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Volumn 112, Issue 8, 2017, Pages 1703-1713

Live-Cell Super-resolution Reveals F-Actin and Plasma Membrane Dynamics at the T Cell Synapse

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTININ; TUBULIN MODULATOR;

EID: 85018630922     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2017.01.038     Document Type: Article
Times cited : (42)

References (50)
  • 1
    • 27544441784 scopus 로고    scopus 로고
    • Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling
    • 1 Campi, G., Varma, R., Dustin, M.L., Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling. J. Exp. Med. 202 (2005), 1031–1036.
    • (2005) J. Exp. Med. , vol.202 , pp. 1031-1036
    • Campi, G.1    Varma, R.2    Dustin, M.L.3
  • 2
    • 84864139002 scopus 로고    scopus 로고
    • Integration of the movement of signaling microclusters with cellular motility in immunological synapses
    • 2 Beemiller, P., Jacobelli, J., Krummel, M.F., Integration of the movement of signaling microclusters with cellular motility in immunological synapses. Nat. Immunol. 13 (2012), 787–795.
    • (2012) Nat. Immunol. , vol.13 , pp. 787-795
    • Beemiller, P.1    Jacobelli, J.2    Krummel, M.F.3
  • 3
    • 84863992208 scopus 로고    scopus 로고
    • F-actin polymerization and retrograde flow drive sustained PLCγ1 signaling during T cell activation
    • 3 Babich, A., Li, S., et al., Burkhardt, J.K., F-actin polymerization and retrograde flow drive sustained PLCγ1 signaling during T cell activation. J. Cell Biol. 197 (2012), 775–787.
    • (2012) J. Cell Biol. , vol.197 , pp. 775-787
    • Babich, A.1    Li, S.2    Burkhardt, J.K.3
  • 4
    • 84863229197 scopus 로고    scopus 로고
    • Actin retrograde flow and actomyosin II arc contraction drive receptor cluster dynamics at the immunological synapse in Jurkat T cells
    • 4 Yi, J., Wu, X.S., et al., Hammer, J.A. 3rd, Actin retrograde flow and actomyosin II arc contraction drive receptor cluster dynamics at the immunological synapse in Jurkat T cells. Mol. Biol. Cell 23 (2012), 834–852.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 834-852
    • Yi, J.1    Wu, X.S.2    Hammer, J.A.3
  • 5
    • 33746011209 scopus 로고    scopus 로고
    • T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster
    • 5 Varma, R., Campi, G., et al., Dustin, M.L., T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster. Immunity 25 (2006), 117–127.
    • (2006) Immunity , vol.25 , pp. 117-127
    • Varma, R.1    Campi, G.2    Dustin, M.L.3
  • 6
    • 84929664587 scopus 로고    scopus 로고
    • Actin depletion initiates events leading to granule secretion at the immunological synapse
    • 6 Ritter, A.T., Asano, Y., et al., Griffiths, G.M., Actin depletion initiates events leading to granule secretion at the immunological synapse. Immunity 42 (2015), 864–876.
    • (2015) Immunity , vol.42 , pp. 864-876
    • Ritter, A.T.1    Asano, Y.2    Griffiths, G.M.3
  • 7
    • 80053325995 scopus 로고    scopus 로고
    • Remodelling of cortical actin where lytic granules dock at natural killer cell immune synapses revealed by super-resolution microscopy
    • 7 Brown, A.C.N., Oddos, S., et al., Davis, D.M., Remodelling of cortical actin where lytic granules dock at natural killer cell immune synapses revealed by super-resolution microscopy. PLoS Biol., 9, 2011, e1001152.
    • (2011) PLoS Biol. , vol.9 , pp. e1001152
    • Brown, A.C.N.1    Oddos, S.2    Davis, D.M.3
  • 8
    • 80053321288 scopus 로고    scopus 로고
    • Natural killer cell lytic granule secretion occurs through a pervasive actin network at the immune synapse
    • 8 Rak, G.D., Mace, E.M., et al., Orange, J.S., Natural killer cell lytic granule secretion occurs through a pervasive actin network at the immune synapse. PLoS Biol., 9, 2011, e1001151.
