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Volumn 1746, Issue 3, 2005, Pages 234-251

Toward understanding the dynamics of membrane-raft-based molecular interactions

Author keywords

Chemical fixation; Immunofluorescence colocalization; Raft domain; Temporary molecular interaction; Time scale; Transient recruitment

Indexed keywords

ANTIBODY; CELL PROTEIN; CHOLERA TOXIN; GANGLIOSIDE GM1; GLUTARALDEHYDE; PARAFORMALDEHYDE;

EID: 29144483525     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2005.10.001     Document Type: Review
Times cited : (203)

References (107)
  • 1
    • 0020455954 scopus 로고
    • Spin-label saturation-transfer electron spin resonance detection of transient association of rhodopsin in reconstituted membranes
    • A. Kusumi, and J.S. Hyde Spin-label saturation-transfer electron spin resonance detection of transient association of rhodopsin in reconstituted membranes Biochemistry 21 1982 5978 5983
    • (1982) Biochemistry , vol.21 , pp. 5978-5983
    • Kusumi, A.1    Hyde, J.S.2
  • 2
    • 0023864445 scopus 로고
    • Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: Temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact: I. Biochemical analysis
    • M. Pasdar, and W.J. Nelson Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact: I. Biochemical analysis J. Cell Biol. 106 1988 677 685
    • (1988) J. Cell Biol. , vol.106 , pp. 677-685
    • Pasdar, M.1    Nelson, W.J.2
  • 3
    • 0023838729 scopus 로고
    • Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: Temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact: II. Morphological analysis
    • M. Pasdar, and W.J. Nelson Kinetics of desmosome assembly in Madin-Darby canine kidney epithelial cells: temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact: II. Morphological analysis J. Cell Biol. 106 1988 687 695
    • (1988) J. Cell Biol. , vol.106 , pp. 687-695
    • Pasdar, M.1    Nelson, W.J.2
  • 4
    • 0024383949 scopus 로고
    • Regulation of desmosome assembly in epithelial cells: Kinetics of synthesis, transport, and stabilization of desmoglein I, a major protein of the membrane core domain
    • M. Pasdar, and W.J. Nelson Regulation of desmosome assembly in epithelial cells: kinetics of synthesis, transport, and stabilization of desmoglein I, a major protein of the membrane core domain J. Cell Biol. 109 1989 163 177
    • (1989) J. Cell Biol. , vol.109 , pp. 163-177
    • Pasdar, M.1    Nelson, W.J.2
  • 6
    • 0036702299 scopus 로고    scopus 로고
    • Plasma membrane microdomains
    • F.R. Maxfield Plasma membrane microdomains Curr. Opin. Cell Biol. 14 2002 483 487
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 483-487
    • Maxfield, F.R.1
  • 7
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • A.D. Douglass, and R.D. Vale Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells Cell 121 2005 937 950
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 8
    • 29144528298 scopus 로고    scopus 로고
    • Without a raft
    • B. Nichols Without a raft Nature 436 2005 608 609
    • (2005) Nature , vol.436 , pp. 608-609
    • Nichols, B.1
  • 9
    • 0038788003 scopus 로고    scopus 로고
    • Mechanism of Lck recruitment to the T-cell receptor cluster as studied by single-molecule-fluorescence video imaging
    • H. Ike, A. Kosugi, A. Kato, R. Iino, H. Hirano, T. Fujiwara, K. Ritchie, and A. Kusumi Mechanism of Lck recruitment to the T-cell receptor cluster as studied by single-molecule-fluorescence video imaging Chemphyschem 4 2003 620 626
    • (2003) Chemphyschem , vol.4 , pp. 620-626
    • Ike, H.1    Kosugi, A.2    Kato, A.3    Iino, R.4    Hirano, H.5    Fujiwara, T.6    Ritchie, K.7    Kusumi, A.8
  • 10
    • 0041731992 scopus 로고    scopus 로고
    • Lipid rafts make for slippery platforms
    • E.C. Lai Lipid rafts make for slippery platforms J. Cell Biol. 162 2003 365 370
    • (2003) J. Cell Biol. , vol.162 , pp. 365-370
    • Lai, E.C.1
  • 11
    • 0034707082 scopus 로고    scopus 로고
    • Insolubility of lipids in Triton X-100: Physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts)
    • E. London, and D.A. Brown Insolubility of lipids in Triton X-100: physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts) Biochim. Biophys. Acta 1508 2000 182 195
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 182-195
    • London, E.1    Brown, D.A.2
  • 12
    • 0031964607 scopus 로고    scopus 로고
    • Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains
