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Volumn 26, Issue 2, 2005, Pages 97-103

Merging complexes: Properties of membrane raft assembly during lymphocyte signaling

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MEMBRANE LIPID;

EID: 12744262695     PISSN: 14714906     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.it.2004.11.016     Document Type: Review
Times cited : (53)

References (72)
  • 2
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • R. Xavier Membrane compartmentation is required for efficient T cell activation Immunity 8 1998 723 732
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1
  • 3
    • 0030746106 scopus 로고    scopus 로고
    • S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes
    • P.S. Kabouridis S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes EMBO J. 16 1997 4983 4998
    • (1997) EMBO J. , vol.16 , pp. 4983-4998
    • Kabouridis, P.S.1
  • 4
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • P. Sharma 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
  • 5
    • 2542472339 scopus 로고    scopus 로고
    • Markers for detergent-resistant lipid rafts occupy distinct and dynamic domains in native membranes
    • B.S. Wilson Markers for detergent-resistant lipid rafts occupy distinct and dynamic domains in native membranes Mol. Biol. Cell 15 2004 2580 2592
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2580-2592
    • Wilson, B.S.1
  • 6
    • 0035879095 scopus 로고    scopus 로고
    • Glycolipid-enriched membrane domains are assembled into membrane patches by associating with the actin cytoskeleton
    • W. Rodgers, and J. Zavzavadjian Glycolipid-enriched membrane domains are assembled into membrane patches by associating with the actin cytoskeleton Exp. Cell Res. 267 2001 173 183
    • (2001) Exp. Cell Res. , vol.267 , pp. 173-183
    • Rodgers, W.1    Zavzavadjian, J.2
  • 7
    • 0037869152 scopus 로고    scopus 로고
    • T cell glycolipid-enriched membrane domains are constitutively assembled as membrane patches that translocate to immune synapses
    • S. Jordan, and W. Rodgers T cell glycolipid-enriched membrane domains are constitutively assembled as membrane patches that translocate to immune synapses J. Immunol. 171 2003 78 87
    • (2003) J. Immunol. , vol.171 , pp. 78-87
    • Jordan, S.1    Rodgers, W.2
  • 8
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • I.A. Prior 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
  • 9
    • 0033613826 scopus 로고    scopus 로고
    • T lymphocyte costimulation mediated by reorganization of membrane microdomains
    • A. Viola T lymphocyte costimulation mediated by reorganization of membrane microdomains Science 283 1999 680 682
    • (1999) Science , vol.283 , pp. 680-682
    • Viola, A.1
  • 10
    • 0037105477 scopus 로고    scopus 로고
    • Quantitative imaging of raft accumulation in the immunological synapse
    • W.R. Burack Quantitative imaging of raft accumulation in the immunological synapse J. Immunol. 169 2002 2837 2841
    • (2002) J. Immunol. , vol.169 , pp. 2837-2841
    • Burack, W.R.1
  • 11
    • 0842343443 scopus 로고    scopus 로고
    • Visualization of antigen presentation by actin-mediated targeting of glycolipid-enriched membrane domains to the immune synapse of B cell APCs
    • C. Gordy Visualization of antigen presentation by actin-mediated targeting of glycolipid-enriched membrane domains to the immune synapse of B cell APCs J. Immunol. 172 2004 2030 2038
    • (2004) J. Immunol. , vol.172 , pp. 2030-2038
    • Gordy, C.1
  • 12
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • C.R. Monks Three-dimensional segregation of supramolecular activation clusters in T cells Nature 395 1998 82 86
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1
  • 13
    • 0037154747 scopus 로고    scopus 로고
    • T cell receptor signaling precedes immunological synapse formation
    • K.H. Lee T cell receptor signaling precedes immunological synapse formation Science 295 2002 1539 1542