    • (2011) PLoS Biol. , vol.9 , pp. e1001151
    • Rak, G.D.1    Mace, E.M.2    Orange, J.S.3
  • 9
    • 84899866481 scopus 로고    scopus 로고
    • Lytic immune synapse function requires filamentous actin deconstruction by Coronin 1A
    • 9 Mace, E.M., Orange, J.S., Lytic immune synapse function requires filamentous actin deconstruction by Coronin 1A. Proc. Natl. Acad. Sci. USA 111 (2014), 6708–6713.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 6708-6713
    • Mace, E.M.1    Orange, J.S.2
  • 10
    • 9644284452 scopus 로고    scopus 로고
    • Single-molecule tracking of membrane molecules: plasma membrane compartmentalization and dynamic assembly of raft-philic signaling molecules
    • 10 Kusumi, A., Ike, H., et al., Fujiwara, T., Single-molecule tracking of membrane molecules: plasma membrane compartmentalization and dynamic assembly of raft-philic signaling molecules. Semin. Immunol. 17 (2005), 3–21.
    • (2005) Semin. Immunol. , vol.17 , pp. 3-21
    • Kusumi, A.1    Ike, H.2    Fujiwara, T.3
  • 11
    • 84861991991 scopus 로고    scopus 로고
    • Active remodeling of cortical actin regulates spatiotemporal organization of cell surface molecules
    • 11 Gowrishankar, K., Ghosh, S., et al., Rao, M., Active remodeling of cortical actin regulates spatiotemporal organization of cell surface molecules. Cell 149 (2012), 1353–1367.
    • (2012) Cell , vol.149 , pp. 1353-1367
    • Gowrishankar, K.1    Ghosh, S.2    Rao, M.3
  • 12
    • 37549035926 scopus 로고    scopus 로고
    • Clustering of membrane raft proteins by the actin cytoskeleton
    • 12 Chichili, G.R., Rodgers, W., Clustering of membrane raft proteins by the actin cytoskeleton. J. Biol. Chem. 282 (2007), 36682–36691.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36682-36691
    • Chichili, G.R.1    Rodgers, W.2
  • 13
    • 34247861082 scopus 로고    scopus 로고
    • Plasma membrane-associated proteins are clustered into islands attached to the cytoskeleton
    • 13 Lillemeier, B.F., Pfeiffer, J.R., et al., Davis, M.M., Plasma membrane-associated proteins are clustered into islands attached to the cytoskeleton. Proc. Natl. Acad. Sci. USA 103 (2006), 18992–18997.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 18992-18997
    • Lillemeier, B.F.1    Pfeiffer, J.R.2    Davis, M.M.3
  • 14
    • 84875891990 scopus 로고    scopus 로고
    • Lateral membrane diffusion modulated by a minimal actin cortex
    • 14 Heinemann, F., Vogel, S.K., Schwille, P., Lateral membrane diffusion modulated by a minimal actin cortex. Biophys. J. 104 (2013), 1465–1475.
    • (2013) Biophys. J. , vol.104 , pp. 1465-1475
    • Heinemann, F.1    Vogel, S.K.2    Schwille, P.3
  • 15
    • 84894263203 scopus 로고    scopus 로고
    • Cross talk between CD3 and CD28 is spatially modulated by protein lateral mobility
    • 15 Bashour, K.T., Tsai, J., et al., Kam, L.C., Cross talk between CD3 and CD28 is spatially modulated by protein lateral mobility. Mol. Cell. Biol. 34 (2014), 955–964.
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 955-964
    • Bashour, K.T.1    Tsai, J.2    Kam, L.C.3
  • 16
    • 84924668103 scopus 로고    scopus 로고
    • The dendritic cell cytoskeleton promotes T cell adhesion and activation by constraining ICAM-1 mobility
    • 16 Comrie, W.A., Li, S., et al., Burkhardt, J.K., The dendritic cell cytoskeleton promotes T cell adhesion and activation by constraining ICAM-1 mobility. J. Cell Biol. 208 (2015), 457–473.