    • R.J. Schroeder, S.N. Ahmed, Y. Zhu, E. London, and D.A. Brown Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains J. Biol. Chem. 273 1998 1150 1157
    • (1998) J. Biol. Chem. , vol.273 , pp. 1150-1157
    • Schroeder, R.J.1    Ahmed, S.N.2    Zhu, Y.3    London, E.4    Brown, D.A.5
  • 14
    • 0036841874 scopus 로고    scopus 로고
    • Triton promotes domain formation in lipid raft mixtures
    • H. Heerklotz Triton promotes domain formation in lipid raft mixtures Biophys. J. 83 2002 2693 2701
    • (2002) Biophys. J. , vol.83 , pp. 2693-2701
    • Heerklotz, H.1
  • 15
    • 0038730762 scopus 로고    scopus 로고
    • The sensitivity of lipid domains to small perturbations demonstrated by the effect of Triton
    • H. Heerklotz, H. Szadkowska, T. Anderson, and J. Seelig The sensitivity of lipid domains to small perturbations demonstrated by the effect of Triton J. Mol. Biol. 329 2003 793 799
    • (2003) J. Mol. Biol. , vol.329 , pp. 793-799
    • Heerklotz, H.1    Szadkowska, H.2    Anderson, T.3    Seelig, J.4
  • 16
    • 1842536499 scopus 로고    scopus 로고
    • Rafts: Scale-dependent, active lipid organization at the cell surface
    • S. Mayor, and M. Rao Rafts: scale-dependent, active lipid organization at the cell surface Traffic 5 2004 231 240
    • (2004) Traffic , vol.5 , pp. 231-240
    • Mayor, S.1    Rao, M.2
  • 17
    • 1842432088 scopus 로고    scopus 로고
    • Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts
    • A. Kusumi, I. Koyama-Honda, and K. Suzuki Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts Traffic 5 2004 213 230
    • (2004) Traffic , vol.5 , pp. 213-230
    • Kusumi, A.1    Koyama-Honda, I.2    Suzuki, K.3
  • 18
    • 0037429658 scopus 로고    scopus 로고
    • Dynamics of raft molecules in the cell and artificial membranes: Approaches by pulse EPR spin labeling and single molecule optical microscopy
    • W.K. Subczynski, and A. Kusumi Dynamics of raft molecules in the cell and artificial membranes: approaches by pulse EPR spin labeling and single molecule optical microscopy Biochim. Biophys. Acta 1610 2003 231 243
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 231-243
    • Subczynski, W.K.1    Kusumi, A.2
  • 19
    • 23844460833 scopus 로고    scopus 로고
    • Cold-induced coalescence of T-cell plasma membrane microdomains activates signalling pathways
    • A.I. Magee, J. Adler, and I. Parmryd Cold-induced coalescence of T-cell plasma membrane microdomains activates signalling pathways J. Cell Sci. 118 2005 3141 3151
    • (2005) J. Cell Sci. , vol.118 , pp. 3141-3151
    • Magee, A.I.1    Adler, J.2    Parmryd, I.3
  • 23
    • 0037874731 scopus 로고    scopus 로고
    • Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy
    • G.J. Schütz, G. Kada, V.P. Pastushenko, and H. Schindler Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy EMBO J. 19 2000 892 901
    • (2000) EMBO J. , vol.19 , pp. 892-901
    • Schütz, G.J.1    Kada, G.2    Pastushenko, V.P.3    Schindler, H.4
  • 24
    • 0345255797 scopus 로고    scopus 로고
    • Visualization of protein compartmentation within the plasma membrane of living yeast cells
    • K. Malinska, J. Malinsky, M. Opekarova, and W. Tanner Visualization of protein compartmentation within the plasma membrane of living yeast cells Mol. Biol. Cell 14 2003 4427 4436
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4427-4436
    • Malinska, K.1    Malinsky, J.2    Opekarova, M.3    Tanner, W.4
  • 25
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of living cells
    • D.A. Zacharias, J.D. Violin, A.C. Newton, and R.Y. Tsien Partitioning of lipid-modified monomeric GFPs into membrane microdomains of living cells Science 296 2002 913 916
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 26
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking
    • S. Mayor, K.G. Rothberg, and F.R. Maxfield Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking Science 264 1994 1948 1951
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.G.2    Maxfield, F.R.3
  • 27
    • 0030878573 scopus 로고    scopus 로고
    • Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains
    • T. Harder, and K. Simons Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains Curr. Opin. Cell Biol. 9 1997 534 542
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 534-542
    • Harder, T.1    Simons, K.2
  • 28
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • T. Harder, P. Scheiffele, P. Verkade, and K. Simons Lipid domain structure of the plasma membrane revealed by patching of membrane components J. Cell. Biol. 141 1998 929 942
