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Volumn 1853, Issue 4, 2015, Pages 830-840

The nanoscale organization of the B lymphocyte membrane

Author keywords

B cell antigen receptor; Nanocluster; Protein islands

Indexed keywords

B LYMPHOCYTE RECEPTOR; MEMBRANE PROTEIN; PROTEIN KINASE SYK; CELL SURFACE RECEPTOR; NANOPARTICLE;

EID: 84923164472     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2014.11.010     Document Type: Article
Times cited : (32)

References (129)
  • 1
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E., von Heijne G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 1998, 7:1029-1038.
    • (1998) Protein Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 2
    • 0034213573 scopus 로고    scopus 로고
    • Do more complex organisms have a greater proportion of membrane proteins in their genomes?
    • Stevens T.J., Arkin I.T. Do more complex organisms have a greater proportion of membrane proteins in their genomes?. Proteins 2000, 39:417-420.
    • (2000) Proteins , vol.39 , pp. 417-420
    • Stevens, T.J.1    Arkin, I.T.2
  • 3
    • 42949117368 scopus 로고    scopus 로고
    • Protein area occupancy at the center of the red blood cell membrane
    • Dupuy A.D., Engelman D.M. Protein area occupancy at the center of the red blood cell membrane. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:2848-2852.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 2848-2852
    • Dupuy, A.D.1    Engelman, D.M.2
  • 4
    • 25144443228 scopus 로고    scopus 로고
    • Cellular lipidomics
    • van Meer G. Cellular lipidomics. EMBO J. 2005, 24:3159-3165.
    • (2005) EMBO J. , vol.24 , pp. 3159-3165
    • van Meer, G.1
  • 5
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer S.J., Nicolson G.L. The fluid mosaic model of the structure of cell membranes. Science 1972, 175:720-731.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 6
    • 0029005840 scopus 로고
    • Revisiting the fluid mosaic model of membranes
    • Jacobson K., Sheets E.D., Simson R. Revisiting the fluid mosaic model of membranes. Science 1995, 268:1441-1442.
    • (1995) Science , vol.268 , pp. 1441-1442
    • Jacobson, K.1    Sheets, E.D.2    Simson, R.3
  • 7
    • 0036702299 scopus 로고    scopus 로고
    • Plasma membrane microdomains
    • Maxfield F.R. Plasma membrane microdomains. Curr. Opin. Cell Biol. 2002, 14:483-487.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 483-487
    • Maxfield, F.R.1
  • 8
    • 0036733284 scopus 로고    scopus 로고
    • Caveolae: from cell biology to animal physiology
    • Razani B., Woodman S.E., Lisanti M.P. Caveolae: from cell biology to animal physiology. Pharmacol. Rev. 2002, 54:431-467.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 431-467
    • Razani, B.1    Woodman, S.E.2    Lisanti, M.P.3
  • 9
    • 77952944942 scopus 로고    scopus 로고
    • The distribution and function of phosphatidylserine in cellular membranes
    • Leventis P.A., Grinstein S. The distribution and function of phosphatidylserine in cellular membranes. Annu. Rev. Biophys. 2010, 39:407-427.
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 407-427
    • Leventis, P.A.1    Grinstein, S.2
  • 10
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D., Simons K. Lipid rafts as a membrane-organizing principle. Science 2010, 327:46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 11
    • 84904015318 scopus 로고    scopus 로고
    • B cell activation involves nanoscale receptor reorganizations and inside-out signaling by Syk
    • Klasener K., Maity P.C., Hobeika E., Yang J., Reth M. B cell activation involves nanoscale receptor reorganizations and inside-out signaling by Syk. Elife 2014, 3:e02069.
    • (2014) Elife , vol.3 , pp. e02069
    • Klasener, K.1    Maity, P.C.2    Hobeika, E.3    Yang, J.4    Reth, M.5
  • 13
    • 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
    • Plowman S.J., Muncke C., Parton R.G., Hancock J.F. 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. 2005, 102:15500-15505.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15500-15505
    • Plowman, S.J.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 14
    • 3242699883 scopus 로고    scopus 로고
    • B-cell signal transduction: tyrosine phosphorylation, kinase activity, and calcium mobilization
    • Brummer T., Elis W., Reth M., Huber M. B-cell signal transduction: tyrosine phosphorylation, kinase activity, and calcium mobilization. Methods Mol. Biol. 2004, 271:189-212.
    • (2004) Methods Mol. Biol. , vol.271 , pp. 189-212
    • Brummer, T.1    Elis, W.2    Reth, M.3    Huber, M.4
  • 15
    • 29144483525 scopus 로고    scopus 로고
    • Toward understanding the dynamics of membrane-raft-based molecular interactions
    • Kusumi A., Suzuki K. Toward understanding the dynamics of membrane-raft-based molecular interactions. Biochim. Biophys. Acta 2005, 1746:234-251.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 234-251
    • Kusumi, A.1    Suzuki, K.2
  • 16
    • 1842432088 scopus 로고    scopus 로고
    • Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts
    • Kusumi A., Koyama-Honda I., Suzuki K. Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts. Traffic 2004, 5:213-230.