    • (2015) J. Cell Biol. , vol.208 , pp. 457-473
    • Comrie, W.A.1    Li, S.2    Burkhardt, J.K.3
  • 17
    • 77955623486 scopus 로고    scopus 로고
    • Altered actin centripetal retrograde flow in physically restricted immunological synapses
    • 17 Yu, C.H., Wu, H.J., et al., Groves, J.T., Altered actin centripetal retrograde flow in physically restricted immunological synapses. PLoS One, 5, 2010, e11878.
    • (2010) PLoS One , vol.5 , pp. e11878
    • Yu, C.H.1    Wu, H.J.2    Groves, J.T.3
  • 18
    • 35548942611 scopus 로고    scopus 로고
    • Tether and trap: regulation of membrane-raft dynamics by actin-binding proteins
    • 18 Viola, A., Gupta, N., Tether and trap: regulation of membrane-raft dynamics by actin-binding proteins. Nat. Rev. Immunol. 7 (2007), 889–896.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 889-896
    • Viola, A.1    Gupta, N.2
  • 19
    • 84872162032 scopus 로고    scopus 로고
    • Actin filaments attachment at the plasma membrane in live cells cause the formation of ordered lipid domains
    • 19 Dinic, J., Ashrafzadeh, P., Parmryd, I., Actin filaments attachment at the plasma membrane in live cells cause the formation of ordered lipid domains. Biochim. Biophys. Acta 1828 (2013), 1102–1111.
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 1102-1111
    • Dinic, J.1    Ashrafzadeh, P.2    Parmryd, I.3
  • 20
    • 79959655729 scopus 로고    scopus 로고
    • Minimal model of plasma membrane heterogeneity requires coupling cortical actin to criticality
    • 20 Machta, B.B., Papanikolaou, S., et al., Veatch, S.L., Minimal model of plasma membrane heterogeneity requires coupling cortical actin to criticality. Biophys. J. 100 (2011), 1668–1677.
    • (2011) Biophys. J. , vol.100 , pp. 1668-1677
    • Machta, B.B.1    Papanikolaou, S.2    Veatch, S.L.3
  • 21
    • 77954481265 scopus 로고    scopus 로고
    • High plasma membrane lipid order imaged at the immunological synapse periphery in live T cells
    • 21 Owen, D.M., Oddos, S., et al., Cebecauer, M., High plasma membrane lipid order imaged at the immunological synapse periphery in live T cells. Mol. Membr. Biol. 27 (2010), 178–189.
    • (2010) Mol. Membr. Biol. , vol.27 , pp. 178-189
    • Owen, D.M.1    Oddos, S.2    Cebecauer, M.3
  • 22
    • 84863798003 scopus 로고    scopus 로고
    • Cytoskeletal modulation of lipid interactions regulates Lck kinase activity
    • 22 Chichili, G.R., Cail, R.C., Rodgers, W., Cytoskeletal modulation of lipid interactions regulates Lck kinase activity. J. Biol. Chem. 287 (2012), 24186–24194.
    • (2012) J. Biol. Chem. , vol.287 , pp. 24186-24194
    • Chichili, G.R.1    Cail, R.C.2    Rodgers, W.3
  • 23
    • 67650762824 scopus 로고    scopus 로고
    • Super-resolution fluorescence microscopy
    • 23 Huang, B., Bates, M., Zhuang, X., Super-resolution fluorescence microscopy. Annu. Rev. Biochem. 78 (2009), 993–1016.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 993-1016
    • Huang, B.1    Bates, M.2    Zhuang, X.3
  • 24
    • 74049157769 scopus 로고    scopus 로고
    • TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation
    • 24 Lillemeier, B.F., Mörtelmaier, M.A., et al., Davis, M.M., TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation. Nat. Immunol. 11 (2010), 90–96.
    • (2010) Nat. Immunol. , vol.11 , pp. 90-96
    • Lillemeier, B.F.1    Mörtelmaier, M.A.2    Davis, M.M.3
  • 25
    • 79959373064 scopus 로고    scopus 로고
    • Pre-existing clusters of the adaptor Lat do not participate in early T cell signaling events
    • 25 Williamson, D.J., Owen, D.M., et al., Gaus, K., Pre-existing clusters of the adaptor Lat do not participate in early T cell signaling events. Nat. Immunol. 12 (2011), 655–662.