    • (2002) Science , vol.295 , pp. 1539-1542
    • Lee, K.H.1
  • 14
    • 0032727709 scopus 로고    scopus 로고
    • Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor
    • P.W. Janes 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
  • 15
    • 0036253813 scopus 로고    scopus 로고
    • Making membranes green: Construction and characterization of GFP-fusion proteins targeted to discrete plasma membrane domains
    • W. Rodgers Making membranes green: construction and characterization of GFP-fusion proteins targeted to discrete plasma membrane domains Biotechniques 32 2002 1044 1051
    • (2002) Biotechniques , vol.32 , pp. 1044-1051
    • Rodgers, W.1
  • 16
    • 0032438178 scopus 로고    scopus 로고
    • Engagement of GPI-linked CD48 contributes to TCR signals and cytoskeletal reorganization: A role for lipid rafts in T cell activation
    • M. Moran, and M.C. Miceli Engagement of GPI-linked CD48 contributes to TCR signals and cytoskeletal reorganization: a role for lipid rafts in T cell activation Immunity 9 1998 787 796
    • (1998) Immunity , vol.9 , pp. 787-796
    • Moran, M.1    Miceli, M.C.2
  • 17
    • 0035433580 scopus 로고    scopus 로고
    • Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains
    • P.D. von Haller Mass spectrometric characterization of proteins extracted from Jurkat T cell detergent-resistant membrane domains Proteomics 1 2001 1010 1021
    • (2001) Proteomics , vol.1 , pp. 1010-1021
    • Von Haller, P.D.1
  • 18
    • 0037044851 scopus 로고    scopus 로고
    • Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes
    • T. Nebl Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes J. Biol. Chem. 277 2002 43399 43409
    • (2002) J. Biol. Chem. , vol.277 , pp. 43399-43409
    • Nebl, T.1
  • 19
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • L.J. Foster Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors Proc. Natl. Acad. Sci. U. S. A. 100 2003 5813 5818
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5813-5818
    • Foster, L.J.1
  • 20
    • 0037008853 scopus 로고    scopus 로고
    • Clustering of a lipid-raft associated pool of ERM proteins at the immunological synapse upon T cell receptor or CD28 ligation
    • E.M. Tomas Clustering of a lipid-raft associated pool of ERM proteins at the immunological synapse upon T cell receptor or CD28 ligation Immunol. Lett. 83 2002 143 147
    • (2002) Immunol. Lett. , vol.83 , pp. 143-147
    • Tomas, E.M.1
  • 21
    • 0032498528 scopus 로고    scopus 로고
    • Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association
    • T. Matsui Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association J. Cell Biol. 140 1998 647 657
    • (1998) J. Cell Biol. , vol.140 , pp. 647-657
    • Matsui, T.1
  • 22
    • 0035955452 scopus 로고    scopus 로고
    • Interaction between two adapter proteins, PAG and EBP50: A possible link between membrane rafts and actin cytoskeleton
    • N. Brdickova Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton FEBS Lett. 507 2001 133 136
    • (2001) FEBS Lett. , vol.507 , pp. 133-136
    • Brdickova, N.1
  • 23
    • 0032571406 scopus 로고    scopus 로고
    • Protein kinase C-θ phosphorylation of moesin in the actin-binding sequence
    • S.F. Pietromonaco Protein kinase C-θ phosphorylation of moesin in the actin-binding sequence J. Biol. Chem. 273 1998 7594 7603
    • (1998) J. Biol. Chem. , vol.273 , pp. 7594-7603
    • Pietromonaco, S.F.1
  • 24
    • 0035374476 scopus 로고    scopus 로고
    • Antigen-induced translocation of PKC-θ to membrane rafts is required for T cell activation
    • K. Bi Antigen-induced translocation of PKC-θ to membrane rafts is required for T cell activation Nat. Immunol. 2 2001 556 563
    • (2001) Nat. Immunol. , vol.2 , pp. 556-563
    • Bi, K.1
  • 25
    • 0029899011 scopus 로고    scopus 로고
    • Phosphoinositides and phosphoinositide-utilizing enzymes in detergent-insoluble lipid domains
    • H.R. Hope, and L.J. Pike Phosphoinositides and phosphoinositide-utilizing enzymes in detergent-insoluble lipid domains Mol. Biol. Cell 7 1996 843 851