    • (1998) J. Cell. Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 29
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • I.A. Prior, C. Muncke, R.G. Parton, and J.F. Hancock Direct visualization of Ras proteins in spatially distinct cell surface microdomains J. Cell Biol. 160 2003 165 170
    • (2003) J. Cell Biol. , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 30
    • 27344456331 scopus 로고    scopus 로고
    • H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton
    • S.S. Plowman, C. Muncke, R.G. Parton, and J.F. Hancock H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton Proc. Natl. Acad. Sci. U. S. A. 102 2005 15500 15505
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15500-15505
    • Plowman, S.S.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 31
    • 0031563789 scopus 로고    scopus 로고
    • The motility-associated proteins GAP-43, MARCKS, and CAP-23 share unique targeting and surface activity-inducing properties
    • A. Wiederkehr, J. Staple, and P. Caroni The motility-associated proteins GAP-43, MARCKS, and CAP-23 share unique targeting and surface activity-inducing properties Exp. Cell Res. 236 1997 103 116
    • (1997) Exp. Cell Res. , vol.236 , pp. 103-116
    • Wiederkehr, A.1    Staple, J.2    Caroni, P.3
  • 32
    • 0034717707 scopus 로고    scopus 로고
    • GAP43, MARCKS, and CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism
    • T. Laux, K. Fukami, M. Thelen, T. Golub, D. Frey, and P. Caroni GAP43, MARCKS, and CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism J. Cell Biol. 149 2000 1455 1471
    • (2000) J. Cell Biol. , vol.149 , pp. 1455-1471
    • Laux, T.1    Fukami, K.2    Thelen, M.3    Golub, T.4    Frey, D.5    Caroni, P.6
  • 33
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • P. Sharma, R. Varma, R.C. Sarasij, I.G. Krishnamoorthy, M. Rao, and S. Mayor Nanoscale organization of multiple GPI-anchored proteins in living cell membranes Cell 116 2004 577 589
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    Krishnamoorthy, I.G.4    Rao, M.5    Mayor, S.6
  • 34
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • R. Varma, and S. Mayor GPI-anchored proteins are organized in submicron domains at the cell surface Nature 394 1998 798 801
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 35
    • 0029946890 scopus 로고    scopus 로고
    • Constrained diffusion or immobile fraction on cell surfaces: A new interpretation
    • T.J. Feder, I. Brust-Mascher, J.P. Slattery, B. Baird, and W.W. Webb Constrained diffusion or immobile fraction on cell surfaces: a new interpretation Biophys. J. 70 1996 2767 2773
    • (1996) Biophys. J. , vol.70 , pp. 2767-2773
    • Feder, T.J.1    Brust-Mascher, I.2    Slattery, J.P.3    Baird, B.4    Webb, W.W.5
  • 36
    • 1542399850 scopus 로고    scopus 로고
    • Lipid raft proteins have a random distribution during localized activation of the T-cell receptor
    • O.O. Glebov, and B.J. Nichols Lipid raft proteins have a random distribution during localized activation of the T-cell receptor Na. Cell Biol. 6 2004 238 243
    • (2004) Na. Cell Biol. , vol.6 , pp. 238-243
    • Glebov, O.O.1    Nichols, B.J.2
  • 37
    • 0034075971 scopus 로고    scopus 로고
    • High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes
    • A.K. Kenworthy, N. Petranova, and M. Edidin High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes Mol. Biol. Cell 11 2000 1645 1655
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1645-1655
    • Kenworthy, A.K.1    Petranova, N.2    Edidin, M.3
  • 38
    • 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 fluorescence resonance energy transfer
    • A.K. Kenworthy, and M. Edidin Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 A using imaging fluorescence resonance energy transfer J. Cell Biol. 142 1998 69 84
    • (1998) J. Cell Biol. , vol.142 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 39
    • 0026783791 scopus 로고
    • Long tail kinetics in biophysics?
    • J.F. Nagle Long tail kinetics in biophysics? Biophys. J. 63 1992 366 370
    • (1992) Biophys. J. , vol.63 , pp. 366-370
    • Nagle, J.F.1
  • 40
    • 0037446837 scopus 로고    scopus 로고
    • GM1-containing lipid rafts are depleted within clathrin-coated pits
    • B.J. Nichols GM1-containing lipid rafts are depleted within clathrin-coated pits Curr. Biol. 13 2003 686 690
    • (2003) Curr. Biol. , vol.13 , pp. 686-690
    • Nichols, B.J.1
  • 41