    • (2004) Traffic , vol.5 , pp. 213-230
    • Kusumi, A.1    Koyama-Honda, I.2    Suzuki, K.3
  • 19
    • 0020455954 scopus 로고
    • Spin-label saturation-transfer electron spin resonance detection of transient association of rhodopsin in reconstituted membranes
    • Kusumi A., Hyde J.S. Spin-label saturation-transfer electron spin resonance detection of transient association of rhodopsin in reconstituted membranes. Biochemistry 1982, 21:5978-5983.
    • (1982) Biochemistry , vol.21 , pp. 5978-5983
    • Kusumi, A.1    Hyde, J.S.2
  • 20
    • 84921514653 scopus 로고    scopus 로고
    • Approaches to analyze protein-protein interactions of membrane proteins
    • InTech, J. Cai (Ed.)
    • Hunke Sabine, Müller Volker S. Approaches to analyze protein-protein interactions of membrane proteins. Protein Interactions 2012, InTech, (ISBN: 978-953-51-0244-1). 10.5772/38069. J. Cai (Ed.).
    • (2012) Protein Interactions
    • Hunke, S.1    Müller, V.S.2
  • 22
    • 0034995774 scopus 로고    scopus 로고
    • Single molecule imaging of green fluorescent proteins in living cells: E-cadherin forms oligomers on the free cell surface
    • Iino R., Koyama I., Kusumi A. Single molecule imaging of green fluorescent proteins in living cells: E-cadherin forms oligomers on the free cell surface. Biophys. J. 2001, 80:2667-2677.
    • (2001) Biophys. J. , vol.80 , pp. 2667-2677
    • Iino, R.1    Koyama, I.2    Kusumi, A.3
  • 23
    • 78650512639 scopus 로고    scopus 로고
    • Breaking the diffraction barrier: super-resolution imaging of cells
    • Huang B., Babcock H., Zhuang X. Breaking the diffraction barrier: super-resolution imaging of cells. Cell 2010, 143:1047-1058.
    • (2010) Cell , vol.143 , pp. 1047-1058
    • Huang, B.1    Babcock, H.2    Zhuang, X.3
  • 24
    • 79953010049 scopus 로고    scopus 로고
    • Proteomic characterization of plasma membrane-proximal T cell activation responses
    • de Wet B., Zech T., Salek M., Acuto O., Harder T. Proteomic characterization of plasma membrane-proximal T cell activation responses. J. Biol. Chem. 2011, 286:4072-4080.
    • (2011) J. Biol. Chem. , vol.286 , pp. 4072-4080
    • de Wet, B.1    Zech, T.2    Salek, M.3    Acuto, O.4    Harder, T.5
  • 25
    • 0035957138 scopus 로고    scopus 로고
    • Immunoisolation of TCR signaling complexes from Jurkat T leukemic cells
    • Harder T., Kuhn M. Immunoisolation of TCR signaling complexes from Jurkat T leukemic cells. Sci. STKE 2001, 2001:l1.
    • (2001) Sci. STKE , vol.2001 , pp. l1
    • Harder, T.1    Kuhn, M.2
  • 27
    • 0033858039 scopus 로고    scopus 로고
    • Stability of the B cell antigen receptor complex
    • Schamel W.W., Reth M. Stability of the B cell antigen receptor complex. Mol. Immunol. 2000, 37:253-259.
    • (2000) Mol. Immunol. , vol.37 , pp. 253-259
    • Schamel, W.W.1    Reth, M.2
  • 30
    • 0036195136 scopus 로고    scopus 로고
    • An essential role for membrane rafts in the initiation of Fas/CD95-triggered cell death in mouse thymocytes
    • Hueber A.O., Bernard A.M., Herincs Z., Couzinet A., He H.T. An essential role for membrane rafts in the initiation of Fas/CD95-triggered cell death in mouse thymocytes. EMBO Rep. 2002, 3:190-196.
    • (2002) EMBO Rep. , vol.3 , pp. 190-196
    • Hueber, A.O.1    Bernard, A.M.2    Herincs, Z.3    Couzinet, A.4    He, H.T.5
  • 31
  • 32
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger H., von Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 1991, 199:223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    von Jagow, G.2
  • 33
    • 0033697266 scopus 로고    scopus 로고
    • Monomeric and oligomeric complexes of the B cell antigen receptor
    • Schamel W.W., Reth M. Monomeric and oligomeric complexes of the B cell antigen receptor. Immunity 2000, 13:5-14.
    • (2000) Immunity , vol.13 , pp. 5-14
    • Schamel, W.W.1    Reth, M.2
  • 34
    • 36549032156 scopus 로고    scopus 로고
    • SPINE: a method for the rapid detection and analysis of protein-protein interactions in vivo
    • Herzberg C., Weidinger L.A., Dorrbecker B., Hubner S., Stulke J., Commichau F.M. SPINE: a method for the rapid detection and analysis of protein-protein interactions in vivo. Proteomics 2007, 7:4032-4035.
