메뉴 건너뛰기




Volumn 8, Issue 4, 1996, Pages 566-574

Cell surface organization by the membrane skeleton

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 0030222116     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80036-6     Document Type: Article
Times cited : (331)

References (76)
  • 2
    • 0026675654 scopus 로고
    • Transmembrane signaling: The joy of aggregation
    • 2. Metzger H: Transmembrane signaling: the joy of aggregation. J Immunol 1992, 149:1477-1487.
    • (1992) J Immunol , vol.149 , pp. 1477-1487
    • Metzger, H.1
  • 3
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation
    • 3. Gadella TWJ, Jovin TM: Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation. J Cell Biol 1995, 129:1543-1558. The aggregation states of the epidermal growth factor receptor on A431 cells were assessed using a fluorescence resonance energy transfer technique. The results suggest that the receptors of the high-affinity, functional subclass on quiescent A431 cells are present in a predimerized or oligomerized state.
    • (1995) J Cell Biol , vol.129 , pp. 1543-1558
    • Gadella, T.W.J.1    Jovin, T.M.2
  • 4
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • 4. Heldin C-H: Dimerization of cell surface receptors in signal transduction. Cell 1995, 80:213-223. An extensive review of ligand-induced receptor activation through dimerization and oligomerization of the receptor molecules. Emphasis is placed on growth factor receptors.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.-H.1
  • 5
    • 0028839834 scopus 로고
    • The body language of cells: The intimate connection between cell adhesion and behavior
    • 5. Klymkowski MW, Parr B: The body language of cells: the intimate connection between cell adhesion and behavior. Cell 1995, 83:5-8. A succinct and good review of how cell-cell contact leads to formation of the adherens junction. It covers both structural and informational aspects of the assembly of adherens junctions.
    • (1995) Cell , vol.83 , pp. 5-8
    • Klymkowski, M.W.1    Parr, B.2
  • 6
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • 6. Miyamoto S, Akiyama SK, Yamada KM: Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science 1995, 267:883-885. The effects of binding of large (12 mm-φ) latex beads, coated with either various antibodies or ligands for integrin, to the human foreskin fibroblast cell surface were studied to examine the roles of ligand occupancy and aggregation of integrins. Tensin and focal adhesion kinase were accumulated at the beads that caused integrin aggregation, and tyrosine phosphorylation of proteins was induced. Receptor occupancy by the ligands was not needed for these processes. However, accumulation of F-actin, vinculin, talin, α-actinin, paxillin and filamin required both aggregation and occupancy of integrins (ligand-coated beads, or non-inhibitory antibodies on beads plus soluble ligands, produced these effects).
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 8
    • 0026446341 scopus 로고
    • Regulation of surface polarity from bacteria to mammals
    • 8. Nelson WJ: Regulation of surface polarity from bacteria to mammals. Science 1992, 258:948-955.
    • (1992) Science , vol.258 , pp. 948-955
    • Nelson, W.J.1
  • 9
    • 0026603896 scopus 로고
    • Optical tweezers in cell biology
    • 9. Kuo S, Sheetz MP: Optical tweezers in cell biology. Trends Cell Biol 1992, 2:116-118.
    • (1992) Trends Cell Biol , vol.2 , pp. 116-118
    • Kuo, S.1    Sheetz, M.P.2
  • 11
    • 0029126377 scopus 로고
    • New insights into membrane dynamics from the analysis of cell surface interactions by physical methods
    • 11. Sheets ED, Simson R, Jacobson K: New insights into membrane dynamics from the analysis of cell surface interactions by physical methods. Curr Opin Cell Biol 1995, 7:707-714. Excellent review on the translational diffusion of proteins and on molecular interactions in the plasma membrane, as analyzed by microscopy-based physical methods. Includes an interesting discussion of the structural origins of various modes of protein motion.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 707-714
    • Sheets, E.D.1    Simson, R.2    Jacobson, K.3
  • 12
    • 0024990463 scopus 로고
    • Spectrin-based membrane skeleton: A multipotential adaptor between plasma membrane and cytoplasm
    • 12. Bennett V: Spectrin-based membrane skeleton: a multipotential adaptor between plasma membrane and cytoplasm. Physiol Rev 1990, 70:1029-1065.