    • (1996) Mol. Biol. Cell , vol.7 , pp. 843-851
    • Hope, H.R.1    Pike, L.J.2
  • 26
    • 0035881755 scopus 로고    scopus 로고
    • New EMBO members' review: Actin cytoskeleton regulation through modulation of PI(4,5)P(2) rafts
    • P. Caroni New EMBO members' review: actin cytoskeleton regulation through modulation of PI(4,5)P(2) rafts EMBO J. 20 2001 4332 4336
    • (2001) EMBO J. , vol.20 , pp. 4332-4336
    • Caroni, P.1
  • 27
    • 0033677862 scopus 로고    scopus 로고
    • The actin cytoskeleton and plasma membrane connection: PtdIns(4,5)P(2) influences cytoskeletal protein activity at the plasma membrane
    • A.S. Sechi, and J. Wehland The actin cytoskeleton and plasma membrane connection: PtdIns(4,5)P(2) influences cytoskeletal protein activity at the plasma membrane J. Cell Sci. 113 2000 3685 3695
    • (2000) J. Cell Sci. , vol.113 , pp. 3685-3695
    • Sechi, A.S.1    Wehland, J.2
  • 28
    • 0037392883 scopus 로고    scopus 로고
    • Positive and negative regulation of T-cell activation through kinases and phosphatases
    • T. Mustelin, and K. Tasken Positive and negative regulation of T-cell activation through kinases and phosphatases Biochem. J. 371 2003 15 27
    • (2003) Biochem. J. , vol.371 , pp. 15-27
    • Mustelin, T.1    Tasken, K.2
  • 29
    • 0032493028 scopus 로고    scopus 로고
    • Defects in actin-cap formation in Vav-deficient mice implicate an actin requirement for lymphocyte signal transduction
    • L.J. Holsinger Defects in actin-cap formation in Vav-deficient mice implicate an actin requirement for lymphocyte signal transduction Curr. Biol. 8 1998 563 572
    • (1998) Curr. Biol. , vol.8 , pp. 563-572
    • Holsinger, L.J.1
  • 30
    • 13144259727 scopus 로고    scopus 로고
    • Vav is a regulator of cytoskeletal reorganization mediated by the T-cell receptor
    • K.D. Fischer Vav is a regulator of cytoskeletal reorganization mediated by the T-cell receptor Curr. Biol. 8 1998 554 562
    • (1998) Curr. Biol. , vol.8 , pp. 554-562
    • Fischer, K.D.1
  • 31
    • 0036794399 scopus 로고    scopus 로고
    • Staging and resetting T cell activation in SMACs
    • B.A. Freiberg Staging and resetting T cell activation in SMACs Nat. Immunol. 3 2002 911 917
    • (2002) Nat. Immunol. , vol.3 , pp. 911-917
    • Freiberg, B.A.1
  • 32
    • 0032483559 scopus 로고    scopus 로고
    • A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts
    • M.L. Dustin A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts Cell 94 1998 667 677
    • (1998) Cell , vol.94 , pp. 667-677
    • Dustin, M.L.1
  • 33
    • 0041929574 scopus 로고    scopus 로고
    • CD28 engagement promotes actin polymerization through the activation of the small Rho GTPase Cdc42 in human T cells
    • L.I. Salazar-Fontana CD28 engagement promotes actin polymerization through the activation of the small Rho GTPase Cdc42 in human T cells J. Immunol. 171 2003 2225 2232
    • (2003) J. Immunol. , vol.171 , pp. 2225-2232
    • Salazar-Fontana, L.I.1
  • 34
    • 0033083257 scopus 로고    scopus 로고
    • TCR, LFA-1, and CD28 play unique and complementary roles in signaling T cell cytoskeletal reorganization
    • C.E. Sedwick TCR, LFA-1, and CD28 play unique and complementary roles in signaling T cell cytoskeletal reorganization J. Immunol. 162 1999 1367 1375
    • (1999) J. Immunol. , vol.162 , pp. 1367-1375
    • Sedwick, C.E.1
  • 35
    • 0005448458 scopus 로고    scopus 로고
    • Polarity of T cell shape, motility, and sensitivity to antigen
    • P.A. Negulescu Polarity of T cell shape, motility, and sensitivity to antigen Immunity 4 1996 421 430
    • (1996) Immunity , vol.4 , pp. 421-430
    • Negulescu, P.A.1
  • 36
    • 0035803552 scopus 로고    scopus 로고
    • Cytotoxic T lymphocyte antigen 4 and CD28 modulate cell surface raft expression in their regulation of T cell function
    • M. Martin Cytotoxic T lymphocyte antigen 4 and CD28 modulate cell surface raft expression in their regulation of T cell function J. Exp. Med. 194 2001 1675 1681
