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Volumn 171, Issue 1, 2005, Pages 121-131

Condensation of the plasma membrane at the site of T lymphocyte activation

Author keywords

[No Author keywords available]

Indexed keywords

CD28 ANTIGEN; FLUORESCENT DYE; MEMBRANE PROTEIN;

EID: 26444452661     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200505047     Document Type: Article
Times cited : (210)

References (55)
  • 1
    • 0347505003 scopus 로고    scopus 로고
    • CD28-mediated co-stimulation: A quantitative support for TCR signalling
    • Acuto, O., and F. Michel. 2003. CD28-mediated co-stimulation: a quantitative support for TCR signalling. Nat. Rev. Immunol. 3:939-951.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 939-951
    • Acuto, O.1    Michel, F.2
  • 4
    • 12244278268 scopus 로고    scopus 로고
    • Giant vesicles, Laurdan, and two-photon fluorescence microscopy: Evidence of lipid lateral separation in bilayers
    • Bagatolli, L.A., S.A. Sanchez, T. Hazlett, and E. Gratton. 2003. Giant vesicles, Laurdan, and two-photon fluorescence microscopy: evidence of lipid lateral separation in bilayers. Methods Enzymol. 360:481-500.
    • (2003) Methods Enzymol. , vol.360 , pp. 481-500
    • Bagatolli, L.A.1    Sanchez, S.A.2    Hazlett, T.3    Gratton, E.4
  • 6
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown, D.A., and E. London. 1998. Structure and origin of ordered lipid domains in biological membranes. J. Membr. Biol. 164:103-114.
    • (1998) J. Membr. Biol. , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 7
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown, D.A., and E. London. 2000. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275:17221-17224.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 8
    • 0035075507 scopus 로고    scopus 로고
    • Dynamic actin polymerization drives T cell receptor-induced spreading: A role for the signal transduction adaptor LAT
    • Bunnell, S.C., V. Kapoor, R.P. Trible, W. Zhang, and L.E. Samelson. 2001. Dynamic actin polymerization drives T cell receptor-induced spreading: a role for the signal transduction adaptor LAT. Immunity. 14:315-329.
    • (2001) Immunity , vol.14 , pp. 315-329
    • Bunnell, S.C.1    Kapoor, V.2    Trible, R.P.3    Zhang, W.4    Samelson, L.E.5
  • 11
    • 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
    • Douglass, A.D., and R.D. Vale. 2005. Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell. 121:937-950.
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 13
    • 0035213174 scopus 로고    scopus 로고
    • Rafts and synapses in the spatial organization of immune cell signaling receptors
    • Dykstra, M., A. Cherukuri, and S.K. Pierce. 2001. Rafts and synapses in the spatial organization of immune cell signaling receptors. J. Leukoc. Biol. 70:699-707.
    • (2001) J. Leukoc. Biol. , vol.70 , pp. 699-707
    • Dykstra, M.1    Cherukuri, A.2    Pierce, S.K.3
  • 15
    • 0002708386 scopus 로고
    • An analysis of T cell receptor-ligand interaction using a transgenic antigen model for T cell tolerance and T cell receptor mutagenesis
    • F.W. Alt and H.J. Vogel, editors. Academic Press, San Diego, CA
    • Fazekas de St. Groth, B., P.A. Patten, W.Y. Ho, E.P. Rock, and M.M. Davis. 1993. An analysis of T cell receptor-ligand interaction using a transgenic antigen model for T cell tolerance and T cell receptor mutagenesis. In Molecular Mechanisms of Immunological Self-Recognition. F.W. Alt and H.J. Vogel, editors. Academic Press, San Diego, CA. 123-127.
    • (1993) Molecular Mechanisms of Immunological Self-Recognition , pp. 123-127
    • Fazekas De St Groth, B.1    Patten, P.A.2    Ho, W.Y.3    Rock, E.P.4    Davis, M.M.5
  • 18
    • 1542399850 scopus 로고    scopus 로고
    • Lipid raft proteins have a random distribution during localized activation of the T-cell receptor