    • (2007) Proteomics , vol.7 , pp. 4032-4035
    • Herzberg, C.1    Weidinger, L.A.2    Dorrbecker, B.3    Hubner, S.4    Stulke, J.5    Commichau, F.M.6
  • 35
    • 79955780957 scopus 로고    scopus 로고
    • Membrane-SPINE: an improved method to identify protein-protein interaction partners of membrane proteins in vivo
    • Muller V.S., Jungblut P.R., Meyer T.F., Hunke S. Membrane-SPINE: an improved method to identify protein-protein interaction partners of membrane proteins in vivo. Proteomics 2011, 11:2124-2128.
    • (2011) Proteomics , vol.11 , pp. 2124-2128
    • Muller, V.S.1    Jungblut, P.R.2    Meyer, T.F.3    Hunke, S.4
  • 36
    • 18744389180 scopus 로고    scopus 로고
    • Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells
    • Suchanek M., Radzikowska A., Thiele C. Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells. Nat. Methods 2005, 2:261-267.
    • (2005) Nat. Methods , vol.2 , pp. 261-267
    • Suchanek, M.1    Radzikowska, A.2    Thiele, C.3
  • 38
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • Rust M.J., Bates M., Zhuang X. Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat. Methods 2006, 3:793-795.
    • (2006) Nat. Methods , vol.3 , pp. 793-795
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3
  • 39
    • 0028460042 scopus 로고
    • Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy
    • Hell S.W., Wichmann J. Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy. Opt. Lett. 1994, 19:780-782.
    • (1994) Opt. Lett. , vol.19 , pp. 780-782
    • Hell, S.W.1    Wichmann, J.2
  • 40
    • 0032607671 scopus 로고    scopus 로고
    • Subdiffraction resolution in far-field fluorescence microscopy
    • Klar T.A., Hell S.W. Subdiffraction resolution in far-field fluorescence microscopy. Opt. Lett. 1999, 24:954-956.
    • (1999) Opt. Lett. , vol.24 , pp. 954-956
    • Klar, T.A.1    Hell, S.W.2
  • 41
    • 0036674522 scopus 로고    scopus 로고
    • Saturated patterned excitation microscopy-a concept for optical resolution improvement
    • Heintzmann R., Jovin T.M., Cremer C. Saturated patterned excitation microscopy-a concept for optical resolution improvement. J. Opt. Soc. Am. A Opt. Image Sci. Vis. 2002, 19:1599-1609.
    • (2002) J. Opt. Soc. Am. A Opt. Image Sci. Vis. , vol.19 , pp. 1599-1609
    • Heintzmann, R.1    Jovin, T.M.2    Cremer, C.3
  • 42
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • Patterson G.H., Lippincott-Schwartz J. A photoactivatable GFP for selective photolabeling of proteins and cells. Science 2002, 297:1873-1877.
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 45
    • 56749104130 scopus 로고    scopus 로고
    • Fluorescent probes for super-resolution imaging in living cells
    • Fernandez-Suarez M., Ting A.Y. Fluorescent probes for super-resolution imaging in living cells. Nat. Rev. Mol. Cell Biol. 2008, 9:929-943.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 929-943
    • Fernandez-Suarez, M.1    Ting, A.Y.2
  • 49
    • 42949083695 scopus 로고    scopus 로고
    • Live-cell photoactivated localization microscopy of nanoscale adhesion dynamics
    • Shroff H., Galbraith C.G., Galbraith J.A., Betzig E. Live-cell photoactivated localization microscopy of nanoscale adhesion dynamics. Nat. Methods 2008, 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
  • 50
    • 84856386755 scopus 로고    scopus 로고
    • Optimal 3D single-molecule localization for superresolution microscopy with aberrations and engineered point spread functions
    • Quirin S., Pavani S.R., Piestun R. Optimal 3D single-molecule localization for superresolution microscopy with aberrations and engineered point spread functions. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:675-679.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 675-679
    • Quirin, S.1    Pavani, S.R.2    Piestun, R.3
  • 51
    • 38949216802 scopus 로고    scopus 로고
    • Three-dimensional super-resolution imaging by stochastic optical reconstruction microscopy
    • Huang B., Wang W., Bates M., Zhuang X. Three-dimensional super-resolution imaging by stochastic optical reconstruction microscopy. Science 2008, 319:810-813.
    • (2008) Science , vol.319 , pp. 810-813
    • Huang, B.1    Wang, W.2    Bates, M.3    Zhuang, X.4
  • 52
    • 0034682512 scopus 로고    scopus 로고
    • Fluorescence microscopy with diffraction resolution barrier broken by stimulated emission
    • Klar T.A., Jakobs S., Dyba M., Egner A., Hell S.W. Fluorescence microscopy with diffraction resolution barrier broken by stimulated emission. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:8206-8210.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8206-8210
    • Klar, T.A.1    Jakobs, S.2    Dyba, M.3    Egner, A.4    Hell, S.W.5
  • 54
    • 0016366591 scopus 로고
    • Fluorescence correlation spectroscopy. II. An experimental realization
    • Magde D., Elson E.L., Webb W.W. Fluorescence correlation spectroscopy. II. An experimental realization. Biopolymers 1974, 13:29-61.