    • (2001) J. Exp. Med. , vol.194 , pp. 1675-1681
    • Martin, M.1
  • 37
    • 0035104202 scopus 로고    scopus 로고
    • Organization of plasma membrane functional rafts upon T cell activation
    • L. Tuosto Organization of plasma membrane functional rafts upon T cell activation Eur. J. Immunol. 31 2001 345 349
    • (2001) Eur. J. Immunol. , vol.31 , pp. 345-349
    • Tuosto, L.1
  • 38
    • 17144439652 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3
    • A.L. Rozelle Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3 Curr. Biol. 10 2000 311 320
    • (2000) Curr. Biol. , vol.10 , pp. 311-320
    • Rozelle, A.L.1
  • 39
    • 0030863490 scopus 로고    scopus 로고
    • Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane
    • E.D. Sheets Transient confinement of a glycosylphosphatidylinositol- anchored protein in the plasma membrane Biochemistry 36 1997 12449 12458
    • (1997) Biochemistry , vol.36 , pp. 12449-12458
    • Sheets, E.D.1
  • 40
    • 0036214457 scopus 로고    scopus 로고
    • Relationship of lipid rafts to transient confinement zones detected by single particle tracking
    • C. Dietrich Relationship of lipid rafts to transient confinement zones detected by single particle tracking Biophys. J. 82 2002 274 284
    • (2002) Biophys. J. , vol.82 , pp. 274-284
    • Dietrich, C.1
  • 41
    • 0028346560 scopus 로고
    • CD45: An emerging role as a protein tyrosine phosphatase required for lymphocyte activation and development
    • I.S. Trowbridge, and M.L. Thomas CD45: an emerging role as a protein tyrosine phosphatase required for lymphocyte activation and development Annu. Rev. Immunol. 12 1994 85 116
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 85-116
    • Trowbridge, I.S.1    Thomas, M.L.2
  • 42
    • 0028145334 scopus 로고
    • Signals determining protein tyrosine kinase and glycosyl- phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction
    • W. Rodgers Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction Mol. Cell. Biol. 14 1994 5384 5391
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5384-5391
    • Rodgers, W.1
  • 43
    • 0030453582 scopus 로고    scopus 로고
    • lck associated with glycolipid-enriched membrane domains
    • lck associated with glycolipid-enriched membrane domains J. Cell Biol. 135 1996 1515 1523
    • (1996) J. Cell Biol. , vol.135 , pp. 1515-1523
    • Rodgers, W.1    Rose, J.K.2
  • 44
    • 0037881900 scopus 로고    scopus 로고
    • Regulation of Fyn through translocation of activated Lck into lipid rafts
    • D. Filipp Regulation of Fyn through translocation of activated Lck into lipid rafts J. Exp. Med. 197 2003 1221 1227
    • (2003) J. Exp. Med. , vol.197 , pp. 1221-1227
    • Filipp, D.1
  • 45
    • 0036498797 scopus 로고    scopus 로고
    • Lipid raft heterogeneity in human peripheral blood T lymphoblasts: A mechanism for regulating the initiation of TCR signal transduction
    • A.E. Schade, and A.D. Levine Lipid raft heterogeneity in human peripheral blood T lymphoblasts: a mechanism for regulating the initiation of TCR signal transduction J. Immunol. 168 2002 2233 2239
    • (2002) J. Immunol. , vol.168 , pp. 2233-2239
    • Schade, A.E.1    Levine, A.D.2
  • 46
    • 0029933309 scopus 로고    scopus 로고
    • Altered peptide ligand-induced partial T cell activation: Molecular mechanisms and role in T cell biology
    • J. Sloan-Lancaster, and P.M. Allen Altered peptide ligand-induced partial T cell activation: molecular mechanisms and role in T cell biology Annu. Rev. Immunol. 14 1996 1 27
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 1-27
    • Sloan-Lancaster, J.1    Allen, P.M.2
  • 47
    • 0032545218 scopus 로고    scopus 로고
    • A receptor/cytoskeletal movement triggered by costimulation during T cell activation
    • C. Wulfing, and M.M. Davis A receptor/cytoskeletal movement triggered by costimulation during T cell activation Science 282 1998 2266 2269
    • (1998) Science , vol.282 , pp. 2266-2269
    • Wulfing, C.1    Davis, M.M.2
