteal cell plasma membrane when occupied by ovine LH versus human chorionic gonadotropin. Endocrinology 116:164-169
    • (1985) Endocrinology , vol.116 , pp. 164-169
    • Niswender, G.D.1    Roess, D.A.2    Sawyer, H.R.3    Silvia, W.J.4    Barisas, B.G.5
  • 53
    • 0041494100 scopus 로고    scopus 로고
    • Lipid rafts: Bringing order to chaos
    • Pike LJ (2003) Lipid rafts: bringing order to chaos. J Lipid Res 44:655-667
    • (2003) J Lipid Res , vol.44 , pp. 655-667
    • Pike, L.J.1
  • 54
    • 33746085241 scopus 로고    scopus 로고
    • Rafts defined: A report on the keystone symposium on lipid rafts and cell function
    • Pike LJ (2006) Rafts defined: a report on the keystone symposium on lipid rafts and cell function. J Lipid Res 47:1597-1598
    • (2006) J Lipid Res , vol.47 , pp. 1597-1598
    • Pike, L.J.1
  • 55
    • 33847037508 scopus 로고    scopus 로고
    • Cholesterol depletion induces dynamic confinement of the G-protein coupled serotonin(1A) receptor in the plasma membrane of living cells
    • Pucadyil TJ, Chattopadhyay A (2007) Cholesterol depletion induces dynamic confinement of the G-protein coupled serotonin(1A) receptor in the plasma membrane of living cells. Biochim Biophys Acta 1768:655-668
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 655-668
    • Pucadyil, T.J.1    Chattopadhyay, A.2
  • 56
    • 10844293498 scopus 로고    scopus 로고
    • G-protein-dependent cell surface dynamics of the human serotonin1A receptor tagged to yellow fluorescent protein
    • Pucadyil TJ, Kalipatnapu S, Harikumar KG, Rangaraj N, Karnik SS, Chattopadhyay A (2004) G-protein-dependent cell surface dynamics of the human serotonin1A receptor tagged to yellow fluorescent protein. Biochemistry 43:15852-15862
    • (2004) Biochemistry , vol.43 , pp. 15852-15862
    • Pucadyil, T.J.1    Kalipatnapu, S.2    Harikumar, K.G.3    Rangaraj, N.4    Karnik, S.S.5    Chattopadhyay, A.6
  • 58
    • 0034522937 scopus 로고    scopus 로고
    • Luteinizing hormone receptors are self-associated in the plasma membrane
    • Roess DA, Horvat RD, Munnelly H, Barisas BG (2000) Luteinizing hormone receptors are self-associated in the plasma membrane. Endocrinology 141:4518-4523
    • (2000) Endocrinology , vol.141 , pp. 4518-4523
    • Roess, D.A.1    Horvat, R.D.2    Munnelly, H.3    Barisas, B.G.4
  • 59
    • 0032950226 scopus 로고    scopus 로고
    • Regulation of lateral mobility and cellular trafficking of the CCK receptor by a partial agonist
    • Roettger BF, Pinon DI, Burghardt TP, Miller LJ (1999) Regulation of lateral mobility and cellular trafficking of the CCK receptor by a partial agonist. Am J Physiol 276:C539-C547
    • (1999) Am J Physiol , vol.276
    • Roettger, B.F.1    Pinon, D.I.2    Burghardt, T.P.3    Miller, L.J.4
  • 61
    • 0036945389 scopus 로고    scopus 로고
    • Binding of agonists, antagonists and inverse agonists to the human delta-opioid receptor produces distinctly different conformational states distinguishable by plasmon-waveguide resonance spectroscopy
    • Salamon Z, Hruby VJ, Tollin G, Cowell S (2002) Binding of agonists, antagonists and inverse agonists to the human delta-opioid receptor produces distinctly different conformational states distinguishable by plasmon-waveguide resonance spectroscopy. J Pept Res 60:322-328
    • (2002) J Pept Res , vol.60 , pp. 322-328
    • Salamon, Z.1    Hruby, V.J.2    Tollin, G.3    Cowell, S.4
  • 62
    • 0031851201 scopus 로고    scopus 로고
    • Characterization of membrane domains by FRAP experiments at variable observation areas
    • Salome L, Cazeils JL, Lopez A, Tocanne JF (1998) Characterization of membrane domains by FRAP experiments at variable observation areas. Eur Biophys J 27:391-402
    • (1998) Eur Biophys J , vol.27 , pp. 391-402
    • Salome, L.1    Cazeils, J.L.2    Lopez, A.3    Tocanne, J.F.4
  • 63
    • 33748758457 scopus 로고    scopus 로고
    • Diffusion of the mu opioid receptor at the surface of human neuroblastoma SH-SY5Y cells is restricted to permeable domains
    • Sauliere A, Gaibelet G, Millot C, Mazeres S, Lopez A, Salome L (2006) Diffusion of the mu opioid receptor at the surface of human neuroblastoma SH-SY5Y cells is restricted to permeable domains. FEBS Lett 580:5227-5231
    • (2006) FEBS Lett , vol.580 , pp. 5227-5231
    • Sauliere, A.1    Gaibelet, G.2    Millot, C.3    Mazeres, S.4    Lopez, A.5    Salome, L.6
  • 64
    • 0037095771 scopus 로고    scopus 로고
    • Receptor activation and homer differentially control the lateral mobility of metabotropic glutamate receptor 5 in the neuronal membrane
    • Serge A, Fourgeaud L, Hemar A, Choquet D (2002) Receptor activation and homer differentially control the lateral mobility of metabotropic glutamate receptor 5 in the neuronal membrane. J Neurosci 22:3910-3920
