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Volumn 164, Issue 1-2, 2016, Pages 128-140

Integrins Form an Expanding Diffusional Barrier that Coordinates Phagocytosis

Author keywords

[No Author keywords available]

Indexed keywords

CD45 ANTIGEN; F ACTIN; FC RECEPTOR; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G; INTEGRIN; PHOSPHATASE; VINCULIN; ACTIN; RECEPTOR LIKE PROTEIN TYROSINE PHOSPHATASE;

EID: 84954233588     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2015.11.048     Document Type: Article
Times cited : (151)

References (37)
  • 1
    • 0030459125 scopus 로고    scopus 로고
    • A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages
    • N. Araki, M.T. Johnson, and J.A. Swanson A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages J. Cell Biol. 135 1996 1249 1260
    • (1996) J. Cell Biol. , vol.135 , pp. 1249-1260
    • Araki, N.1    Johnson, M.T.2    Swanson, J.A.3
  • 2
    • 0035942781 scopus 로고    scopus 로고
    • B cells acquire antigen from target cells after synapse formation
    • F.D. Batista, D. Iber, and M.S. Neuberger B cells acquire antigen from target cells after synapse formation Nature 411 2001 489 494
    • (2001) Nature , vol.411 , pp. 489-494
    • Batista, F.D.1    Iber, D.2    Neuberger, M.S.3
  • 4
    • 56649109834 scopus 로고    scopus 로고
    • Fibrinogen binds IgG antibody and enhances IgG-mediated phagocytosis
    • T.K. Boehm, and E. DeNardin Fibrinogen binds IgG antibody and enhances IgG-mediated phagocytosis Hum. Antibodies 17 2008 45 56
    • (2008) Hum. Antibodies , vol.17 , pp. 45-56
    • Boehm, T.K.1    DeNardin, E.2
  • 5
    • 78649649128 scopus 로고    scopus 로고
    • Class i and class III phosphoinositide 3-kinases are required for actin polymerization that propels phagosomes
    • M. Bohdanowicz, G. Cosío, J.M. Backer, and S. Grinstein Class I and class III phosphoinositide 3-kinases are required for actin polymerization that propels phagosomes J. Cell Biol. 191 2010 999 1012
    • (2010) J. Cell Biol. , vol.191 , pp. 999-1012
    • Bohdanowicz, M.1    Cosío, G.2    Backer, J.M.3    Grinstein, S.4
  • 7
    • 84880407025 scopus 로고    scopus 로고
    • The large ectodomains of CD45 and CD148 regulate their segregation from and inhibition of ligated T-cell receptor
    • S.P. Cordoba, K. Choudhuri, H. Zhang, M. Bridge, A.B. Basat, M.L. Dustin, and P.A. van der Merwe The large ectodomains of CD45 and CD148 regulate their segregation from and inhibition of ligated T-cell receptor Blood 121 2013 4295 4302
    • (2013) Blood , vol.121 , pp. 4295-4302
    • Cordoba, S.P.1    Choudhuri, K.2    Zhang, H.3    Bridge, M.4    Basat, A.B.5    Dustin, M.L.6    Van Der Merwe, P.A.7
  • 8
    • 0033555931 scopus 로고    scopus 로고
    • A requirement for phosphatidylinositol 3-kinase in pseudopod extension
    • D. Cox, C.C. Tseng, G. Bjekic, and S. Greenberg A requirement for phosphatidylinositol 3-kinase in pseudopod extension J. Biol. Chem. 274 1999 1240 1247
    • (1999) J. Biol. Chem. , vol.274 , pp. 1240-1247
    • Cox, D.1    Tseng, C.C.2    Bjekic, G.3    Greenberg, S.4
  • 9
    • 33746114879 scopus 로고    scopus 로고
    • The kinetic-segregation model: TCR triggering and beyond
    • S.J. Davis, and P.A. van der Merwe The kinetic-segregation model: TCR triggering and beyond Nat. Immunol. 7 2006 803 809
    • (2006) Nat. Immunol. , vol.7 , pp. 803-809
    • Davis, S.J.1    Van Der Merwe, P.A.2
  • 12
    • 80053111149 scopus 로고    scopus 로고
    • Regulating Rap small G-proteins in time and space
    • M. Gloerich, and J.L. Bos Regulating Rap small G-proteins in time and space Trends Cell Biol. 21 2011 615 623
    • (2011) Trends Cell Biol. , vol.21 , pp. 615-623
    • Gloerich, M.1    Bos, J.L.2
  • 13
    • 80052847053 scopus 로고    scopus 로고
    • Evidence for a fence that impedes the diffusion of phosphatidylinositol 4,5-bisphosphate out of the forming phagosomes of macrophages