  • 48
    • 0025339511 scopus 로고
    • A cell culture model for T lymphocyte clonal anergy
    • R.H. Schwartz A cell culture model for T lymphocyte clonal anergy Science 248 1990 1349 1356
    • (1990) Science , vol.248 , pp. 1349-1356
    • Schwartz, R.H.1
  • 49
    • 12144290293 scopus 로고    scopus 로고
    • Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins
    • V. Heissmeyer Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins Nat. Immunol. 5 2004 255 265
    • (2004) Nat. Immunol. , vol.5 , pp. 255-265
    • Heissmeyer, V.1
  • 50
    • 0035901597 scopus 로고    scopus 로고
    • Fingerprints of anergic T cells
    • O. Lechner Fingerprints of anergic T cells Curr. Biol. 11 2001 587 595
    • (2001) Curr. Biol. , vol.11 , pp. 587-595
    • Lechner, O.1
  • 51
    • 0037077135 scopus 로고    scopus 로고
    • Transcriptional mechanisms underlying lymphocyte tolerance
    • F. Macian Transcriptional mechanisms underlying lymphocyte tolerance Cell 109 2002 719 731
    • (2002) Cell , vol.109 , pp. 719-731
    • MacIan, F.1
  • 52
    • 0034678656 scopus 로고    scopus 로고
    • Entry of B cell receptor into signaling domains is inhibited in tolerant B cells
    • B.C. Weintraub Entry of B cell receptor into signaling domains is inhibited in tolerant B cells J. Exp. Med. 191 2000 1443 1448
    • (2000) J. Exp. Med. , vol.191 , pp. 1443-1448
    • Weintraub, B.C.1
  • 53
    • 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
  • 54
    • 0035859925 scopus 로고    scopus 로고
    • Segregation of leading-edge and uropod components into specific lipid rafts during T cell polarization
    • C. Gomez-Mouton Segregation of leading-edge and uropod components into specific lipid rafts during T cell polarization Proc. Natl. Acad. Sci. U. S. A. 98 2001 9642 9647
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9642-9647
    • Gomez-Mouton, C.1
  • 55
    • 0025602953 scopus 로고
    • Interaction of cholesterol with various glycerophospholipids and sphingomyelin
    • M.B. Sankaram, and T.E. Thompson Interaction of cholesterol with various glycerophospholipids and sphingomyelin Biochemistry 29 1990 10670 10675
    • (1990) Biochemistry , vol.29 , pp. 10670-10675
    • Sankaram, M.B.1    Thompson, T.E.2
  • 56
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • R. Schroeder Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior Proc. Natl. Acad. Sci. U. S. A. 91 1994 12130 12134
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 12130-12134
    • Schroeder, R.1
  • 57
    • 0035114678 scopus 로고    scopus 로고
    • Lipid rafts reconstituted in model membranes
    • C. Dietrich Lipid rafts reconstituted in model membranes Biophys. J. 80 2001 1417 1428
    • (2001) Biophys. J. , vol.80 , pp. 1417-1428
    • Dietrich, C.1
  • 58
    • 0035845497 scopus 로고    scopus 로고
    • Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers
    • C. Dietrich Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers Proc. Natl. Acad. Sci. U. S. A. 98 2001 10642 10647
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10642-10647
    • Dietrich, C.1
  • 59
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • S. Munro Lipid rafts: elusive or illusive? Cell 115 2003 377 388
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 60
    • 0032820709 scopus 로고    scopus 로고
    • Mobility and cytoskeletal interactions of cell adhesion receptors
    • A. Kusumi Mobility and cytoskeletal interactions of cell adhesion receptors Curr. Opin. Cell Biol. 11 1999 582 590
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 582-590
    • Kusumi, A.1
  • 61
    • 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 Nat. Cell Biol. 6 2004 238 243
    • (2004) Nat. Cell Biol. , vol.6 , pp. 238-243
    • Glebov, O.O.1    Nichols, B.J.2
  • 62
    • 0035338444 scopus 로고    scopus 로고
    • Clustering of peptide-loaded MHC class I molecules for endoplasmic reticulum export imaged by fluorescence resonance energy transfer