    • (2002) J Neurosci , vol.22 , pp. 3910-3920
    • Serge, A.1    Fourgeaud, L.2    Hemar, A.3    Choquet, D.4
  • 65
    • 0348143123 scopus 로고    scopus 로고
    • Active surface transport of metabotropic glutamate receptors through binding to microtubules and actin flow
    • Serge A, Fourgeaud L, Hemar A, Choquet D (2003) Active surface transport of metabotropic glutamate receptors through binding to microtubules and actin flow. J Cell Sci 116:5015-5022
    • (2003) J Cell Sci , vol.116 , pp. 5015-5022
    • Serge, A.1    Fourgeaud, L.2    Hemar, A.3    Choquet, D.4
  • 66
    • 33645520326 scopus 로고    scopus 로고
    • Luteinizing hormone receptors translocate to plasma membrane microdomains after binding of human chorionic gonadotropin
    • Smith SM, Lei Y, Liu J, Cahill ME, Hagen GM, Barisas BG, Roess DA (2006) Luteinizing hormone receptors translocate to plasma membrane microdomains after binding of human chorionic gonadotropin. Endocrinology 147:1789-1795
    • (2006) Endocrinology , vol.147 , pp. 1789-1795
    • Smith, S.M.1    Lei, Y.2    Liu, J.3    Cahill, M.E.4    Hagen, G.M.5    Barisas, B.G.6    Roess, D.A.7
  • 67
    • 4143105734 scopus 로고    scopus 로고
    • Mobility of the human immunodeficiency virus (HIV) receptor CD4 and coreceptor CCR5 in living cells: Implications for HIV fusion and entry events
    • Steffens CM, Hope TJ (2004) Mobility of the human immunodeficiency virus (HIV) receptor CD4 and coreceptor CCR5 in living cells: implications for HIV fusion and entry events. J Virol 78:9573-9578
    • (2004) J Virol , vol.78 , pp. 9573-9578
    • Steffens, C.M.1    Hope, T.J.2
  • 68
    • 17844389341 scopus 로고    scopus 로고
    • Rapid hop diffusion of a G-protein-coupled receptor in the plasma membrane as revealed by single-molecule techniques
    • Suzuki K, Ritchie K, Kajikawa E, Fujiwara T, Kusumi A (2005) Rapid hop diffusion of a G-protein-coupled receptor in the plasma membrane as revealed by single-molecule techniques. Biophys J 88:3659-3680
    • (2005) Biophys J , vol.88 , pp. 3659-3680
    • Suzuki, K.1    Ritchie, K.2    Kajikawa, E.3    Fujiwara, T.4    Kusumi, A.5
  • 69
    • 33746006525 scopus 로고    scopus 로고
    • Evaluation of two novel tag-based labelling technologies for site-specific modification of proteins
    • Tirat A, Freuler F, Stettler T, Mayr LM, Leder L (2006) Evaluation of two novel tag-based labelling technologies for site-specific modification of proteins. Int J Biol Macromol 39:66-76
    • (2006) Int J Biol Macromol , vol.39 , pp. 66-76
    • Tirat, A.1    Freuler, F.2    Stettler, T.3    Mayr, L.M.4    Leder, L.5
  • 70
    • 0018125541 scopus 로고
    • Mode of coupling between the beta-adrenergic receptor and adenylate cyclase in turkey erythrocytes
    • Tolkovsky AM, Levitzki A (1978) Mode of coupling between the beta-adrenergic receptor and adenylate cyclase in turkey erythrocytes. Biochemistry 17:3795
    • (1978) Biochemistry , vol.17 , pp. 3795
    • Tolkovsky, A.M.1    Levitzki, A.2
  • 72
    • 11244339619 scopus 로고    scopus 로고
    • Cholesterol depletion suppresses the translational diffusion of class II major histocompatibility complex proteins in the plasma membrane
    • Vrljic M, Nishimura SY, Moerner WE, McConnell HM (2005) Cholesterol depletion suppresses the translational diffusion of class II major histocompatibility complex proteins in the plasma membrane. Biophys J 88:334-347
    • (2005) Biophys J , vol.88 , pp. 334-347
    • Vrljic, M.1    Nishimura, S.Y.2    Moerner, W.E.3    McConnell, H.M.4
  • 73
    • 28444443820 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization
    • Wawrezinieck L, Rigneault H, Marguet D, Lenne PF (2005) Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization. Biophys J 89:4029-4042
    • (2005) Biophys J , vol.89 , pp. 4029-4042
    • Wawrezinieck, L.1    Rigneault, H.2    Marguet, D.3    Lenne, P.F.4
  • 75
    • 0033082623 scopus 로고    scopus 로고
    • Photobleaching GFP reveals protein dynamics inside live cells
    • White J, Stelzer E (1999) Photobleaching GFP reveals protein dynamics inside live cells. Trends Cell Biol 9:61-65
    • (1999) Trends Cell Biol , vol.9 , pp. 61-65
    • White, J.1    Stelzer, E.2
  • 76
    • 0035397971 scopus 로고    scopus 로고
    • Agonist-dependent immobilization of chimeric bombesin/GRP receptors: Dependence on c-Src activity and dissociation from internalization
    • Young SH, Walsh JH, Rozengurt E, Slice LW (2001) Agonist-dependent immobilization of chimeric bombesin/GRP receptors: dependence on c-Src activity and dissociation from internalization. Exp Cell Res 267:37-44
    • (2001) Exp Cell Res , vol.267 , pp. 37-44
    • Young, S.H.1    Walsh, J.H.2    Rozengurt, E.3    Slice, L.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.