    • U. Golebiewska, J.G. Kay, T. Masters, S. Grinstein, W. Im, R.W. Pastor, S. Scarlata, and S. McLaughlin Evidence for a fence that impedes the diffusion of phosphatidylinositol 4,5-bisphosphate out of the forming phagosomes of macrophages Mol. Biol. Cell 22 2011 3498 3507
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3498-3507
    • Golebiewska, U.1    Kay, J.G.2    Masters, T.3    Grinstein, S.4    Im, W.5    Pastor, R.W.6    Scarlata, S.7    McLaughlin, S.8
  • 16
    • 0016816227 scopus 로고
    • Studies on the mechanism of phagocytosis. I. Requirements for circumferential attachment of particle-bound ligands to specific receptors on the macrophage plasma membrane
    • F.M. Griffin Jr., J.A. Griffin, J.E. Leider, and S.C. Silverstein Studies on the mechanism of phagocytosis. I. Requirements for circumferential attachment of particle-bound ligands to specific receptors on the macrophage plasma membrane J. Exp. Med. 142 1975 1263 1282
    • (1975) J. Exp. Med. , vol.142 , pp. 1263-1282
    • Griffin, F.M.1    Griffin, J.A.2    Leider, J.E.3    Silverstein, S.C.4
  • 17
    • 61849136595 scopus 로고    scopus 로고
    • CD45, CD148, and Lyp/Pep: Critical phosphatases regulating Src family kinase signaling networks in immune cells
    • M.L. Hermiston, J. Zikherman, and J.W. Zhu CD45, CD148, and Lyp/Pep: critical phosphatases regulating Src family kinase signaling networks in immune cells Immunol. Rev. 228 2009 288 311
    • (2009) Immunol. Rev. , vol.228 , pp. 288-311
    • Hermiston, M.L.1    Zikherman, J.2    Zhu, J.W.3
  • 18
    • 84863482471 scopus 로고    scopus 로고
    • Biophysical mechanism of T-cell receptor triggering in a reconstituted system
    • J.R. James, and R.D. Vale Biophysical mechanism of T-cell receptor triggering in a reconstituted system Nature 487 2012 64 69
    • (2012) Nature , vol.487 , pp. 64-69
    • James, J.R.1    Vale, R.D.2
  • 20
  • 21
    • 0034730188 scopus 로고    scopus 로고
    • A supramolecular basis for CD45 tyrosine phosphatase regulation in sustained T cell activation
    • K.G. Johnson, S.K. Bromley, M.L. Dustin, and M.L. Thomas A supramolecular basis for CD45 tyrosine phosphatase regulation in sustained T cell activation Proc. Natl. Acad. Sci. USA 97 2000 10138 10143
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10138-10143
    • Johnson, K.G.1    Bromley, S.K.2    Dustin, M.L.3    Thomas, M.L.4
  • 22
    • 0032562605 scopus 로고    scopus 로고
    • Two signaling mechanisms for activation of alphaM β2 avidity in polymorphonuclear neutrophils
    • S.L. Jones, U.G. Knaus, G.M. Bokoch, and E.J. Brown Two signaling mechanisms for activation of alphaM β2 avidity in polymorphonuclear neutrophils J. Biol. Chem. 273 1998 10556 10566
    • (1998) J. Biol. Chem. , vol.273 , pp. 10556-10566
    • Jones, S.L.1    Knaus, U.G.2    Bokoch, G.M.3    Brown, E.J.4
  • 24
    • 0035954430 scopus 로고    scopus 로고
    • Restricted accumulation of phosphatidylinositol 3-kinase products in a plasmalemmal subdomain during Fc gamma receptor-mediated phagocytosis
    • J.G. Marshall, J.W. Booth, V. Stambolic, T. Mak, T. Balla, A.D. Schreiber, T. Meyer, and S. Grinstein Restricted accumulation of phosphatidylinositol 3-kinase products in a plasmalemmal subdomain during Fc gamma receptor-mediated phagocytosis J. Cell Biol. 153 2001 1369 1380
    • (2001) J. Cell Biol. , vol.153 , pp. 1369-1380
    • Marshall, J.G.1    Booth, J.W.2    Stambolic, V.3    Mak, T.4    Balla, T.5    Schreiber, A.D.6    Meyer, T.7    Grinstein, S.8
  • 25
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • C.R. Monks, B.A. Freiberg, H. Kupfer, N. Sciaky, and A. Kupfer 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    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 27
    • 79961004062 scopus 로고    scopus 로고
    • CalDAG-GEFI deficiency protects mice in a novel model of Fcγ RIIA-mediated thrombosis and thrombocytopenia
    • M. Stolla, L. Stefanini, P. André, T.D. Ouellette, M.P. Reilly, S.E. McKenzie, and W. Bergmeier CalDAG-GEFI deficiency protects mice in a novel model of Fcγ RIIA-mediated thrombosis and thrombocytopenia Blood 118 2011 1113 1120