    • 1442274700 scopus 로고    scopus 로고
    • Lipid rafts and plasma microorganization: Insights from Ras
    • R.G. Parton, and J.F. Hancock Lipid rafts and plasma microorganization: insights from Ras Trends Cell Biol. 14 2004 141 147
    • (2004) Trends Cell Biol. , vol.14 , pp. 141-147
    • Parton, R.G.1    Hancock, J.F.2
  • 42
  • 43
    • 11244339619 scopus 로고    scopus 로고
    • Cholesterol depletion suppresses the translational movement of class II major histocompatibility complex proteins in the plasma membrane
    • M. Vrljic, S.Y. Nishimura, W.E. Moerner, and H.M. McConnell Cholesterol depletion suppresses the translational movement of class II major histocompatibility complex proteins in the plasma membrane Biophys. J. 88 2005 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
  • 46
    • 0012050693 scopus 로고
    • Lateral and rotational diffusion of bacteriorhodopsin in lipid bilayers: Experimental test of the Saffman-Delbrück equations
    • R. Peters, and R.J. Cherry Lateral and rotational diffusion of bacteriorhodopsin in lipid bilayers: experimental test of the Saffman-Delbrück equations Proc. Natl. Acad. Sci. U. S. A. 79 1982 4317 4321
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 4317-4321
    • Peters, R.1    Cherry, R.J.2
  • 47
    • 0020491932 scopus 로고
    • Size dependence of the translational diffusion of large integral membrane proteins in liquid-crystalline phase lipid bilayers. a study using fluorescence recovery after photobleaching
    • W.L. Vaz, M. Criado, V.M. Madeira, G. Schoellmann, and T.M. Jovin Size dependence of the translational diffusion of large integral membrane proteins in liquid-crystalline phase lipid bilayers. A study using fluorescence recovery after photobleaching Biochemistry 21 1982 5608 5612
    • (1982) Biochemistry , vol.21 , pp. 5608-5612
    • Vaz, W.L.1    Criado, M.2    Madeira, V.M.3    Schoellmann, G.4    Jovin, T.M.5
  • 48
    • 0037054546 scopus 로고    scopus 로고
    • Phospholipids undergo hop diffusion in compartmentalized cell membrane
    • T. Fujiwara, K. Ritchie, H. Murakoshi, K. Jacobson, and A. Kusumi Phospholipids undergo hop diffusion in compartmentalized cell membrane J. Cell Biol. 157 2002 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
  • 49
    • 17844364513 scopus 로고    scopus 로고
    • Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: High-speed single-molecule tracking of membrane molecules
    • A. Kusumi, C. Nakada, K. Ritchie, K. Murase, K. Suzuki, H. Murakoshi, R.S. Kasai, J. Kondo, and T. Fujiwara Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules Annu. Rev. Biophys. Biomol. Struct. 34 2005 351 378
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 351-378
    • Kusumi, A.1    Nakada, C.2    Ritchie, K.3    Murase, K.4    Suzuki, K.5    Murakoshi, H.6    Kasai, R.S.7    Kondo, J.8    Fujiwara, T.9
  • 51
    • 0028243194 scopus 로고
    • Compartmentalized structure of the plasma membrane for receptor movements as revealed by a nanometer-level motion analysis
    • Y. Sako, and A. Kusumi Compartmentalized structure of the plasma membrane for receptor movements as revealed by a nanometer-level motion analysis J. Cell Biol. 125 1994 1251 1264
    • (1994) J. Cell Biol. , vol.125 , pp. 1251-1264
    • Sako, Y.1    Kusumi, A.2
  • 52
    • 0029014265 scopus 로고
    • Barriers for lateral diffusion of transferrin receptor in the plasma membrane as characterized by receptor dragging by laser tweezers: Fence versus tether
    • Y. Sako, and A. Kusumi Barriers for lateral diffusion of transferrin receptor in the plasma membrane as characterized by receptor dragging by laser tweezers: fence versus tether J. Cell Biol. 129 1995 1559 1574
    • (1995) J. Cell Biol. , vol.129 , pp. 1559-1574
    • Sako, Y.1    Kusumi, A.2
  • 53
    • 0032498847 scopus 로고    scopus 로고
    • Cytoplasmic regulation of the movement of E-cadherin on the free cell surface as studied by optical tweezers and single particle tracking: Corralling and tethering by the membrane skeleton
    • Y. Sako, A. Nagafuchi, S. Tsukita, M. Takeichi, and A. Kusumi Cytoplasmic regulation of the movement of E-cadherin on the free cell surface as studied by optical tweezers and single particle tracking: corralling and tethering by the membrane skeleton J. Cell Biol. 140 1998 1227 1240
    • (1998) J. Cell Biol. , vol.140 , pp. 1227-1240
    • Sako, Y.1    Nagafuchi, A.2    Tsukita, S.3    Takeichi, M.4    Kusumi, A.5
  • 54
    • 0032563615 scopus 로고    scopus 로고