    • (1974) Biopolymers , vol.13 , pp. 29-61
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 55
    • 0019494948 scopus 로고
    • Cell-substrate contacts illuminated by total internal reflection fluorescence
    • Axelrod D. Cell-substrate contacts illuminated by total internal reflection fluorescence. J. Cell Biol. 1981, 89:141-145.
    • (1981) J. Cell Biol. , vol.89 , pp. 141-145
    • Axelrod, D.1
  • 56
    • 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. Relationship of lipid rafts to transient confinement zones detected by single particle tracking. Biophys. J. 2002, 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
  • 57
    • 0029162080 scopus 로고
    • Detection of temporary lateral confinement of membrane proteins using single-particle tracking analysis
    • Simson R., Sheets E.D., Jacobson K. Detection of temporary lateral confinement of membrane proteins using single-particle tracking analysis. Biophys. J. 1995, 69:989-993.
    • (1995) Biophys. J. , vol.69 , pp. 989-993
    • Simson, R.1    Sheets, E.D.2    Jacobson, K.3
  • 58
    • 28444443820 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization
    • Wawrezinieck L., Rigneault H., Marguet D., Lenne P.F. Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization. Biophys. J. 2005, 89:4029-4042.
    • (2005) Biophys. J. , vol.89 , pp. 4029-4042
    • Wawrezinieck, L.1    Rigneault, H.2    Marguet, D.3    Lenne, P.F.4
  • 59
    • 79953730584 scopus 로고    scopus 로고
    • Detecting nanodomains in living cell membrane by fluorescence correlation spectroscopy
    • He H.T., Marguet D. Detecting nanodomains in living cell membrane by fluorescence correlation spectroscopy. Annu. Rev. Phys. Chem. 2011, 62:417-436.
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 417-436
    • He, H.T.1    Marguet, D.2
  • 60
    • 79551678673 scopus 로고    scopus 로고
    • Oligomerization state of dynamin 2 in cell membranes using TIRF and number and brightness analysis
    • Ross J.A., Digman M.A., Wang L., Gratton E., Albanesi J.P., Jameson D.M. Oligomerization state of dynamin 2 in cell membranes using TIRF and number and brightness analysis. Biophys. J. 2011, 100:L15-L17.
    • (2011) Biophys. J. , vol.100 , pp. L15-L17
    • Ross, J.A.1    Digman, M.A.2    Wang, L.3    Gratton, E.4    Albanesi, J.P.5    Jameson, D.M.6
  • 64
    • 84892140345 scopus 로고    scopus 로고
    • Pre-clustering of the B cell antigen receptor demonstrated by mathematically extended electron microscopy
    • Fiala G.J., Kaschek D., Blumenthal B., Reth M., Timmer J., Schamel W.W. Pre-clustering of the B cell antigen receptor demonstrated by mathematically extended electron microscopy. Front. Immunol. 2013, 4:427.
    • (2013) Front. Immunol. , vol.4 , pp. 427
    • Fiala, G.J.1    Kaschek, D.2    Blumenthal, B.3    Reth, M.4    Timmer, J.5    Schamel, W.W.6
  • 65
    • 0034728966 scopus 로고    scopus 로고
    • Observing FcepsilonRI signaling from the inside of the mast cell membrane
    • Wilson B.S., Pfeiffer J.R., Oliver J.M. Observing FcepsilonRI signaling from the inside of the mast cell membrane. J. Cell Biol. 2000, 149:1131-1142.
    • (2000) J. Cell Biol. , vol.149 , pp. 1131-1142
    • Wilson, B.S.1    Pfeiffer, J.R.2    Oliver, J.M.3
  • 66
    • 0036032969 scopus 로고    scopus 로고
    • FcepsilonRI signaling observed from the inside of the mast cell membrane
    • Wilson B.S., Pfeiffer J.R., Oliver J.M. FcepsilonRI signaling observed from the inside of the mast cell membrane. Mol. Immunol. 2002, 38:1259-1268.
    • (2002) Mol. Immunol. , vol.38 , pp. 1259-1268
    • Wilson, B.S.1    Pfeiffer, J.R.2    Oliver, J.M.3
  • 67
    • 1442274700 scopus 로고    scopus 로고
    • Lipid rafts and plasma membrane microorganization: insights from Ras
    • Parton R.G., Hancock J.F. Lipid rafts and plasma membrane microorganization: insights from Ras. Trends Cell Biol. 2004, 14:141-147.