    • (1990) Physiol Rev , vol.70 , pp. 1029-1065
    • Bennett, V.1
  • 13
    • 0027333413 scopus 로고
    • The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane
    • 13. Bennett V, Gilligan DM: The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu Rev Cell Biol 1993, 9:27-66.
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 27-66
    • Bennett, V.1    Gilligan, D.M.2
  • 14
    • 0026497661 scopus 로고
    • Cytoskeleton-plasma membrane interactions
    • 14 Luna EJ, Hitt AL: Cytoskeleton-plasma membrane interactions. Science 1992, 258:955-964.
    • (1992) Science , vol.258 , pp. 955-964
    • Luna, E.J.1    Hitt, A.L.2
  • 15
    • 0026539874 scopus 로고
    • Patches, posts and fences: Proteins and plasma membrane domains
    • 15 Edidin M: Patches, posts and fences: proteins and plasma membrane domains. Trends Cell Biol 1992, 2:376-380.
    • (1992) Trends Cell Biol , vol.2 , pp. 376-380
    • Edidin, M.1
  • 16
    • 0027748723 scopus 로고
    • Patches and fences: Probing for plasma membrane domains
    • 16. Edidin M: Patches and fences: probing for plasma membrane domains. J Cell Sci 1993, 17(suppl):165-169.
    • (1993) J Cell Sci , vol.17 , Issue.SUPPL. , pp. 165-169
    • Edidin, M.1
  • 17
    • 0028036369 scopus 로고
    • Membrane interactions with the actin cytoskeleton
    • 17. Hitt AL, Luna EJ: Membrane interactions with the actin cytoskeleton. Curr Opin Cell Biol 1994, 6:120-130.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 120-130
    • Hitt, A.L.1    Luna, E.J.2
  • 18
    • 0029005840 scopus 로고
    • Revisiting the fluid mosaic model of membranes
    • 18. Jacobson K, Sheets ED, Simson R: Revisiting the fluid mosaic model of membranes. Science 1995, 268:1441-1442. An excellent and succinct review of our present understanding of protein dynamics in the plasma membrane.
    • (1995) Science , vol.268 , pp. 1441-1442
    • Jacobson, K.1    Sheets, E.D.2    Simson, R.3
  • 19
    • 0027217936 scopus 로고
    • Quantitaten of membrane receptor distributions by image correlation spectroscopy: Concept and applications
    • 19. Petersen NO, Höddelius PL, Wiseman PW, Seger O, Magnusson K-E: Quantitaten of membrane receptor distributions by image correlation spectroscopy: concept and applications. Biophys J 1993, 65:1135-1146.
    • (1993) Biophys J , vol.65 , pp. 1135-1146
    • Petersen, N.O.1    Höddelius, P.L.2    Wiseman, P.W.3    Seger, O.4    Magnusson, K.-E.5
  • 20
    • 0029147426 scopus 로고
    • Digging into caveolae
    • 20. Parton RG, Simons K: Digging into caveolae. Science 1995, 269:1398-1399. A brief review on the structure, and mechanism of formation, of caveolae. Presents a very interesting discussion of detergent-insoluble glycosphingolipid-enriched (DIG) domains and caveolae. This review clearly indicates that future studies should benefit greatly from a concerted effort of the protein and lipid research camps, which have been working separately.
    • (1995) Science , vol.269 , pp. 1398-1399
    • Parton, R.G.1    Simons, K.2
  • 21
    • 0023871621 scopus 로고
    • Tracking kinesin-driven movements with nanometre-scale precision
    • 21. Gelles J, Schnapp BJ, Sheetz MP: Tracking kinesin-driven movements with nanometre-scale precision. Nature 1988, 331:450-453.
    • (1988) Nature , vol.331 , pp. 450-453
    • Gelles, J.1    Schnapp, B.J.2    Sheetz, M.P.3
  • 23
    • 0026528045 scopus 로고
    • Tracking of cell surface receptors by fluorescence digital imaging microscopy using a charge-coupled device camera. Low-density lipoprotein and influenza virus receptor mobility at 4°C
    • 23. Anderson CM, Georgiou GN, Morrison IEG, Stevenson GVW, Cherry RJ: Tracking of cell surface receptors by fluorescence digital imaging microscopy using a charge-coupled device camera. Low-density lipoprotein and influenza virus receptor mobility at 4°C. J Cell Sci 1992, 101:415-425.