    • Regulation mechanism of the lateral diffusion of band 3 in erythrocyte membranes by the membrane skeleton
    • M. Tomishige, Y. Sako, and A. Kusumi Regulation mechanism of the lateral diffusion of band 3 in erythrocyte membranes by the membrane skeleton J. Cell Biol. 142 1998 989 1000
    • (1998) J. Cell Biol. , vol.142 , pp. 989-1000
    • Tomishige, M.1    Sako, Y.2    Kusumi, A.3
  • 55
    • 0026071516 scopus 로고
    • Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins
    • M.M. Sperotto, and O.G. Mouritsen Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins Biophys. J. 59 1991 261 270
    • (1991) Biophys. J. , vol.59 , pp. 261-270
    • Sperotto, M.M.1    Mouritsen, O.G.2
  • 56
    • 0026658542 scopus 로고
    • Lateral diffusion and percolation in two-phase, two-component lipid bilayers. Topology of the solid-phase domains in-plane and across the lipid bilayer
    • P.F.F. Almeida, W.L.C. Vaz, and T.E. Thompson Lateral diffusion and percolation in two-phase, two-component lipid bilayers. Topology of the solid-phase domains in-plane and across the lipid bilayer Biochemistry 31 1992 7198 7210
    • (1992) Biochemistry , vol.31 , pp. 7198-7210
    • Almeida, P.F.F.1    Vaz, W.L.C.2    Thompson, T.E.3
  • 57
    • 0029310846 scopus 로고
    • Numerical simulations of the effect of hydrodynamic interactions on diffusivities of integral membrane proteins
    • T.L. Dodd, D.A. Hammer, A.S. Sangani, and D.L. Koch Numerical simulations of the effect of hydrodynamic interactions on diffusivities of integral membrane proteins J. Fluid Mech. 293 1995 147 180
    • (1995) J. Fluid Mech. , vol.293 , pp. 147-180
    • Dodd, T.L.1    Hammer, D.A.2    Sangani, A.S.3    Koch, D.L.4
  • 58
    • 0034995774 scopus 로고    scopus 로고
    • Single molecule imaging of green fluorescent proteins in living cells: E-cadherin forms oligomers on the free cell surface
    • R. Iino, I. Koyama, and A. Kusumi Single molecule imaging of green fluorescent proteins in living cells: E-cadherin forms oligomers on the free cell surface Biophys. J. 80 2001 2667 2677
    • (2001) Biophys. J. , vol.80 , pp. 2667-2677
    • Iino, R.1    Koyama, I.2    Kusumi, A.3
  • 59
    • 17844389341 scopus 로고    scopus 로고
    • Rapid hop diffusion of a G-protein-coupled receptor in the plasma membrane as revealed by single-molecule techniques
    • K. Suzuki, K. Ritchie, E. Kajikawa, T. Fujiwara, and A. Kusumi Rapid hop diffusion of a G-protein-coupled receptor in the plasma membrane as revealed by single-molecule techniques Biophys. J. 88 2005 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
  • 60
    • 0034764754 scopus 로고    scopus 로고
    • Condensed complexes and the calorimetry of cholesterol-phospholipid bilayers
    • T.G. Anderson, and H.M. McConnell Condensed complexes and the calorimetry of cholesterol-phospholipid bilayers Biophys. J. 81 2001 2774 2785
    • (2001) Biophys. J. , vol.81 , pp. 2774-2785
    • Anderson, T.G.1    McConnell, H.M.2
  • 61
    • 0036788567 scopus 로고    scopus 로고
    • A thermodynamic model for extended complexes of cholesterol and phospholipid
    • T.G. Anderson, and H.M. McConnell A thermodynamic model for extended complexes of cholesterol and phospholipid Biophys. J. 83 2002 2039 2052
    • (2002) Biophys. J. , vol.83 , pp. 2039-2052
    • Anderson, T.G.1    McConnell, H.M.2
  • 62
    • 0037429704 scopus 로고    scopus 로고
    • Condensed complexes of cholesterol and phospholipids
    • H.M. McConnell, and A. Radhakrishnan Condensed complexes of cholesterol and phospholipids Biochim. Biophys. Acta 1610 2003 159 173
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 159-173
    • McConnell, H.M.1    Radhakrishnan, A.2
  • 64
    • 0037136069 scopus 로고    scopus 로고
    • Two fatty acids can replace one phospholipid in condensed complexes with cholesterol
    • T.M. Okonogi, A. Radhakrishnan, and H.M. McConnell Two fatty acids can replace one phospholipid in condensed complexes with cholesterol Biochim. Biophys. Acta 1564 2002 1 4
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 1-4
    • Okonogi, T.M.1    Radhakrishnan, A.2    McConnell, H.M.3
  • 65
    • 0033732176 scopus 로고    scopus 로고
    • Condensed complexes, rafts, and the chemical activity of cholesterol in membranes
    • A. Radhakrishnan, T.G. Anderson, and H.M. McConnell Condensed complexes, rafts, and the chemical activity of cholesterol in membranes Proc. Natl. Acad. Sci. U. S. A. 97 2000 12422 12427
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 12422-12427