    • (2004) Trends Cell Biol. , vol.14 , pp. 141-147
    • Parton, R.G.1    Hancock, J.F.2
  • 68
    • 69449102231 scopus 로고    scopus 로고
    • On the use of Ripley's K-function and its derivatives to analyze domain size
    • Kiskowski M.A., Hancock J.F., Kenworthy A.K. On the use of Ripley's K-function and its derivatives to analyze domain size. Biophys. J. 2009, 97:1095-1103.
    • (2009) Biophys. J. , vol.97 , pp. 1095-1103
    • Kiskowski, M.A.1    Hancock, J.F.2    Kenworthy, A.K.3
  • 70
    • 84857580744 scopus 로고    scopus 로고
    • Correlation functions quantify super-resolution images and estimate apparent clustering due to over-counting
    • Veatch S.L., Machta B.B., Shelby S.A., Chiang E.N., Holowka D.A., Baird B.A. Correlation functions quantify super-resolution images and estimate apparent clustering due to over-counting. PLoS ONE 2012, 7:e31457.
    • (2012) PLoS ONE , vol.7 , pp. e31457
    • Veatch, S.L.1    Machta, B.B.2    Shelby, S.A.3    Chiang, E.N.4    Holowka, D.A.5    Baird, B.A.6
  • 71
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior I.A., Muncke C., Parton R.G., Hancock J.F. Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J. Cell Biol. 2003, 160:165-170.
    • (2003) J. Cell Biol. , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 72
    • 84923138765 scopus 로고    scopus 로고
    • Pre-embedding immunogold labeling to optimize protein localization at subcellular compartments and membrane microdomains of leukocytes
    • Melo R.C., Morgan E., Monahan-Earley R., Dvorak A.M., Weller P.F. Pre-embedding immunogold labeling to optimize protein localization at subcellular compartments and membrane microdomains of leukocytes. Nat. Protoc. 2014, 9:2382-2394.
    • (2014) Nat. Protoc. , vol.9 , pp. 2382-2394
    • Melo, R.C.1    Morgan, E.2    Monahan-Earley, R.3    Dvorak, A.M.4    Weller, P.F.5
  • 75
    • 84922515976 scopus 로고    scopus 로고
    • The "in situ" proximity ligation assay to probe protein-protein interactions in intact tissues
    • Bellucci A., Fiorentini C., Zaltieri M., Missale C., Spano P. The "in situ" proximity ligation assay to probe protein-protein interactions in intact tissues. Methods Mol. Biol. 2014, 1174:397-405.
    • (2014) Methods Mol. Biol. , vol.1174 , pp. 397-405
    • Bellucci, A.1    Fiorentini, C.2    Zaltieri, M.3    Missale, C.4    Spano, P.5
  • 76
    • 84903513722 scopus 로고    scopus 로고
    • In situ proximity ligation assay for detection of proteins, their interactions and modifications
    • Brychtova V., Vojtesek B. In situ proximity ligation assay for detection of proteins, their interactions and modifications. Klin. Onkol. 2014, 27(Suppl.):87-91.
    • (2014) Klin. Onkol. , vol.27 , pp. 87-91
    • Brychtova, V.1    Vojtesek, B.2
  • 77
    • 60049093598 scopus 로고    scopus 로고
    • BlobFinder, a tool for fluorescence microscopy image cytometry
    • Allalou A., Wahlby C. BlobFinder, a tool for fluorescence microscopy image cytometry. Comput. Methods Programs Biomed. 2009, 94:58-65.
    • (2009) Comput. Methods Programs Biomed. , vol.94 , pp. 58-65
    • Allalou, A.1    Wahlby, C.2
  • 78
    • 84890206912 scopus 로고    scopus 로고
    • Proximity ligation assay for high-content profiling of cell signaling pathways on a microfluidic chip
    • Blazek M., Betz C., Hall M.N., Reth M., Zengerle R., Meier M. Proximity ligation assay for high-content profiling of cell signaling pathways on a microfluidic chip. Mol. Cell. Proteomics 2013, 12:3898-3907.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 3898-3907
    • Blazek, M.1    Betz, C.2    Hall, M.N.3    Reth, M.4    Zengerle, R.5    Meier, M.6
  • 79
    • 77951045295 scopus 로고    scopus 로고
    • Arginine methylation of the B cell antigen receptor promotes differentiation
    • Infantino S., Benz B., Waldmann T., Jung M., Schneider R., Reth M. Arginine methylation of the B cell antigen receptor promotes differentiation. J. Exp. Med. 2010, 207:711-719.
    • (2010) J. Exp. Med. , vol.207 , pp. 711-719
    • Infantino, S.1    Benz, B.2    Waldmann, T.3    Jung, M.4    Schneider, R.5    Reth, M.6
  • 81
    • 0742305006 scopus 로고    scopus 로고
    • Imaging immune cell interactions and functions: SMACs and the Immunological Synapse
    • Kupfer A., Kupfer H. Imaging immune cell interactions and functions: SMACs and the Immunological Synapse. Semin. Immunol. 2003, 15:295-300.