    • (1992) J Cell Sci , vol.101 , pp. 415-425
    • Anderson, C.M.1    Georgiou, G.N.2    Morrison, I.E.G.3    Stevenson, G.V.W.4    Cherry, R.J.5
  • 24
    • 0026683137 scopus 로고
    • Keeping track of cell surface receptors
    • 24. Cherry RJ: Keeping track of cell surface receptors. Trends Cell Biol 1992, 2:242-244.
    • (1992) Trends Cell Biol , vol.2 , pp. 242-244
    • Cherry, R.J.1
  • 25
    • 0028281482 scopus 로고
    • Automated detection and tracking of individual and clustered cell surface low density lipoprotein receptor molecules
    • 25. Ghosh RN, Webb WW: Automated detection and tracking of individual and clustered cell surface low density lipoprotein receptor molecules. Biophys J 1994, 66:1301-1318.
    • (1994) Biophys J , vol.66 , pp. 1301-1318
    • Ghosh, R.N.1    Webb, W.W.2
  • 26
    • 0027970208 scopus 로고
    • Single particle tracking of surface receptor movement during cell division
    • 26. Wang Y-L, Silverman JD, Cao L-G: Single particle tracking of surface receptor movement during cell division. J Cell Biol 1994, 127:963-971.
    • (1994) J Cell Biol , vol.127 , pp. 963-971
    • Wang, Y.-L.1    Silverman, J.D.2    Cao, L.-G.3
  • 27
    • 0025997180 scopus 로고
    • Single particle tracking (analysis of diffusion and flow in two-dimensional systems)
    • 27. Qian H, Sheetz MP, Elson E: Single particle tracking (analysis of diffusion and flow in two-dimensional systems). Biophys J 1991, 60:910-921.
    • (1991) Biophys J , vol.60 , pp. 910-921
    • Qian, H.1    Sheetz, M.P.2    Elson, E.3
  • 28
    • 0027197103 scopus 로고
    • Lateral diffusion in an archipelago. Single-particle diffusion
    • 28. Saxton MJ: Lateral diffusion in an archipelago. Single-particle diffusion. Biophys J 1993, 64:1766-1780.
    • (1993) Biophys J , vol.64 , pp. 1766-1780
    • Saxton, M.J.1
  • 29
    • 0028140412 scopus 로고
    • Anomalous diffusion due to obstacles: A Monte Carlo study
    • 29. Saxton MJ: Anomalous diffusion due to obstacles: a Monte Carlo study. Biophys J 1994, 66:683-688.
    • (1994) Biophys J , vol.66 , pp. 683-688
    • Saxton, M.J.1
  • 30
    • 0029163176 scopus 로고
    • Single-particle tracking: Effects of corrals
    • 30. Saxton MJ: Single-particle tracking: effects of corrals. Biophys J 1995, 69:389-398. Monte Carlo simulation of lateral diffusion of membrane proteins in corrals was carried out to develop a method to interpret the trajectories obtained by single-particle tracking. Escape times for a diffusing particle in a corral were obtained, and the possibility of the identification of corrals in tracking experiments was carefully examined.
    • (1995) Biophys J , vol.69 , pp. 389-398
    • Saxton, M.J.1
  • 31
    • 4244183420 scopus 로고    scopus 로고
    • Single-particle tracking: New methods of data analysis
    • 31. Saxton MJ: Single-particle tracking: new methods of data analysis. Biophys J 1996, 70:A334.
    • (1996) Biophys J , vol.70
    • Saxton, M.J.1
  • 32
    • 0027504198 scopus 로고
    • Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells
    • 32. Kusumi A, Sako Y, Yamamoto M: Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells. Biophys J 1993 65:2021-2040.
    • (1993) Biophys J , vol.65 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 34
    • 0024338987 scopus 로고
    • Nanometre-level analysis demonstrates that lipid flow does not drive membrane glycoprotein movements
    • 34. Sheetz MP, Turney S, Qian H, Elson EL: Nanometre-level analysis demonstrates that lipid flow does not drive membrane glycoprotein movements. Nature 1989, 340:284-288.