    • Radhakrishnan, A.1    Anderson, T.G.2    McConnell, H.M.3
  • 66
  • 67
    • 0037036135 scopus 로고    scopus 로고
    • A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains
    • R.G. Anderson, and K. Jacobson A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains Science 296 2002 1821 1825
    • (2002) Science , vol.296 , pp. 1821-1825
    • Anderson, R.G.1    Jacobson, K.2
  • 68
    • 0021837375 scopus 로고
    • Exchange rates and numbers of annular lipids for the calcium and magnesium ion dependent adenosinetriphosphatase
    • J.M. East, D. Melville, and A.G. Lee Exchange rates and numbers of annular lipids for the calcium and magnesium ion dependent adenosinetriphosphatase Biochemistry 24 1985 2615 2623
    • (1985) Biochemistry , vol.24 , pp. 2615-2623
    • East, J.M.1    Melville, D.2    Lee, A.G.3
  • 69
    • 0024284789 scopus 로고
    • Exchange rates at the lipid-protein interface of myelin proteolipid protein studied by spin-label electron spin resonance
    • L.I. Horvath, P.J. Brophy, and D. Marsh Exchange rates at the lipid-protein interface of myelin proteolipid protein studied by spin-label electron spin resonance Biochemistry 27 1988 46 52
    • (1988) Biochemistry , vol.27 , pp. 46-52
    • Horvath, L.I.1    Brophy, P.J.2    Marsh, D.3
  • 73
    • 0035937857 scopus 로고    scopus 로고
    • Crystal structure of alkaline phosphatase from human placenta at 1.8 a resolution. Implication for a substrate specificity
    • M.H. Le Du, T. Stigbrand, M.J. Taussig, A. Menez, and E.A. Stura Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity J. Biol. Chem. 276 2001 9158 9165
    • (2001) J. Biol. Chem. , vol.276 , pp. 9158-9165
    • Le Du, M.H.1    Stigbrand, T.2    Taussig, M.J.3    Menez, A.4    Stura, E.A.5
  • 74
    • 0037008103 scopus 로고    scopus 로고
    • Proximity of the protein moiety of a GPI-anchored protein to the membrane surface: A FRET study
    • M.T. Lehto, and F.J. Sharom Proximity of the protein moiety of a GPI-anchored protein to the membrane surface: a FRET study Biochemistry 41 2002 8368 8376
    • (2002) Biochemistry , vol.41 , pp. 8368-8376
    • Lehto, M.T.1    Sharom, F.J.2
  • 75
    • 0035142949 scopus 로고    scopus 로고
    • Pulse EPR detection of lipid exchange between protein-rich raft and bulk domains in the membrane: Methodology development and its application to studies of influenza viral membrane
    • K. Kawasaki, J.J. Yin, W.K. Subczynski, J.S. Hyde, and A. Kusumi Pulse EPR detection of lipid exchange between protein-rich raft and bulk domains in the membrane: methodology development and its application to studies of influenza viral membrane Biophys. J. 80 2001 738 748
    • (2001) Biophys. J. , vol.80 , pp. 738-748
    • Kawasaki, K.1    Yin, J.J.2    Subczynski, W.K.3    Hyde, J.S.4    Kusumi, A.5
  • 76
    • 0242599280 scopus 로고    scopus 로고
    • Formaldehyde, formalin, paraformaldehyde and glutaraldehyde: What they are and what they do
    • J.A. Kiernan Formaldehyde, formalin, paraformaldehyde and glutaraldehyde: what they are and what they do Microsc. Today 00-1 2000 8 12
    • (2000) Microsc. Today , vol.1 , pp. 8-12
    • Kiernan, J.A.1
  • 77
    • 0026558912 scopus 로고
    • The structure of glutaraldehyde in aqueous solution determined by ultraviolet adsorption and light scattering
    • J. Kawahara, T. Ohmori, T. Ohkubo, S. Hattori, and M. Kawamura The structure of glutaraldehyde in aqueous solution determined by ultraviolet adsorption and light scattering Anal. Biochem. 201 1992 94 98
    • (1992) Anal. Biochem. , vol.201 , pp. 94-98
    • Kawahara, J.1    Ohmori, T.2    Ohkubo, T.3    Hattori, S.4    Kawamura, M.5
  • 78
    • 0014414239 scopus 로고
    • Glutaraldehyde as a protein crosslinkage reagent
    • F.M. Richards, and J.R. Knowles Glutaraldehyde as a protein crosslinkage reagent J. Mol. Biol. 37 1968 231 233
    • (1968) J. Mol. Biol. , vol.37 , pp. 231-233
    • Richards, F.M.1    Knowles, J.R.2
  • 79
    • 0000411099 scopus 로고
    • Reaction of formaldehyde with proteins
    • H. Frankel-Conrat, and H.S. Olcott Reaction of formaldehyde with proteins J. Biol. Chem. 174 1948 827 843
    • (1948) J. Biol. Chem. , vol.174 , pp. 827-843
    • Frankel-Conrat, H.1    Olcott, H.S.2
  • 84
    • 0033178166 scopus 로고    scopus 로고
    • Dynamics of molecules involved in antigen presentation: Effects of fixation
    • B.G. Barisas, W.F. Wada, T.M. Jovin, A. Jovin, and D.A. Roess Dynamics of molecules involved in antigen presentation: effects of fixation Mol. Immunol. 36 1999 701 708