    • T. Pentcheva, and M. Edidin Clustering of peptide-loaded MHC class I molecules for endoplasmic reticulum export imaged by fluorescence resonance energy transfer J. Immunol. 166 2001 6625 6632
    • (2001) J. Immunol. , vol.166 , pp. 6625-6632
    • Pentcheva, T.1    Edidin, M.2
  • 63
    • 0036224370 scopus 로고    scopus 로고
    • Inhibition of T cell receptor-coreceptor interactions by antagonist ligands visualized by live FRET imaging of the T-hybridoma immunological synapse
    • T. Zal Inhibition of T cell receptor-coreceptor interactions by antagonist ligands visualized by live FRET imaging of the T-hybridoma immunological synapse Immunity 16 2002 521 534
    • (2002) Immunity , vol.16 , pp. 521-534
    • Zal, T.1
  • 64
    • 0034714184 scopus 로고    scopus 로고
    • Differential clustering of CD4 and CD3ζ during T cell recognition
    • M.F. Krummel Differential clustering of CD4 and CD3ζ during T cell recognition Science 289 2000 1349 1352
    • (2000) Science , vol.289 , pp. 1349-1352
    • Krummel, M.F.1
  • 65
    • 0035380477 scopus 로고    scopus 로고
    • Dynamic recruitment of human CD2 into lipid rafts. Linkage to T cell signal transduction
    • H. Yang, and E.L. Reinherz Dynamic recruitment of human CD2 into lipid rafts. Linkage to T cell signal transduction J. Biol. Chem. 276 2001 18775 18785
    • (2001) J. Biol. Chem. , vol.276 , pp. 18775-18785
    • Yang, H.1    Reinherz, E.L.2
  • 66
    • 0032530369 scopus 로고    scopus 로고
    • Engagement of T cell receptor triggers its recruitment to low-density detergent-insoluble membrane domains
    • C. Montixi Engagement of T cell receptor triggers its recruitment to low-density detergent-insoluble membrane domains EMBO J. 17 1998 5334 5348
    • (1998) EMBO J. , vol.17 , pp. 5334-5348
    • Montixi, C.1
  • 67
    • 0032532949 scopus 로고    scopus 로고
    • Pp56Lck mediates TCRζ-chain binding to the microfilament cytoskeleton
    • M.M. Rozdzial pp56Lck mediates TCRζ-chain binding to the microfilament cytoskeleton J. Immunol. 161 1998 5491 5499
    • (1998) J. Immunol. , vol.161 , pp. 5491-5499
    • Rozdzial, M.M.1
  • 68
    • 3843149248 scopus 로고    scopus 로고
    • Translocation of CD28 to lipid rafts and costimulation of IL-2
    • A. Sadra Translocation of CD28 to lipid rafts and costimulation of IL-2 Proc. Natl. Acad. Sci. U. S. A. 101 2004 11422 11427
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 11422-11427
    • Sadra, A.1
  • 69
    • 0031962106 scopus 로고    scopus 로고
    • Growth factor receptor-bound protein 2 SH2/SH3 domain binding to CD28 and its role in co-signaling
    • H.H. Kim Growth factor receptor-bound protein 2 SH2/SH3 domain binding to CD28 and its role in co-signaling J. Biol. Chem. 273 1998 296 301
    • (1998) J. Biol. Chem. , vol.273 , pp. 296-301
    • Kim, H.H.1
  • 70
    • 0032525106 scopus 로고    scopus 로고
    • CD44 selectively associates with active Src family protein tyrosine kinases Lck and Fyn in glycosphingolipid-rich plasma membrane domains of human peripheral blood lymphocytes
    • S. Ilangumaran CD44 selectively associates with active Src family protein tyrosine kinases Lck and Fyn in glycosphingolipid-rich plasma membrane domains of human peripheral blood lymphocytes Blood 91 1998 3901 3908
    • (1998) Blood , vol.91 , pp. 3901-3908
    • Ilangumaran, S.1
  • 71
    • 0032559637 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2
    • S. Yonemura Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2 J. Cell Biol. 140 1998 885 895
    • (1998) J. Cell Biol. , vol.140 , pp. 885-895
    • Yonemura, S.1
  • 72
    • 0037077718 scopus 로고    scopus 로고
    • E-selectin and ICAM-1 are incorporated into detergent-insoluble membrane domains following clustering in endothelial cells
    • R.W. Tilghman, and R.L. Hoover E-selectin and ICAM-1 are incorporated into detergent-insoluble membrane domains following clustering in endothelial cells FEBS Lett. 525 2002 83 87
    • (2002) FEBS Lett. , vol.525 , pp. 83-87
    • Tilghman, R.W.1    Hoover, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.