    • (1989) Nature , vol.340 , pp. 284-288
    • Sheetz, M.P.1    Turney, S.2    Qian, H.3    Elson, E.L.4
  • 35
    • 0029162080 scopus 로고
    • Detection of temporary lateral confinement of membrane proteins using single particle tracking analysis
    • 35. Simson R, Sheets ED, Jacobson K: Detection of temporary lateral confinement of membrane proteins using single particle tracking analysis. Biophys J 1995, 69:989-993. When studying single-particle trajectories, it would be very useful if the portion of trajectory in which the particle is undergoing confined diffusion could be distinguished. The presence of such a portion indicates temporary confinement of the protein. The authors of this paper developed a protocol to distinguish such a portion. Analysis of the movements of Thy-1 and NCAM125 by this method revealed that ∼30% of the trajectories for both proteins exhibited periods of transient confinement that lasted for 8 seconds on average, in regions that were about 280 nm in diameter.
    • (1995) Biophys J , vol.69 , pp. 989-993
    • Simson, R.1    Sheets, E.D.2    Jacobson, K.3
  • 36
    • 0022966969 scopus 로고
    • Restriction of the lateral motion of band 3 in the erythrocyte membrane by the cytoskeletal network: Dependence on spectrin association state
    • 36. Tsuji A, Ohnishi S: Restriction of the lateral motion of band 3 in the erythrocyte membrane by the cytoskeletal network: dependence on spectrin association state. Biochemistry 1986, 25:6133-6139.
    • (1986) Biochemistry , vol.25 , pp. 6133-6139
    • Tsuji, A.1    Ohnishi, S.2
  • 37
    • 0023688017 scopus 로고
    • Regulation of band 3 mobilities in erythrocyte ghost membranes by protein association and cytoskeletal meshwork
    • 37. Tsuji A, Kawasaki K, Ohnishi S, Merkle H, Kusumi A: Regulation of band 3 mobilities in erythrocyte ghost membranes by protein association and cytoskeletal meshwork. Biochemistry 1988, 27:7447-7452.
    • (1988) Biochemistry , vol.27 , pp. 7447-7452
    • Tsuji, A.1    Kawasaki, K.2    Ohnishi, S.3    Merkle, H.4    Kusumi, A.5
  • 38
    • 0028141959 scopus 로고
    • Differential control of band 3 lateral and rotational mobility in intact red cells
    • 38. Corbett JD, Agre P, Palek J, Golan DE: Differential control of band 3 lateral and rotational mobility in intact red cells. J Clin Invest 1994, 94:683-688.
    • (1994) J Clin Invest , vol.94 , pp. 683-688
    • Corbett, J.D.1    Agre, P.2    Palek, J.3    Golan, D.E.4
  • 39
    • 0028243194 scopus 로고
    • Compartmentalized structure of the plasma membrane for lateral diffusion of receptors as revealed by nanometer-level motion analysis
    • 39. Sako Y, Kusumi A: Compartmentalized structure of the plasma membrane for lateral diffusion of receptors as revealed by nanometer-level motion analysis. J Cell Biol 1994, 125:1251-1264.
    • (1994) J Cell Biol , vol.125 , pp. 1251-1264
    • Sako, Y.1    Kusumi, A.2
  • 40
    • 0026053736 scopus 로고
    • Lateral diffusion and retrograde movements of individual cell surface components on single motile cells observed with nanovid microscopy
    • 40. De Brabander M, Nuydens R, Ishihara A, Holifield B, Jacobson K, Geerts H: Lateral diffusion and retrograde movements of individual cell surface components on single motile cells observed with nanovid microscopy. J Cell Biol 1991, 112:111-124.
    • (1991) J Cell Biol , vol.112 , pp. 111-124
    • De Brabander, M.1    Nuydens, R.2    Ishihara, A.3    Holifield, B.4    Jacobson, K.5    Geerts, H.6
  • 41
    • 0023606954 scopus 로고
    • Micrometer-scale domains in fibroblast plasma membranes
    • 41. Yechiel E, Edidin M: Micrometer-scale domains in fibroblast plasma membranes. J Cell Biol 1987, 105:755-760.
    • (1987) J Cell Biol , vol.105 , pp. 755-760
    • Yechiel, E.1    Edidin, M.2
  • 42
    • 0026071833 scopus 로고
    • Differences between the lateral organization of conventional and inositol phospholipid-anchored membrane proteins. A further definition of micrometer scale domains
    • 42. Edidin M, Stroynowski I: Differences between the lateral organization of conventional and inositol phospholipid-anchored membrane proteins. A further definition of micrometer scale domains. J Cell Biol 1991, 112:1143-1150.