    • (2011) Nat. Immunol. , vol.12 , pp. 655-662
    • Williamson, D.J.1    Owen, D.M.2    Gaus, K.3
  • 26
    • 17844395707 scopus 로고    scopus 로고
    • Spatiotemporal image correlation spectroscopy (STICS) theory, verification, and application to protein velocity mapping in living CHO cells
    • 26 Hebert, B., Costantino, S., Wiseman, P.W., Spatiotemporal image correlation spectroscopy (STICS) theory, verification, and application to protein velocity mapping in living CHO cells. Biophys. J. 88 (2005), 3601–3614.
    • (2005) Biophys. J. , vol.88 , pp. 3601-3614
    • Hebert, B.1    Costantino, S.2    Wiseman, P.W.3
  • 27
    • 84908606332 scopus 로고    scopus 로고
    • Molecular flow quantified beyond the diffraction limit by spatiotemporal image correlation of structured illumination microscopy data
    • 27 Ashdown, G.W., Cope, A., et al., Owen, D.M., Molecular flow quantified beyond the diffraction limit by spatiotemporal image correlation of structured illumination microscopy data. Biophys. J. 107 (2014), L21–L23.
    • (2014) Biophys. J. , vol.107 , pp. L21-L23
    • Ashdown, G.W.1    Cope, A.2    Owen, D.M.3
  • 28
    • 84952803273 scopus 로고    scopus 로고
    • Cortical actin flow in T cells quantified by spatio-temporal image correlation spectroscopy of structured illumination microscopy data
    • 28 Ashdown, G., Pandžić, E., et al., Owen, D., Cortical actin flow in T cells quantified by spatio-temporal image correlation spectroscopy of structured illumination microscopy data. J. Vis. Exp., 106, 2015, e53749.
    • (2015) J. Vis. Exp. , vol.106 , pp. e53749
    • Ashdown, G.1    Pandžić, E.2    Owen, D.3
  • 29
    • 84863632247 scopus 로고    scopus 로고
    • EWI-2 association with α-actinin regulates T cell immune synapses and HIV viral infection
    • 29 Gordón-Alonso, M., Sala-Valdés, M., et al., Yáñez-Mó, M., EWI-2 association with α-actinin regulates T cell immune synapses and HIV viral infection. J. Immunol. 189 (2012), 689–700.
    • (2012) J. Immunol. , vol.189 , pp. 689-700
    • Gordón-Alonso, M.1    Sala-Valdés, M.2    Yáñez-Mó, M.3
  • 30
    • 13844253573 scopus 로고    scopus 로고
    • Identification of the β1-integrin binding site on α-actinin by cryoelectron microscopy
    • 30 Kelly, D.F., Taylor, K.A., Identification of the β1-integrin binding site on α-actinin by cryoelectron microscopy. J. Struct. Biol. 149 (2005), 290–302.
    • (2005) J. Struct. Biol. , vol.149 , pp. 290-302
    • Kelly, D.F.1    Taylor, K.A.2
  • 31
    • 0028358979 scopus 로고
    • Identification of the vinculin-binding site in the cytoskeletal protein α-actinin
    • 31 McGregor, A., Blanchard, A.D., et al., Critchley, D.R., Identification of the vinculin-binding site in the cytoskeletal protein α-actinin. Biochem. J. 301 (1994), 225–233.
    • (1994) Biochem. J. , vol.301 , pp. 225-233
    • McGregor, A.1    Blanchard, A.D.2    Critchley, D.R.3
  • 32
    • 33947306552 scopus 로고    scopus 로고
    • Novel structures for α-actinin:F-actin interactions and their implications for actin-membrane attachment and tension sensing in the cytoskeleton
    • 32 Hampton, C.M., Taylor, D.W., Taylor, K.A., Novel structures for α-actinin:F-actin interactions and their implications for actin-membrane attachment and tension sensing in the cytoskeleton. J. Mol. Biol. 368 (2007), 92–104.