    • Glebov, O.O., and B.J. Nichols. 2004. Lipid raft proteins have a random distribution during localized activation of the T-cell receptor. Nat. Cell Biol. 6:238-243.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 238-243
    • Glebov, O.O.1    Nichols, B.J.2
  • 19
    • 2342492829 scopus 로고    scopus 로고
    • Lipid raft domains and protein networks in T-cell receptor signal transduction
    • Harder, T. 2004. Lipid raft domains and protein networks in T-cell receptor signal transduction. Curr. Opin. Immunol. 16:353-359.
    • (2004) Curr. Opin. Immunol. , vol.16 , pp. 353-359
    • Harder, T.1
  • 20
    • 0033033321 scopus 로고    scopus 로고
    • Clusters of glycolipid and glycosylphosphatidylinositol-anchored proteins in lymphoid cells: Accumulation of actin regulated by local tyrosine phosphorylation
    • Harder, T., and K. Simons. 1999. Clusters of glycolipid and glycosylphosphatidylinositol-anchored proteins in lymphoid cells: accumulation of actin regulated by local tyrosine phosphorylation. Eur. J. Immunol. 29:556-562.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 556-562
    • Harder, T.1    Simons, K.2
  • 21
    • 0034675889 scopus 로고    scopus 로고
    • Selective accumulation of raft-associated membrane protein LAT in T cell receptor signaling assemblies
    • Harder, T., and M. Kuhn. 2000. Selective accumulation of raft-associated membrane protein LAT in T cell receptor signaling assemblies. J. Cell Biol. 151:199-208.
    • (2000) J. Cell Biol. , vol.151 , pp. 199-208
    • Harder, T.1    Kuhn, M.2
  • 22
    • 0035957138 scopus 로고    scopus 로고
    • Immunoisolation of TCR signaling complexes from Jurkat T leukemic cells
    • 10.1126/stke.2001.71.pl1
    • Harder, T., and M. Kuhn. 2001. Immunoisolation of TCR signaling complexes from Jurkat T leukemic cells. Sci. STKE. 10.1126/stke.2001.71.pl1.
    • (2001) Sci. STKE
    • Harder, T.1    Kuhn, M.2
  • 23
    • 0037490183 scopus 로고    scopus 로고
    • Synergistic assembly of linker for activation of T cells signaling protein complexes in T cell plasma membrane domains
    • Hartgroves, L.C., J. Lin, H. Langen, T. Zech, A. Weiss, and T. Harder. 2003. Synergistic assembly of linker for activation of T cells signaling protein complexes in T cell plasma membrane domains. J. Biol. Chem. 278:20389-20394.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20389-20394
    • Hartgroves, L.C.1    Lin, J.2    Langen, H.3    Zech, T.4    Weiss, A.5    Harder, T.6
  • 24
    • 0346244099 scopus 로고    scopus 로고
    • T-cell-antigen recognition and the immunological synapse
    • Huppa, J.B., and M.M. Davis. 2003. T-cell-antigen recognition and the immunological synapse. Nat. Rev. Immunol. 3:973-983.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 973-983
    • Huppa, J.B.1    Davis, M.M.2
  • 25
    • 0033998793 scopus 로고    scopus 로고
    • The role of lipid rafts in T cell antigen receptor (TCR) signalling
    • Janes, P.W., S.C. Ley, A.I. Magee, and P.S. Kabouridis. 2000. The role of lipid rafts in T cell antigen receptor (TCR) signalling. Semin. Immunol. 12:23-34.
    • (2000) Semin. Immunol. , vol.12 , pp. 23-34
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3    Kabouridis, P.S.4
  • 26
    • 0033993454 scopus 로고    scopus 로고
    • Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes
    • Kabouridis, P.S., J. Janzen, A.L. Magee, and S.C. Ley. 2000. Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes. Eur. J. Immunol. 30:954-963.
    • (2000) Eur. J. Immunol. , vol.30 , pp. 954-963
    • Kabouridis, P.S.1    Janzen, J.2    Magee, A.L.3    Ley, S.C.4
  • 28
    • 1842529359 scopus 로고    scopus 로고
    • Cutting edge: Optical microspectrophotometry supports the existence of gel phase lipid rafts at the lamellipodium of neutrophils: Apparent role in calcium signaling
    • Kindzelskii, A.L., R.G. Sitrin, and H.R. Petty. 2004. Cutting edge: optical microspectrophotometry supports the existence of gel phase lipid rafts at the lamellipodium of neutrophils: apparent role in calcium signaling. J. Immunol. 172:4681-4685.