    • (1991) J Cell Biol , vol.112 , pp. 1143-1150
    • Edidin, M.1    Stroynowski, I.2
  • 43
    • 0022655537 scopus 로고
    • Observation of a single-beam gradient force optical trap for dielectric particles
    • 43. Ashkin A, Dziedzic JM, Bjorkholm JE, Chu S: Observation of a single-beam gradient force optical trap for dielectric particles. Opt Letters 1986, 11:288-290.
    • (1986) Opt Letters , vol.11 , pp. 288-290
    • Ashkin, A.1    Dziedzic, J.M.2    Bjorkholm, J.E.3    Chu, S.4
  • 44
    • 0025251665 scopus 로고
    • Force generation of organelle transport measured in vivo by an infrared laser trap
    • 44. Ashkin A., Schütze K, Dziedzic JM, Euteneuer U, Schliwa M: Force generation of organelle transport measured in vivo by an infrared laser trap. Nature 1990, 348:346-347.
    • (1990) Nature , vol.348 , pp. 346-347
    • Ashkin, A.1    Schütze, K.2    Dziedzic, J.M.3    Euteneuer, U.4    Schliwa, M.5
  • 45
    • 0025745355 scopus 로고
    • Preferential attachment of membrane glycoproteins to the cytoskeleton at the leading edge of lamella
    • 45. Kucik DF, Kuo SC, Elson EL, Sheetz MP: Preferential attachment of membrane glycoproteins to the cytoskeleton at the leading edge of lamella. J Cell Biol 1991, 114:1029-1036.
    • (1991) J Cell Biol , vol.114 , pp. 1029-1036
    • Kucik, D.F.1    Kuo, S.C.2    Elson, E.L.3    Sheetz, M.P.4
  • 46
    • 0027423956 scopus 로고
    • Integrin cytoskeletal interactions in migrating fibroblasts are dynamic, asymmetric, and regulated
    • 46. Schmidt CE, Horwitz AF, Lauffenburer DA, Sheetz MP: Integrin cytoskeletal interactions in migrating fibroblasts are dynamic, asymmetric, and regulated. J Cell Biol 1993, 123:977-991.
    • (1993) J Cell Biol , vol.123 , pp. 977-991
    • Schmidt, C.E.1    Horwitz, A.F.2    Lauffenburer, D.A.3    Sheetz, M.P.4
  • 47
    • 0023663919 scopus 로고
    • Optical trapping and manipulation of single cells using infrared-laser beams
    • 47. Ashkin A, Dziedzic JM, Yamane T: Optical trapping and manipulation of single cells using infrared-laser beams. Nature 1987, 330:769-771.
    • (1987) Nature , vol.330 , pp. 769-771
    • Ashkin, A.1    Dziedzic, J.M.2    Yamane, T.3
  • 48
    • 0026320864 scopus 로고
    • Lateral movements of membrane glycoproteins restricted by dynamic cytoplasmic barriers
    • 48. Edidin M, Kuo SC, Sheetz MP: Lateral movements of membrane glycoproteins restricted by dynamic cytoplasmic barriers. Science 1991, 254:1379-1382.
    • (1991) Science , vol.254 , pp. 1379-1382
    • Edidin, M.1    Kuo, S.C.2    Sheetz, M.P.3
  • 49
    • 0028325756 scopus 로고
    • Truncation mutants define and locate cytoplasmic barriers to lateral mobility of membrane glycoproteins
    • 49. Edidin M, Zún̄iga MC, Sheetz MP: Truncation mutants define and locate cytoplasmic barriers to lateral mobility of membrane glycoproteins. Proc Natl Acad Sci USA 1994, 91:3378-3382.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3378-3382
    • Edidin, M.1    Zúniga, M.C.2    Sheetz, M.P.3
  • 50
    • 0029014265 scopus 로고
    • Barriers for lateral diffusion of transferrin receptor in the plasma nembrane as characterized by receptor dragging by laser tweezers: Fence versus tether
    • 50. Sako Y, Kusumi A: Barriers for lateral diffusion of transferrin receptor in the plasma nembrane as characterized by receptor dragging by laser tweezers: fence versus tether. J Cell Biol 1995, 129:1559-1574. Transferrin receptors were labelled with either 40 nm colloidal gold particles or 210nm latex particles and were dragged by laser tweezers along the plasma membrane. For 90% of the receptors, which were undergoing rapid confined diffusion, the distance dragged was consistent with the size of the membrane compartments observed by SPT [39] at a trapping force of 0.05-0.1 pN. The force needed to get over the barriers at the compartment boundaries was 0.1 pN (half of the molecules pass the fences with this force). The remaining 10% of the receptors could not be dragged and were likely to be tethered to the cytoskeleton. The rebound motion of particles after escape from the optical trap suggested that both barriers and tethers were elastic, with an elastic constant between 1-10 pN/μm.