    • (2007) J. Mol. Biol. , vol.368 , pp. 92-104
    • Hampton, C.M.1    Taylor, D.W.2    Taylor, K.A.3
  • 34
    • 84938415188 scopus 로고    scopus 로고
    • Multitarget super-resolution microscopy with high-density labeling by exchangeable probes
    • 34 Kiuchi, T., Higuchi, M., et al., Watanabe, N., Multitarget super-resolution microscopy with high-density labeling by exchangeable probes. Nat. Methods 12 (2015), 743–746.
    • (2015) Nat. Methods , vol.12 , pp. 743-746
    • Kiuchi, T.1    Higuchi, M.2    Watanabe, N.3
  • 35
    • 0036231415 scopus 로고    scopus 로고
    • Precise nanometer localization analysis for individual fluorescent probes
    • 35 Thompson, R.E., Larson, D.R., Webb, W.W., Precise nanometer localization analysis for individual fluorescent probes. Biophys. J. 82 (2002), 2775–2783.
    • (2002) Biophys. J. , vol.82 , pp. 2775-2783
    • Thompson, R.E.1    Larson, D.R.2    Webb, W.W.3
  • 36
    • 12144265571 scopus 로고    scopus 로고
    • Blebbistatin, a myosin II inhibitor, is photoinactivated by blue light
    • 36 Sakamoto, T., Limouze, J., et al., Sellers, J.R., Blebbistatin, a myosin II inhibitor, is photoinactivated by blue light. Biochemistry 44 (2005), 584–588.
    • (2005) Biochemistry , vol.44 , pp. 584-588
    • Sakamoto, T.1    Limouze, J.2    Sellers, J.R.3
  • 37
    • 84859475063 scopus 로고    scopus 로고
    • Time-lapse two-color 3D imaging of live cells with doubled resolution using structured illumination
    • 37 Fiolka, R., Shao, L., et al., Gustafsson, M.G.L., Time-lapse two-color 3D imaging of live cells with doubled resolution using structured illumination. Proc. Natl. Acad. Sci. USA 109 (2012), 5311–5315.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 5311-5315
    • Fiolka, R.1    Shao, L.2    Gustafsson, M.G.L.3
  • 38
    • 42149143016 scopus 로고    scopus 로고
    • Three-dimensional resolution doubling in wide-field fluorescence microscopy by structured illumination
    • 38 Gustafsson, M.G.L., Shao, L., et al., Sedat, J.W., Three-dimensional resolution doubling in wide-field fluorescence microscopy by structured illumination. Biophys. J. 94 (2008), 4957–4970.
    • (2008) Biophys. J. , vol.94 , pp. 4957-4970
    • Gustafsson, M.G.L.1    Shao, L.2    Sedat, J.W.3
  • 39
    • 48249088456 scopus 로고    scopus 로고
    • Functional implications of plasma membrane condensation for T cell activation
    • 39 Rentero, C., Zech, T., et al., Gaus, K., Functional implications of plasma membrane condensation for T cell activation. PLoS One, 3, 2008, e2262.
    • (2008) PLoS One , vol.3 , pp. e2262
    • Rentero, C.1    Zech, T.2    Gaus, K.3
  • 40
    • 84995893128 scopus 로고    scopus 로고
    • Formin-generated actomyosin arcs propel T cell receptor microcluster movement at the immune synapse
    • 40 Murugesan, S., Hong, J., et al., Hammer, J.A., Formin-generated actomyosin arcs propel T cell receptor microcluster movement at the immune synapse. J. Cell Biol. 215 (2016), 383–399.
    • (2016) J. Cell Biol. , vol.215 , pp. 383-399
    • Murugesan, S.1    Hong, J.2    Hammer, J.A.3
  • 41
    • 84867639223 scopus 로고    scopus 로고
    • STICCS reveals matrix-dependent adhesion slipping and gripping in migrating cells
    • 41 Toplak, T., Pandzic, E., et al., Wiseman, P.W., STICCS reveals matrix-dependent adhesion slipping and gripping in migrating cells. Biophys. J. 103 (2012), 1672–1682.