    • (2003) Semin. Immunol. , vol.15 , pp. 295-300
    • Kupfer, A.1    Kupfer, H.2
  • 82
    • 77956393723 scopus 로고    scopus 로고
    • An outlook on organization of lipids in membranes: searching for a realistic connection with the organization of biological membranes
    • Bagatolli L.A., Ipsen J.H., Simonsen A.C., Mouritsen O.G. An outlook on organization of lipids in membranes: searching for a realistic connection with the organization of biological membranes. Prog. Lipid Res. 2010, 49:378-389.
    • (2010) Prog. Lipid Res. , vol.49 , pp. 378-389
    • Bagatolli, L.A.1    Ipsen, J.H.2    Simonsen, A.C.3    Mouritsen, O.G.4
  • 83
    • 77449114018 scopus 로고    scopus 로고
    • A nanometer scale optical view on the compartmentalization of cell membranes
    • van Zanten T.S., Cambi A., Garcia-Parajo M.F. A nanometer scale optical view on the compartmentalization of cell membranes. Biochim. Biophys. Acta 2010, 1798:777-787.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 777-787
    • van Zanten, T.S.1    Cambi, A.2    Garcia-Parajo, M.F.3
  • 85
    • 0030863490 scopus 로고    scopus 로고
    • Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane
    • Sheets E.D., Lee G.M., Simson R., Jacobson K. Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane. Biochemistry 1997, 36:12449-12458.
    • (1997) Biochemistry , vol.36 , pp. 12449-12458
    • Sheets, E.D.1    Lee, G.M.2    Simson, R.3    Jacobson, K.4
  • 86
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature 1997, 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 87
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R., Mayor S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 1998, 394:798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 88
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • Sharma P., Varma R., Sarasij R.C., Ira K.Gousset, Krishnamoorthy G., Rao M., Mayor S. Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell 2004, 116:577-589.
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    Ira, K.G.4    Krishnamoorthy, G.5    Rao, M.6    Mayor, S.7
  • 89
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown D.A., Rose J.K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 1992, 68:533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 90
    • 22744437388 scopus 로고    scopus 로고
    • Detergent-resistant membranes should not be identified with membrane rafts
    • Lichtenberg D., Goni F.M., Heerklotz H. Detergent-resistant membranes should not be identified with membrane rafts. Trends Biochem. Sci. 2005, 30:430-436.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 430-436
    • Lichtenberg, D.1    Goni, F.M.2    Heerklotz, H.3
  • 92
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons K., van Meer G. Lipid sorting in epithelial cells. Biochemistry 1988, 27:6197-6202.
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    van Meer, G.2
  • 93
    • 34250368055 scopus 로고    scopus 로고
    • Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling
    • Fujita A., Cheng J., Hirakawa M., Furukawa K., Kusunoki S., Fujimoto T. Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling. Mol. Biol. Cell 2007, 18:2112-2122.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2112-2122
    • Fujita, A.1    Cheng, J.2    Hirakawa, M.3    Furukawa, K.4    Kusunoki, S.5    Fujimoto, T.6
  • 94
    • 0034914677 scopus 로고    scopus 로고
    • Oligomeric antigen receptors: a new view on signaling for the selection of lymphocytes
    • Reth M. Oligomeric antigen receptors: a new view on signaling for the selection of lymphocytes. Trends Immunol. 2001, 22:356-360.
    • (2001) Trends Immunol. , vol.22 , pp. 356-360
    • Reth, M.1
  • 95
    • 77957125242 scopus 로고    scopus 로고
    • Oligomeric organization of the B-cell antigen receptor on resting cells
    • Yang J., Reth M. Oligomeric organization of the B-cell antigen receptor on resting cells. Nature 2010, 467:465-469.
    • (2010) Nature , vol.467 , pp. 465-469
    • Yang, J.1    Reth, M.2
  • 96
    • 77952584138 scopus 로고    scopus 로고
    • Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals
    • Hite R.K., Li Z., Walz T. Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals. EMBO J. 2010, 29:1652-1658.
    • (2010) EMBO J. , vol.29 , pp. 1652-1658
    • Hite, R.K.1    Li, Z.2    Walz, T.3
  • 98
    • 0026750092 scopus 로고
    • Antigen receptors on B lymphocytes
    • Reth M. Antigen receptors on B lymphocytes. Annu. Rev. Immunol. 1992, 10:97-121.
    • (1992) Annu. Rev. Immunol. , vol.10 , pp. 97-121
    • Reth, M.1
  • 99
    • 0037184955 scopus 로고    scopus 로고
    • The organizing principle in the formation of the T cell receptor-CD3 complex
    • Call M.E., Pyrdol J., Wiedmann M., Wucherpfennig K.W. The organizing principle in the formation of the T cell receptor-CD3 complex. Cell 2002, 111:967-979.