    • (1995) J Cell Biol , vol.129 , pp. 1559-1574
    • Sako, Y.1    Kusumi, A.2
  • 51
    • 0019304034 scopus 로고
    • Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes
    • 51. Sheetz MP, Schindler M, Koppel DE: Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes. Nature 1980, 285:510-512.
    • (1980) Nature , vol.285 , pp. 510-512
    • Sheetz, M.P.1    Schindler, M.2    Koppel, D.E.3
  • 52
    • 0029147973 scopus 로고
    • Barrier-free paths of directed protein motion in the erythrocyte plasma membrane
    • -1.4, where S is proportional to the sum of the protein and cytoskeleton chain radii.
    • (1995) Biophys J , vol.69 , pp. 372-379
    • Boal, D.H.1    Boey, S.K.2
  • 53
    • 0027938023 scopus 로고
    • Molecular maps of red cell deformation: Hidden elasticity and in situ connectivity
    • 53. Discher DE, Mohandas N, Evans EA: Molecular maps of red cell deformation: hidden elasticity and in situ connectivity. Science 1994, 266:1032-1035.
    • (1994) Science , vol.266 , pp. 1032-1035
    • Discher, D.E.1    Mohandas, N.2    Evans, E.A.3
  • 55
    • 0028943834 scopus 로고
    • Mechanical properties of neuronal growth cone membranes studied by tether formation with laser optical tweezers
    • 55. Dai J, Sheetz MP: Mechanical properties of neuronal growth cone membranes studied by tether formation with laser optical tweezers. Biophys J 1995, 68:988-996.
    • (1995) Biophys J , vol.68 , pp. 988-996
    • Dai, J.1    Sheetz, M.P.2
  • 56
    • 0027232839 scopus 로고
    • Glycoprotein motility and dynamic domains in fluid plasma membranes
    • 56. Sheetz MP: Glycoprotein motility and dynamic domains in fluid plasma membranes. Annu Rev Biophys Biomol Struct 1993, 22:417-431.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 417-431
    • Sheetz, M.P.1
  • 57
    • 0020174113 scopus 로고
    • Lateral diffusion in an archipelago (effects of impermeable patches on diffusion in a cell membrane)
    • 57. Saxton MJ: Lateral diffusion in an archipelago (effects of impermeable patches on diffusion in a cell membrane). Biophys J 1982, 39:165-173.
    • (1982) Biophys J , vol.39 , pp. 165-173
    • Saxton, M.J.1
  • 58
    • 0023492928 scopus 로고
    • Lateral diffusion in an archipelago (the effect of mobile obstacles)
    • 58. Saxton MJ: Lateral diffusion in an archipelago (the effect of mobile obstacles). Biophys J 1987, 52:989-997.
    • (1987) Biophys J , vol.52 , pp. 989-997
    • Saxton, M.J.1
  • 59
    • 0024723988 scopus 로고
    • Lateral diffusion in an archipelago. Distance dependence of the diffusion coefficient
    • 59. Saxton MJ: Lateral diffusion in an archipelago. Distance dependence of the diffusion coefficient. Biophys J 1989, 56:615-622.
    • (1989) Biophys J , vol.56 , pp. 615-622
    • Saxton, M.J.1
  • 60
    • 0028343033 scopus 로고
    • Molecular organization and dynamics in bacteriorhodopsin-rich reconstituted membranes: Discrimination of lipid environments by the oxygen transport parameter using a pulse ESR spin-labeling technique
    • 60. Ashikawa I, Yin J-J, Subczynski WK, Kouyama T, Hyde JS, Kusumi A: Molecular organization and dynamics in bacteriorhodopsin-rich reconstituted membranes: discrimination of lipid environments by the oxygen transport parameter using a pulse ESR spin-labeling technique. Biochemistry 1994, 33:4947-4952.