    • (2004) J. Immunol. , vol.172 , pp. 4681-4685
    • Kindzelskii, A.L.1    Sitrin, R.G.2    Petty, H.R.3
  • 29
    • 0035342013 scopus 로고    scopus 로고
    • Molecular controls of antigen receptor clustering and autoimmunity
    • Krawczyk, C., and J.M. Penninger. 2001. Molecular controls of antigen receptor clustering and autoimmunity. Trends Cell Biol. 11:212-220.
    • (2001) Trends Cell Biol. , vol.11 , pp. 212-220
    • Krawczyk, C.1    Penninger, J.M.2
  • 30
    • 1842432088 scopus 로고    scopus 로고
    • Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts
    • Kusumi, A., I. Koyama-Honda, and K. Suzuki. 2004. Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts. Traffic. 5:213-230.
    • (2004) Traffic , vol.5 , pp. 213-230
    • Kusumi, A.1    Koyama-Honda, I.2    Suzuki, K.3
  • 31
    • 0035800805 scopus 로고    scopus 로고
    • Identification of the minimal tyrosine residues required for linker for activation of T cell function
    • Lin, J., and A. Weiss. 2001. Identification of the minimal tyrosine residues required for linker for activation of T cell function. J. Biol. Chem. 276:29588-29595.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29588-29595
    • Lin, J.1    Weiss, A.2
  • 33
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks, C.R., B.A. Freiberg, H. Kupfer, N. Sciaky, and A. Kupfer. 1998. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature. 395:82-86.
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 35
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • Munro, S. 2003. Lipid rafts: elusive or illusive? Cell. 115:377-388.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 37
    • 12744262695 scopus 로고    scopus 로고
    • Merging complexes: Properties of membrane raft assembly during lymphocyte signaling
    • Rodgers, W., D. Farris, and S. Mishra. 2005. Merging complexes: properties of membrane raft assembly during lymphocyte signaling. Trends Immunol. 26:97-103.
    • (2005) Trends Immunol. , vol.26 , pp. 97-103
    • Rodgers, W.1    Farris, D.2    Mishra, S.3
  • 38
    • 0036221481 scopus 로고    scopus 로고
    • Signal transduction mediated by the T cell antigen receptor: The role of adapter proteins
    • Samelson, L.E. 2002. Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins. Annu. Rev. Immunol. 20:371-394.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 371-394
    • Samelson, L.E.1
  • 39
    • 0026058545 scopus 로고
    • Cholesterol-induced fluid-phase immiscibility in membranes
    • Sankaram, M.B., and T.E. Thompson. 1991. Cholesterol-induced fluid-phase immiscibility in membranes. Proc. Natl. Acad. Sci. USA. 88:8686-8690.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8686-8690
    • Sankaram, M.B.1    Thompson, T.E.2
  • 42
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and E. Ikonen. 1997. Functional rafts in cell membranes. Nature. 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 44
    • 6344241298 scopus 로고    scopus 로고
    • CD28 and lipid rafts coordinate recruitment of Lck to the immunological synapse of human T lymphocytes
    • Tavano, R., G. Gri, B. Molon, B. Marinari, C.E. Rudd, L. Tuosto, and A. Viola. 2004. CD28 and lipid rafts coordinate recruitment of Lck to the immunological synapse of human T lymphocytes. J. Immunol. 173:5392-5397.
    • (2004) J. Immunol. , vol.173 , pp. 5392-5397
    • Tavano, R.1    Gri, G.2    Molon, B.3    Marinari, B.4    Rudd, C.E.5    Tuosto, L.6    Viola, A.7
  • 45
    • 0033672473 scopus 로고    scopus 로고
    • Lymphocytes with a complex: Adapter proteins in antigen receptor signaling
    • Tomlinson, M.G., J. Lin, and A. Weiss. 2000. Lymphocytes with a complex: adapter proteins in antigen receptor signaling. Immunol. Today. 21:584-591.
    • (2000) Immunol. Today , vol.21 , pp. 584-591
    • Tomlinson, M.G.1    Lin, J.2    Weiss, A.3