    • (2002) Cell , vol.111 , pp. 967-979
    • Call, M.E.1    Pyrdol, J.2    Wiedmann, M.3    Wucherpfennig, K.W.4
  • 100
    • 1842505447 scopus 로고    scopus 로고
    • Molecular mechanisms for the assembly of the T cell receptor-CD3 complex
    • Call M.E., Wucherpfennig K.W. Molecular mechanisms for the assembly of the T cell receptor-CD3 complex. Mol. Immunol. 2004, 40:1295-1305.
    • (2004) Mol. Immunol. , vol.40 , pp. 1295-1305
    • Call, M.E.1    Wucherpfennig, K.W.2
  • 101
    • 77954299061 scopus 로고    scopus 로고
    • A comprehensive comparison of transmembrane domains reveals organelle-specific properties
    • Sharpe H.J., Stevens T.J., Munro S. A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell 2010, 142:158-169.
    • (2010) Cell , vol.142 , pp. 158-169
    • Sharpe, H.J.1    Stevens, T.J.2    Munro, S.3
  • 103
    • 33846041775 scopus 로고    scopus 로고
    • Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts
    • Kai M., Sakane F., Jia Y.J., Imai S., Yasuda S., Kanoh H. Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts. J. Biochem. 2006, 140:677-686.
    • (2006) J. Biochem. , vol.140 , pp. 677-686
    • Kai, M.1    Sakane, F.2    Jia, Y.J.3    Imai, S.4    Yasuda, S.5    Kanoh, H.6
  • 105
    • 64749090227 scopus 로고    scopus 로고
    • Segregation of GM1 and GM3 clusters in the cell membrane depends on the intact actin cytoskeleton
    • Fujita A., Cheng J., Fujimoto T. Segregation of GM1 and GM3 clusters in the cell membrane depends on the intact actin cytoskeleton. Biochim. Biophys. Acta 2009, 1791:388-396.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 388-396
    • Fujita, A.1    Cheng, J.2    Fujimoto, T.3
  • 106
    • 84861991991 scopus 로고    scopus 로고
    • Active remodeling of cortical actin regulates spatiotemporal organization of cell surface molecules
    • Gowrishankar K., Ghosh S., Saha R.C., Mayor S., Rao M. Active remodeling of cortical actin regulates spatiotemporal organization of cell surface molecules. Cell 2012, 149:1353-1367.
    • (2012) Cell , vol.149 , pp. 1353-1367
    • Gowrishankar, K.1    Ghosh, S.2    Saha, R.C.3    Mayor, S.4    Rao, M.5
  • 107
    • 18244397166 scopus 로고    scopus 로고
    • Actin depolymerization transduces the strength of B-cell receptor stimulation
    • Hao S., August A. Actin depolymerization transduces the strength of B-cell receptor stimulation. Mol. Biol. Cell 2005, 16:2275-2284.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2275-2284
    • Hao, S.1    August, A.2
  • 110
    • 33748185659 scopus 로고    scopus 로고
    • Cytoskeleton regulation of glycine receptor number at synapses and diffusion in the plasma membrane
    • Charrier C., Ehrensperger M.V., Dahan M., Levi S., Triller A. Cytoskeleton regulation of glycine receptor number at synapses and diffusion in the plasma membrane. J. Neurosci. 2006, 26:8502-8511.
    • (2006) J. Neurosci. , vol.26 , pp. 8502-8511
    • Charrier, C.1    Ehrensperger, M.V.2    Dahan, M.3    Levi, S.4    Triller, A.5
  • 111
    • 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
    • Kusumi A., Nakada C., Ritchie K., Murase K., Suzuki K., Murakoshi H., Kasai R.S., Kondo J., Fujiwara T. 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. 2005, 34:351-378.
    • (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
  • 112
    • 0037054546 scopus 로고    scopus 로고
    • Phospholipids undergo hop diffusion in compartmentalized cell membrane
    • Fujiwara T., Ritchie K., Murakoshi H., Jacobson K., Kusumi A. Phospholipids undergo hop diffusion in compartmentalized cell membrane. J. Cell Biol. 2002, 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
  • 113
    • 79956106702 scopus 로고    scopus 로고
    • Dynamic cortical actin remodeling by ERM proteins controls BCR microcluster organization and integrity
    • Treanor B., Depoil D., Bruckbauer A., Batista F.D. Dynamic cortical actin remodeling by ERM proteins controls BCR microcluster organization and integrity. J. Exp. Med. 2011, 208:1055-1068.
    • (2011) J. Exp. Med. , vol.208 , pp. 1055-1068
    • Treanor, B.1    Depoil, D.2    Bruckbauer, A.3    Batista, F.D.4
  • 115
    • 59349120088 scopus 로고    scopus 로고
    • Different GPI-attachment signals affect the oligomerisation of GPI-anchored proteins and their apical sorting
    • Paladino S., Lebreton S., Tivodar S., Campana V., Tempre R., Zurzolo C. Different GPI-attachment signals affect the oligomerisation of GPI-anchored proteins and their apical sorting. J. Cell Sci. 2008, 121:4001-4007.