    • (1994) Biochemistry , vol.33 , pp. 4947-4952
    • Ashikawa, I.1    Yin, J.-J.2    Subczynski, W.K.3    Kouyama, T.4    Hyde, J.S.5    Kusumi, A.6
  • 61
    • 0026076574 scopus 로고
    • Lateral diffusion of membrane-spanning and glycosylphosphatidylinositol-linked proteins: Toward establishing rules governing the lateral mobility of membrane proteins
    • 61. Zhang F, Crise B, Su B, Hou Y, Rose JK, Bothwell A, Jacobson K: Lateral diffusion of membrane-spanning and glycosylphosphatidylinositol-linked proteins: toward establishing rules governing the lateral mobility of membrane proteins. J Cell Biol 1991, 115:75-84.
    • (1991) J Cell Biol , vol.115 , pp. 75-84
    • Zhang, F.1    Crise, B.2    Su, B.3    Hou, Y.4    Rose, J.K.5    Bothwell, A.6    Jacobson, K.7
  • 62
    • 0026725343 scopus 로고
    • The lateral mobility of some membrane proteins is determined by their ectodomains
    • 62. Zhang F, Crise B, Su B, Hou Y, Rose JK, Bothwell A, Jacobson K: The lateral mobility of some membrane proteins is determined by their ectodomains. Biophys J 1992, 62:92-94.
    • (1992) Biophys J , vol.62 , pp. 92-94
    • Zhang, F.1    Crise, B.2    Su, B.3    Hou, Y.4    Rose, J.K.5    Bothwell, A.6    Jacobson, K.7
  • 63
    • 0027392157 scopus 로고
    • Unconfined lateral diffusion and an estimate of pericellular matrix viscosity revealed by measuring the mobility of gold-tagged lipids
    • 63. Lee GM, Zhang F, Ishihara A, McNeil CL, Jacobson K: Unconfined lateral diffusion and an estimate of pericellular matrix viscosity revealed by measuring the mobility of gold-tagged lipids. J Cell Biol 1993, 120:25-35.
    • (1993) J Cell Biol , vol.120 , pp. 25-35
    • Lee, G.M.1    Zhang, F.2    Ishihara, A.3    McNeil, C.L.4    Jacobson, K.5
  • 64
    • 0025325763 scopus 로고
    • The membrane skeleton of erythrocytes (a percolation model)
    • 64. Saxton MJ: The membrane skeleton of erythrocytes (a percolation model). Biophys J 1990, 57:1167-1177.
    • (1990) Biophys J , vol.57 , pp. 1167-1177
    • Saxton, M.J.1
  • 65
    • 0012047619 scopus 로고
    • Fractile time transport in the cell surface
    • 65. Webb WW: Fractile time transport in the cell surface [abstract]. Biophys J 1994, 66:18.
    • (1994) Biophys J , vol.66 , pp. 18
    • Webb, W.W.1
  • 66
    • 0028138521 scopus 로고
    • Regulated internalization of caveolae
    • 66. Parton RG, Joggerst B, Simons K: Regulated internalization of caveolae. J Cell Biol 1994, 127:1199-1215.
    • (1994) J Cell Biol , vol.127 , pp. 1199-1215
    • Parton, R.G.1    Joggerst, B.2    Simons, K.3
  • 67
    • 0027640552 scopus 로고
    • Transport and sorting of membrane lipids
    • 67. Van Meer G: Transport and sorting of membrane lipids. Curr Opin Cell Biol 1993, 5:661-667.
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 661-667
    • Van Meer, G.1
  • 68
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins
    • M1 is enriched in caveolae, whereas GPI-anchored proteins are located adjacent to caveolae on the flat plasma membrane. The purified caveolae contained molecular components required for regulated transport, including various lipid-anchored signaling molecules.