    • (2012) Biophys. J. , vol.103 , pp. 1672-1682
    • Toplak, T.1    Pandzic, E.2    Wiseman, P.W.3
  • 42
    • 84928392356 scopus 로고    scopus 로고
    • Transbilayer lipid interactions mediate nanoclustering of lipid-anchored proteins
    • 42 Raghupathy, R., Anilkumar, A.A., et al., Mayor, S., Transbilayer lipid interactions mediate nanoclustering of lipid-anchored proteins. Cell 161 (2015), 581–594.
    • (2015) Cell , vol.161 , pp. 581-594
    • Raghupathy, R.1    Anilkumar, A.A.2    Mayor, S.3
  • 43
    • 33344465758 scopus 로고    scopus 로고
    • Structure of the α-actinin-vinculin head domain complex determined by cryo-electron microscopy
    • 43 Kelly, D.F., Taylor, D.W., et al., Taylor, K.A., Structure of the α-actinin-vinculin head domain complex determined by cryo-electron microscopy. J. Mol. Biol. 357 (2006), 562–573.
    • (2006) J. Mol. Biol. , vol.357 , pp. 562-573
    • Kelly, D.F.1    Taylor, D.W.2    Taylor, K.A.3
  • 44
    • 58849107192 scopus 로고    scopus 로고
    • Live cell linear dichroism imaging reveals extensive membrane ruffling within the docking structure of natural killer cell immune synapses
    • 44 Benninger, R.K.P., Vanherberghen, B., et al., Onfelt, B., Live cell linear dichroism imaging reveals extensive membrane ruffling within the docking structure of natural killer cell immune synapses. Biophys. J. 96 (2009), L13–L15.
    • (2009) Biophys. J. , vol.96 , pp. L13-L15
    • Benninger, R.K.P.1    Vanherberghen, B.2    Onfelt, B.3
  • 45
    • 78650603500 scopus 로고    scopus 로고
    • Imaging techniques for assaying lymphocyte activation in action
    • 45 Balagopalan, L., Sherman, E., et al., Samelson, L.E., Imaging techniques for assaying lymphocyte activation in action. Nat. Rev. Immunol. 11 (2011), 21–33.
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 21-33
    • Balagopalan, L.1    Sherman, E.2    Samelson, L.E.3
  • 47
    • 0034232037 scopus 로고    scopus 로고
    • The immunological synapse and the actin cytoskeleton: molecular hardware for T cell signaling
    • 47 Dustin, M.L., Cooper, J.A., The immunological synapse and the actin cytoskeleton: molecular hardware for T cell signaling. Nat Immunol. 1 (2000), 23–29.
    • (2000) Nat Immunol. , vol.1 , pp. 23-29
    • Dustin, M.L.1    Cooper, J.A.2
  • 48
    • 0037244777 scopus 로고    scopus 로고
    • Actin cytoskeletal dynamics in T lymphocyte activation and migration
    • 48 Samstag, Y., Eibert, S.M., et al., Wabnitz, G.H., Actin cytoskeletal dynamics in T lymphocyte activation and migration. J. Leukoc. Biol. 73 (2003), 30–48.
    • (2003) J. Leukoc. Biol. , vol.73 , pp. 30-48
    • Samstag, Y.1    Eibert, S.M.2    Wabnitz, G.H.3
  • 49
    • 0025153539 scopus 로고
    • Cell migration does not produce membrane flow
    • 49 Kucik, D.F., Elson, E.L., Sheetz, M.P., Cell migration does not produce membrane flow. J. Cell Biol. 111 (1990), 1617–1622.
    • (1990) J. Cell Biol. , vol.111 , pp. 1617-1622
    • Kucik, D.F.1    Elson, E.L.2    Sheetz, M.P.3
  • 50
    • 30044441433 scopus 로고    scopus 로고
    • Newly generated T cell receptor microclusters initiate and sustain T cell activation by recruitment of Zap70 and SLP-76
    • 50 Yokosuka, T., Sakata-Sogawa, K., et al., Saito, T., Newly generated T cell receptor microclusters initiate and sustain T cell activation by recruitment of Zap70 and SLP-76. Nat. Immunol. 6 (2005), 1253–1262.
    • (2005) Nat. Immunol. , vol.6 , pp. 1253-1262
    • Yokosuka, T.1    Sakata-Sogawa, K.2    Saito, T.3


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