    • (2011) Blood , vol.118 , pp. 1113-1120
    • Stolla, M.1    Stefanini, L.2    André, P.3    Ouellette, T.D.4    Reilly, M.P.5    McKenzie, S.E.6    Bergmeier, W.7
  • 28
    • 56249088313 scopus 로고    scopus 로고
    • Focal adhesion proteins connect IgE receptors to the cytoskeleton as revealed by micropatterned ligand arrays
    • A.J. Torres, L. Vasudevan, D. Holowka, and B.A. Baird Focal adhesion proteins connect IgE receptors to the cytoskeleton as revealed by micropatterned ligand arrays Proc. Natl. Acad. Sci. USA 105 2008 17238 17244
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 17238-17244
    • Torres, A.J.1    Vasudevan, L.2    Holowka, D.3    Baird, B.A.4
  • 29
    • 78650599246 scopus 로고    scopus 로고
    • Mechanisms for T cell receptor triggering
    • P.A. van der Merwe, and O. Dushek Mechanisms for T cell receptor triggering Nat. Rev. Immunol. 11 2011 47 55
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 47-55
    • Van Der Merwe, P.A.1    Dushek, O.2
  • 30
    • 33746011209 scopus 로고    scopus 로고
    • T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster
    • R. Varma, G. Campi, T. Yokosuka, T. Saito, and M.L. Dustin 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    Yokosuka, T.3    Saito, T.4    Dustin, M.L.5
  • 31
    • 0037073752 scopus 로고    scopus 로고
    • A molecular basis for integrin alphaMbeta 2 ligand binding promiscuity
    • V.P. Yakubenko, V.K. Lishko, S.C. Lam, and T.P. Ugarova A molecular basis for integrin alphaMbeta 2 ligand binding promiscuity J. Biol. Chem. 277 2002 48635 48642
    • (2002) J. Biol. Chem. , vol.277 , pp. 48635-48642
    • Yakubenko, V.P.1    Lishko, V.K.2    Lam, S.C.3    Ugarova, T.P.4
  • 32
    • 84866630364 scopus 로고    scopus 로고
    • Myosin II-dependent exclusion of CD45 from the site of Fcγ receptor activation during phagocytosis
    • S. Yamauchi, K. Kawauchi, and Y. Sawada Myosin II-dependent exclusion of CD45 from the site of Fcγ receptor activation during phagocytosis FEBS Lett. 586 2012 3229 3235
    • (2012) FEBS Lett. , vol.586 , pp. 3229-3235
    • Yamauchi, S.1    Kawauchi, K.2    Sawada, Y.3
  • 34
    • 70350349921 scopus 로고    scopus 로고
    • Sequential signaling in plasma-membrane domains during macropinosome formation in macrophages
    • S. Yoshida, A.D. Hoppe, N. Araki, and J.A. Swanson Sequential signaling in plasma-membrane domains during macropinosome formation in macrophages J. Cell Sci. 122 2009 3250 3261
    • (2009) J. Cell Sci. , vol.122 , pp. 3250-3261
    • Yoshida, S.1    Hoppe, A.D.2    Araki, N.3    Swanson, J.A.4
  • 35
    • 51049100594 scopus 로고    scopus 로고
    • Talin depletion reveals independence of initial cell spreading from integrin activation and traction
    • X. Zhang, G. Jiang, Y. Cai, S.J. Monkley, D.R. Critchley, and M.P. Sheetz Talin depletion reveals independence of initial cell spreading from integrin activation and traction Nat. Cell Biol. 10 2008 1062 1068
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1062-1068
    • Zhang, X.1    Jiang, G.2    Cai, Y.3    Monkley, S.J.4    Critchley, D.R.5    Sheetz, M.P.6
  • 36
    • 57749116060 scopus 로고    scopus 로고
    • Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces
    • J. Zhu, B.H. Luo, T. Xiao, C. Zhang, N. Nishida, and T.A. Springer Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces Mol. Cell 32 2008 849 861
    • (2008) Mol. Cell , vol.32 , pp. 849-861
    • Zhu, J.1    Luo, B.H.2    Xiao, T.3    Zhang, C.4    Nishida, N.5    Springer, T.A.6
  • 37
    • 39149139617 scopus 로고    scopus 로고
    • Structurally distinct phosphatases CD45 and CD148 both regulate B cell and macrophage immunoreceptor signaling
    • J.W. Zhu, T. Brdicka, T.R. Katsumoto, J. Lin, and A. Weiss Structurally distinct phosphatases CD45 and CD148 both regulate B cell and macrophage immunoreceptor signaling Immunity 28 2008 183 196
    • (2008) Immunity , vol.28 , pp. 183-196
    • Zhu, J.W.1    Brdicka, T.2    Katsumoto, T.R.3    Lin, J.4    Weiss, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.