    • (1995) Science , vol.269 , pp. 1435-1439
    • Schnitzer, J.E.1    McIntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5
  • 69
    • 0028885614 scopus 로고
    • VIP21/caveolin is a cholesterol-binding protein
    • 69. Murata M, Perämen J, Schreiner R, Wieland F, Kurzchalia TV, Simons K: VIP21/caveolin is a cholesterol-binding protein. Proc Natl Acad Sci USA 1995, 92:10339-10343. VIP21/caveolin was the first protein to be localized in caveolae. In this work, E. coli-expressed VIP21-caveolin was reconstituted in liposomes. The protein reconstituted only with cholesterol-containing lipid mixtures, and formed oligomers. The protein binds at least one mole of cholesterol per mole of protein. These results suggest that VIP21-caveolin, through its cholesterol-binding and self-associating properties, serves a specific function in the formation of sphingolipid-cholesterol rafts during membrane trafficking.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10339-10343
    • Murata, M.1    Perämen, J.2    Schreiner, R.3    Wieland, F.4    Kurzchalia, T.V.5    Simons, K.6
  • 70
    • 0027398589 scopus 로고
    • Spatial and temporal dissection of immediate and early events following cadherin-mediated epithelial cell adhesion
    • 70. McNeill H, Ryan TA, Smith SJ, Nelson WJ: Spatial and temporal dissection of immediate and early events following cadherin-mediated epithelial cell adhesion. J Cell Biol 1993, 120:1217-1226.
    • (1993) J Cell Biol , vol.120 , pp. 1217-1226
    • McNeill, H.1    Ryan, T.A.2    Smith, S.J.3    Nelson, W.J.4
  • 71
    • 0028807349 scopus 로고
    • Axon membrane flows from the growth cone to the cell body
    • 71. Dai J, Sheetz MP: Axon membrane flows from the growth cone to the cell body. Cell 1995, 83:693-701. Using latex particles non-specifically attached to the chick dorsal root ganglion cell surface, the authors found a fast flow of axonal membrane (over 7 μm/min) from the growth cone to the cell body during axonal growth. This flow is powered by a gradient of membrane tension in the same direction. When beads at the center of the axon were pulled perpendicularly to the membrane by an optical trap, a process which induced an artificial membrane flow toward the center of the axon, 80% of the membrane came from the growth cone side. The authors suggest that, during neuron growth, excess membrane is added at the growth cone, which creates a flow that can rapidly alter the content of the axon membrane.
    • (1995) Cell , vol.83 , pp. 693-701
    • Dai, J.1    Sheetz, M.P.2
  • 73
    • 0029326401 scopus 로고
    • Near-field optical microscopy in liquids
    • 73. Muramatsu H, Chiba N, Homma K, Nakajima K, Ataka T, Ohta S, Kusumi A, Fujihira M: Near-field optical microscopy in liquids. Appl Phys Lett 1995, 66:3245-3247. The first report on the development of the scanning near-field optical microscope which can be applied to samples in liquids including water. The tip-sample separation was controlled by the method of the non-contact dynamic mode atomic force microscope. The first observation of cultured cells in aqueous solution was made.
    • (1995) Appl Phys Lett , vol.66 , pp. 3245-3247
    • Muramatsu, H.1    Chiba, N.2    Homma, K.3    Nakajima, K.4    Ataka, T.5    Ohta, S.6    Kusumi, A.7    Fujihira, M.8
  • 74
    • 0029062769 scopus 로고
    • Sensitive force technique to probe molecular adhesion and structural linkages at biological interfaces
    • 3pN. A microscopic bead is biochemically attached to the transducer as a surface probe. This apparatus was applied to measure local mechanical compliance of the BHK (baby hamster kidney) cell surface at a displacement resolution set by structural fluctuations.
    • (1995) Biophys J , vol.68 , pp. 2580-2587
    • Evans, E.1    Ritchie, K.2    Merkel, R.3
  • 75
    • 0027682459 scopus 로고
    • Scanning-force microscope based on an optical trap
    • 75. Ghislain LP, Webb WW: Scanning-force microscope based on an optical trap. Opt Letters 1993, 18:1678-1680.
    • (1993) Opt Letters , vol.18 , pp. 1678-1680
    • Ghislain, L.P.1    Webb, W.W.2
  • 76
    • 85030200271 scopus 로고    scopus 로고
    • 3-d scanning probe microscope based on optical tweezers and 2-photon excitation by a cw-Nd:YAG laser
    • 76. Florin E-L, Hörber JKH, Stelzer EHK: 3-D scanning probe microscope based on optical tweezers and 2-photon excitation by a cw-Nd:YAG laser [abstract]. Biophys J 1996, 70:431.
    • (1996) Biophys J , vol.70 , pp. 431
    • Florin, E.-L.1    Hörber, J.K.H.2    Stelzer, E.H.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.