    • (2008) J. Cell Sci. , vol.121 , pp. 4001-4007
    • Paladino, S.1    Lebreton, S.2    Tivodar, S.3    Campana, V.4    Tempre, R.5    Zurzolo, C.6
  • 119
    • 84886820997 scopus 로고    scopus 로고
    • Regulated vesicle fusion generates signaling nanoterritories that control T cell activation at the immunological synapse
    • Soares H., Henriques R., Sachse M., Ventimiglia L., Alonso M.A., Zimmer C., Thoulouze M.I., Alcover A. Regulated vesicle fusion generates signaling nanoterritories that control T cell activation at the immunological synapse. J. Exp. Med. 2013, 210:2415-2433.
    • (2013) J. Exp. Med. , vol.210 , pp. 2415-2433
    • Soares, H.1    Henriques, R.2    Sachse, M.3    Ventimiglia, L.4    Alonso, M.A.5    Zimmer, C.6    Thoulouze, M.I.7    Alcover, A.8
  • 120
    • 0024980981 scopus 로고
    • Antigen receptor tail clue
    • Reth M. Antigen receptor tail clue. Nature 1989, 338:383-384.
    • (1989) Nature , vol.338 , pp. 383-384
    • Reth, M.1
  • 121
    • 0032055963 scopus 로고    scopus 로고
    • Asymmetrical phosphorylation and function of immunoreceptor tyrosine-based activation motif tyrosines in B cell antigen receptor signal transduction
    • Pao L.I., Famiglietti S.J., Cambier J.C. Asymmetrical phosphorylation and function of immunoreceptor tyrosine-based activation motif tyrosines in B cell antigen receptor signal transduction. J. Immunol. 1998, 160:3305-3314.
    • (1998) J. Immunol. , vol.160 , pp. 3305-3314
    • Pao, L.I.1    Famiglietti, S.J.2    Cambier, J.C.3
  • 122
    • 0030564833 scopus 로고    scopus 로고
    • Catalytic specificity of phosphotyrosine kinases Blk Lyn, c-Src and Syk as assessed by phage display
    • Schmitz R., Baumann G., Gram H. Catalytic specificity of phosphotyrosine kinases Blk Lyn, c-Src and Syk as assessed by phage display. J. Mol. Biol. 1996, 260:664-677.
    • (1996) J. Mol. Biol. , vol.260 , pp. 664-677
    • Schmitz, R.1    Baumann, G.2    Gram, H.3
  • 123
    • 0032555744 scopus 로고    scopus 로고
    • Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide
    • Futterer K., Wong J., Grucza R.A., Chan A.C., Waksman G. Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide. J. Mol. Biol. 1998, 281:523-537.
    • (1998) J. Mol. Biol. , vol.281 , pp. 523-537
    • Futterer, K.1    Wong, J.2    Grucza, R.A.3    Chan, A.C.4    Waksman, G.5
  • 124
    • 27544446258 scopus 로고    scopus 로고
    • The initiation of antigen-induced B cell antigen receptor signaling viewed in living cells by fluorescence resonance energy transfer
    • Tolar P., Sohn H.W., Pierce S.K. The initiation of antigen-induced B cell antigen receptor signaling viewed in living cells by fluorescence resonance energy transfer. Nat. Immunol. 2005, 6:1168-1176.
    • (2005) Nat. Immunol. , vol.6 , pp. 1168-1176
    • Tolar, P.1    Sohn, H.W.2    Pierce, S.K.3
  • 125
    • 33745785300 scopus 로고    scopus 로고
    • Visualization of molecular interactions by fluorescence complementation
    • Kerppola T.K. Visualization of molecular interactions by fluorescence complementation. Nat. Rev. Mol. Cell Biol. 2006, 7:449-456.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 449-456
    • Kerppola, T.K.1
  • 126
  • 127
    • 33749009002 scopus 로고    scopus 로고
    • Identification of disulfide bonds in the Ig-alpha/Ig-beta component of the B cell antigen receptor using the Drosophila S2 cell reconstitution system
    • Siegers G.M., Yang J., Duerr C.U., Nielsen P.J., Reth M., Schamel W.W. Identification of disulfide bonds in the Ig-alpha/Ig-beta component of the B cell antigen receptor using the Drosophila S2 cell reconstitution system. Int. Immunol. 2006, 18:1385-1396.
    • (2006) Int. Immunol. , vol.18 , pp. 1385-1396
    • Siegers, G.M.1    Yang, J.2    Duerr, C.U.3    Nielsen, P.J.4    Reth, M.5    Schamel, W.W.6
  • 128
    • 78649863361 scopus 로고    scopus 로고
    • The dissociation activation model of B cell antigen receptor triggering
    • Yang J., Reth M. The dissociation activation model of B cell antigen receptor triggering. FEBS Lett. 2010, 584:4872-4877.
    • (2010) FEBS Lett. , vol.584 , pp. 4872-4877
    • Yang, J.1    Reth, M.2


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