    • (1999) Mol. Immunol. , vol.36 , pp. 701-708
    • Barisas, B.G.1    Wada, W.F.2    Jovin, T.M.3    Jovin, A.4    Roess, D.A.5
  • 85
    • 1242317020 scopus 로고    scopus 로고
    • Increased diffusional mobility of CFTR at the plasma membrane after deletion of its C-terminal PDZ binding motif
    • P.M. Haggie, B.A. Stanton, and A.S. Verkman Increased diffusional mobility of CFTR at the plasma membrane after deletion of its C-terminal PDZ binding motif J. Biol. Chem. 279 2004 5494 5500
    • (2004) J. Biol. Chem. , vol.279 , pp. 5494-5500
    • Haggie, P.M.1    Stanton, B.A.2    Verkman, A.S.3
  • 86
    • 0034075677 scopus 로고    scopus 로고
    • CAMP regulated membrane diffusion of a green fluorescent protein-auaporin 2 chimera
    • F. Umenishi, J.M. Verbavatz, and A.S. Verkman cAMP regulated membrane diffusion of a green fluorescent protein-auaporin 2 chimera Biophys. J. 78 2000 1024 1035
    • (2000) Biophys. J. , vol.78 , pp. 1024-1035
    • Umenishi, F.1    Verbavatz, J.M.2    Verkman, A.S.3
  • 87
    • 0031793885 scopus 로고    scopus 로고
    • Regionalized lipid diffusion in the plasma membrane of mammalian spermatozoa
    • C.A. Wolfe, P.S. James, A.R. Mackie, S. Ladha, and R. Jones Regionalized lipid diffusion in the plasma membrane of mammalian spermatozoa Biol. Reprod. 59 1998 1506 1514
    • (1998) Biol. Reprod. , vol.59 , pp. 1506-1514
    • Wolfe, C.A.1    James, P.S.2    MacKie, A.R.3    Ladha, S.4    Jones, R.5
  • 88
    • 0015507640 scopus 로고
    • Rhodopsin rotates in the visual receptor membrane
    • P.K. Brown Rhodopsin rotates in the visual receptor membrane Nat. New Biol. 236 1972 35 38
    • (1972) Nat. New Biol. , vol.236 , pp. 35-38
    • Brown, P.K.1
  • 89
    • 0015507871 scopus 로고
    • Rotational diffusion of rhodopsin in the visual receptor membrane
    • R.A. Cone Rotational diffusion of rhodopsin in the visual receptor membrane Nat. New Biol. 236 1972 39 43
    • (1972) Nat. New Biol. , vol.236 , pp. 39-43
    • Cone, R.A.1
  • 90
    • 0017804539 scopus 로고
    • Rotational motion of rhodopsin in the visual receptor membrane as studied by saturation transfer spectroscopy
    • A. Kusumi, S. Ohnishi, T. Ito, and T. Yoshizawa Rotational motion of rhodopsin in the visual receptor membrane as studied by saturation transfer spectroscopy Biochim. Biophys. Acta 507 1978 539 543
    • (1978) Biochim. Biophys. Acta , vol.507 , pp. 539-543
    • Kusumi, A.1    Ohnishi, S.2    Ito, T.3    Yoshizawa, T.4
  • 91
    • 0019202941 scopus 로고
    • Protein-lipid interaction on rhodopsin recombinant membranes as studied by protein rotational mobility and lipid alkyl chain flexibility measurement
    • A. Kusumi, T. Sakaki, T. Yoshizawa, and S. Ohnishi Protein-lipid interaction on rhodopsin recombinant membranes as studied by protein rotational mobility and lipid alkyl chain flexibility measurement J. Biochem. 88 1980 1103 1111
    • (1980) J. Biochem. , vol.88 , pp. 1103-1111
    • Kusumi, A.1    Sakaki, T.2    Yoshizawa, T.3    Ohnishi, S.4
  • 92
    • 22344442585 scopus 로고    scopus 로고
    • Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutinin
    • S.T. Hess, M. Kumar, A. Verma, J. Farrington, A. Kenworthy, and J. Zimmerberg Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutinin J. Cell Biol. 169 2005 965 976
    • (2005) J. Cell Biol. , vol.169 , pp. 965-976
    • Hess, S.T.1    Kumar, M.2    Verma, A.3    Farrington, J.4    Kenworthy, A.5    Zimmerberg, J.6
  • 94
    • 1542379962 scopus 로고    scopus 로고
    • The membrane domains occupied by glycosylphosphatidylinositol-anchored prion protein and Thy-1 differ in lipid composition
    • B. Brügger, C. Graham, I. Leibrecht, E. Mombelli, A. Jen, F. Wieland, and R. Morris The membrane domains occupied by glycosylphosphatidylinositol-anchored prion protein and Thy-1 differ in lipid composition J. Biol. Chem. 279 2004 7530 7536
    • (2004) J. Biol. Chem. , vol.279 , pp. 7530-7536
    • Brügger, B.1    Graham, C.2    Leibrecht, I.3    Mombelli, E.4    Jen, A.5    Wieland, F.6    Morris, R.7
  • 96
    • 0037445938 scopus 로고    scopus 로고
    • Imaging metabolism of phosphatidylinositol 4,5-bisphosphate in T-cell GM1-enriched domains containing Ras proteins
    • I. Parmryd, J. Adler, R. Patel, and A.I. Magee Imaging metabolism of phosphatidylinositol 4,5-bisphosphate in T-cell GM1-enriched domains containing Ras proteins Exp. Cell Res. 285 2003 27 38
    • (2003) Exp. Cell Res. , vol.285 , pp. 27-38