  • 46
    • 0036915756 scopus 로고    scopus 로고
    • Do T cell receptors do it alone?
    • van der Merwe, P.A. 2002. Do T cell receptors do it alone? Nat. Immunol. 3:1122-1123.
    • (2002) Nat. Immunol. , vol.3 , pp. 1122-1123
    • Van Der Merwe, P.A.1
  • 47
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma, R., and S. Mayor. 1998. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature. 394:798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 48
    • 0035851918 scopus 로고    scopus 로고
    • Vav1/Rac-dependent actin cytoskeleton reorganization is required for lipid raft clustering in T cells
    • Villalba, M., K. Bi, F. Rodriguez, Y. Tanaka, S. Schoenberger, and A. Altman. 2001. Vav1/Rac-dependent actin cytoskeleton reorganization is required for lipid raft clustering in T cells. J. Cell Biol. 155:331-338.
    • (2001) J. Cell Biol. , vol.155 , pp. 331-338
    • Villalba, M.1    Bi, K.2    Rodriguez, F.3    Tanaka, Y.4    Schoenberger, S.5    Altman, A.6
  • 49
    • 0037092038 scopus 로고    scopus 로고
    • Translocation of PKC[τ] in T cells is mediated by a nonconventional, PI3-K- and Vav-dependent pathway, but does not absolutely require phospholipase C
    • Villalba, M., K. Bi, J. Hu, Y. Altman, P. Bushway, E. Reits, J. Neefjes, G. Baier, R.T. Abraham, and A. Altman. 2002. Translocation of PKC[τ] in T cells is mediated by a nonconventional, PI3-K- and Vav-dependent pathway, but does not absolutely require phospholipase C. J. Cell Biol. 157:253-263.
    • (2002) J. Cell Biol. , vol.157 , pp. 253-263
    • Villalba, M.1    Bi, K.2    Hu, J.3    Altman, Y.4    Bushway, P.5    Reits, E.6    Neefjes, J.7    Baier, G.8    Abraham, R.T.9    Altman, A.10
  • 50
    • 0033613826 scopus 로고    scopus 로고
    • T lymphocyte costimulation mediated by reorganization of membrane microdomains
    • Viola, A., S. Schroeder, Y. Sakakibara, and A. Lanzavecchia. 1999. T lymphocyte costimulation mediated by reorganization of membrane microdomains. Science. 283:680-682.
    • (1999) Science , vol.283 , pp. 680-682
    • Viola, A.1    Schroeder, S.2    Sakakibara, Y.3    Lanzavecchia, A.4
  • 51
    • 0031570952 scopus 로고    scopus 로고
    • Dendritic cell subtypes in mouse lymphoid organs. Cross-correlation of surface markers, changes with incubation and differences among thymus, spleen and lymph nodes
    • Vremec, D., and K. Shortman. 1997. Dendritic cell subtypes in mouse lymphoid organs. Cross-correlation of surface markers, changes with incubation and differences among thymus, spleen and lymph nodes. J. Immunol. 159:565-573.
    • (1997) J. Immunol. , vol.159 , pp. 565-573
    • Vremec, D.1    Shortman, K.2
  • 52
    • 0034874686 scopus 로고    scopus 로고
    • Regulation of phospholipase C gamma isoforms in haematopoietic cells: Why one, not the other?
    • Wilde, J.I., and S.P. Watson. 2001. Regulation of phospholipase C gamma isoforms in haematopoietic cells: why one, not the other? Cell. Signal. 13:691-701.
    • (2001) Cell. Signal. , vol.13 , pp. 691-701
    • Wilde, J.I.1    Watson, S.P.2
  • 53
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias, D.A., J.D. Violin, A.C. Newton, and R.Y. Tsien. 2002. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science. 296:913-916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 54
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • Zhang, W., J. Sloan-Lancaster, J. Kitchen, R.P. Trible, and L.E. Samelson. 1998a. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell. 92:83-92.
    • (1998) Cell , vol.92 , pp. 83-92
    • Zhang, W.1    Sloan-Lancaster, J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 55
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang, W., R.P. Trible, and L.E. Samelson. 1998b. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity. 9:239-246.
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3


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