    • Parmryd, I.1    Adler, J.2    Patel, R.3    Magee, A.I.4
  • 97
    • 0031041581 scopus 로고    scopus 로고
    • Compartmentalized activation of the high affinity immunoglobulin e receptor within membrane domains
    • K.A. Field, D. Holowka, and B. Baird Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains J. Biol. Chem. 272 1997 4276 4280
    • (1997) J. Biol. Chem. , vol.272 , pp. 4276-4280
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 98
    • 0033577805 scopus 로고    scopus 로고
    • Critical role for cholesterol in Lyn-mediated tyrosine phosphorylation of FcepsilonRI and their association with detergent-resistant membranes
    • E.D. Sheets, D. Holowka, and B. Baird Critical role for cholesterol in Lyn-mediated tyrosine phosphorylation of FcepsilonRI and their association with detergent-resistant membranes J. Cell Biol. 145 1999 877 887
    • (1999) J. Cell Biol. , vol.145 , pp. 877-887
    • Sheets, E.D.1    Holowka, D.2    Baird, B.3
  • 99
    • 0034069892 scopus 로고    scopus 로고
    • Interactions between Fc(epsilon)RI and lipid raft components are regulated by the actin cytoskeleton
    • D. Holowka, E.D. Sheets, and B. Baird Interactions between Fc(epsilon)RI and lipid raft components are regulated by the actin cytoskeleton J. Cell Sci. 113 2000 1009 1019
    • (2000) J. Cell Sci. , vol.113 , pp. 1009-1019
    • Holowka, D.1    Sheets, E.D.2    Baird, B.3
  • 100
    • 4644364556 scopus 로고    scopus 로고
    • Visualization of plasma membrane compartmentalization with patterned lipid bilayers
    • M. Wu, D. Holowka, H.G. Craighead, and B. Baird Visualization of plasma membrane compartmentalization with patterned lipid bilayers Proc. Natl. Acad. Sci. U. S. A. 101 2004 13798 13803
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 13798-13803
    • Wu, M.1    Holowka, D.2    Craighead, H.G.3    Baird, B.4
  • 102
    • 4344676836 scopus 로고    scopus 로고
    • Lipid rafts mediate association of LFA-1 and CD3 and formation of the immunological synapse of CTL
    • M.R. Marwali, M.A. MacLeod, D.N. Muzia, and F. Takei Lipid rafts mediate association of LFA-1 and CD3 and formation of the immunological synapse of CTL J. Immunol. 173 2004 2960 2967
    • (2004) J. Immunol. , vol.173 , pp. 2960-2967
    • Marwali, M.R.1    MacLeod, M.A.2    Muzia, D.N.3    Takei, F.4
  • 103
    • 0027970448 scopus 로고
    • Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae
    • A.M. Fra, E. Williamson, K. Simons, and R.G. Parton Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae J. Biol. Chem. 269 1994 30745 30748
    • (1994) J. Biol. Chem. , vol.269 , pp. 30745-30748
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 104
    • 0032727709 scopus 로고    scopus 로고
    • Aggregation of Lipid rafts accompanies signaling via the T cell antigen receptor
    • P.W. Janes, S.C. Ley, and A.I. Magee Aggregation of Lipid rafts accompanies signaling via the T cell antigen receptor J. Cell Biol. 147 1999 447 461
    • (1999) J. Cell Biol. , vol.147 , pp. 447-461
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3
  • 105
    • 0037087307 scopus 로고    scopus 로고
    • Lipid microdomain clustering induces a redistribution of antigen recognition and adhesion molecules on human T lymphocyte
    • J.S. Mitchell, O. Kanca, and B.W. McIntyre Lipid microdomain clustering induces a redistribution of antigen recognition and adhesion molecules on human T lymphocyte J. Immunol. 168 2002 2737 2744
    • (2002) J. Immunol. , vol.168 , pp. 2737-2744
    • Mitchell, J.S.1    Kanca, O.2    McIntyre, B.W.3
  • 106
    • 0033613826 scopus 로고    scopus 로고
    • T lymphocyte costimulation mediated by reorganization of membrane microdomain
    • A. Viola, S. Schroeder, Y. Sakakibara, and A. Lanzavecchia T lymphocyte costimulation mediated by reorganization of membrane microdomain Science 283 1999 680 682
    • (1999) Science , vol.283 , pp. 680-682
    • Viola, A.1    Schroeder, S.2    Sakakibara, Y.3    Lanzavecchia, A.4
  • 107
    • 0345599000 scopus 로고    scopus 로고
    • Differently anchored influenza hemagglutinin mutants display distinct interaction dynamics with mutual rafts
    • D.E. Shvartsman, M. Kotler, R.D. Tall, M.G. Roth, and Y.I. Henis Differently anchored influenza hemagglutinin mutants display distinct interaction dynamics with mutual rafts J. Cell Biol. 163 2003 879 888
    • (2003) J. Cell Biol. , vol.163 , pp. 879-888
    • Shvartsman, D.E.1    Kotler, M.2    Tall, R.D.3    Roth, M.G.4    Henis, Y.I.5


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