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Volumn 65, Issue 14, 2008, Pages 2175-2190

Regulation of phagocyte migration and recruitment by Src-family kinases

Author keywords

Cell adhesion; Cell migration; Integrins; Macrophage; Neutrophil; Signal transduction; Src family kinases

Indexed keywords

CBL PROTEIN; FOCAL ADHESION KINASE 2; PROTEIN P190; PROTEIN TYROSINE KINASE;

EID: 47749143997     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-8005-6     Document Type: Review
Times cited : (47)

References (138)
  • 1
    • 0033755863 scopus 로고    scopus 로고
    • Src kinase-mediated signaling in leukocytes
    • Korade-Mirnics Z. and Corey S. J. (2000) Src kinase-mediated signaling in leukocytes. J. Leukoc. Biol. 68, 603-613.
    • (2000) J. Leukoc. Biol , vol.68 , pp. 603-613
    • Korade-Mirnics, Z.1    Corey, S.J.2
  • 2
    • 3042615397 scopus 로고    scopus 로고
    • Src-family kinases: Rheostats of immune cell signaling
    • Lowell C. A. (2004) Src-family kinases: rheostats of immune cell signaling. Mol. Immunol. 41, 631-643.
    • (2004) Mol. Immunol , vol.41 , pp. 631-643
    • Lowell, C.A.1
  • 3
    • 20044363664 scopus 로고    scopus 로고
    • Src and Syk kinases: Key regulators of phagocytic cell activation
    • Berton G., Mocsai A. and Lowell C. A. (2005) Src and Syk kinases: key regulators of phagocytic cell activation. Trends Immunol. 26, 208-214.
    • (2005) Trends Immunol , vol.26 , pp. 208-214
    • Berton, G.1    Mocsai, A.2    Lowell, C.A.3
  • 4
    • 34447309018 scopus 로고    scopus 로고
    • Convergence of immunoreceptor and integrin signaling
    • Abram C. L. and Lowell C. A. (2007) Convergence of immunoreceptor and integrin signaling. Immunol. Rev. 218, 29-44.
    • (2007) Immunol. Rev , vol.218 , pp. 29-44
    • Abram, C.L.1    Lowell, C.A.2
  • 5
    • 34247470836 scopus 로고    scopus 로고
    • Second generation inhibitors of BCRABL for the treatment of imatinib-resistant chronic myeloid leukaemia
    • Weisberg E., Manley P. W., Cowan-Jacob S. W., Hochhaus A. and Griffin J. D. (2007) Second generation inhibitors of BCRABL for the treatment of imatinib-resistant chronic myeloid leukaemia. Nat. Rev. Cancer. 7, 345-356.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 345-356
    • Weisberg, E.1    Manley, P.W.2    Cowan-Jacob, S.W.3    Hochhaus, A.4    Griffin, J.D.5
  • 6
    • 0028925552 scopus 로고
    • Urokinase plasminogen activator receptor, beta 2-integrins, and Src-kinases within a single receptor complex of human monocytes
    • Bohuslav J., Horejsi V., Hansmann C., Stockl J., Weidle U. H., Majdic O., Bartke I., Knapp W. and Stockinger H. (1995) Urokinase plasminogen activator receptor, beta 2-integrins, and Src-kinases within a single receptor complex of human monocytes. J. Exp. Med. 181, 1381-1390.
    • (1995) J. Exp. Med , vol.181 , pp. 1381-1390
    • Bohuslav, J.1    Horejsi, V.2    Hansmann, C.3    Stockl, J.4    Weidle, U.H.5    Majdic, O.6    Bartke, I.7    Knapp, W.8    Stockinger, H.9
  • 7
    • 0035209941 scopus 로고    scopus 로고
    • Role of Src kinases and Syk in Fcgamma receptor-mediated phagocytosis and phagosome-lysosome fusion
    • Majeed M., Caveggion E., Lowell C. A. and Berton G. (2001) Role of Src kinases and Syk in Fcgamma receptor-mediated phagocytosis and phagosome-lysosome fusion. J. Leukoc. Biol. 70, 801-811.
    • (2001) J. Leukoc. Biol , vol.70 , pp. 801-811
    • Majeed, M.1    Caveggion, E.2    Lowell, C.A.3    Berton, G.4
  • 8
    • 35548985405 scopus 로고    scopus 로고
    • Chemical inhibition of Src family kinases affects major LPS-activated pathways in primary human macrophages
    • Smolinska M. J., Horwood N. J., Page T. H., Smallie T. and Foxwell B. M. (2008) Chemical inhibition of Src family kinases affects major LPS-activated pathways in primary human macrophages. Mol. Immunol. 45, 990-1000.
    • (2008) Mol. Immunol , vol.45 , pp. 990-1000
    • Smolinska, M.J.1    Horwood, N.J.2    Page, T.H.3    Smallie, T.4    Foxwell, B.M.5
  • 9
    • 33748666884 scopus 로고    scopus 로고
    • Evidence for the requirement of ITAM domains but not SLP-76/Gads interaction for integrin signaling in hematopoietic cells
    • Abtahian F., Bezman N., Clemens R., Sebzda E., Cheng L., Shattil S. J., Kahn M. L. and Koretzky G. A. (2006) Evidence for the requirement of ITAM domains but not SLP-76/Gads interaction for integrin signaling in hematopoietic cells. Mol. Cell Biol. 26, 6936-6949.
    • (2006) Mol. Cell Biol , vol.26 , pp. 6936-6949
    • Abtahian, F.1    Bezman, N.2    Clemens, R.3    Sebzda, E.4    Cheng, L.5    Shattil, S.J.6    Kahn, M.L.7    Koretzky, G.A.8
  • 10
    • 33846295127 scopus 로고    scopus 로고
    • Integrin signaling in neutrophils and macrophages uses adaptors containing immunoreceptor tyrosine-based activation motifs
    • Mocsai A., Abram C. L., Jakus Z., Hu Y., Lanier L. L. and Lowell C. A. (2006) Integrin signaling in neutrophils and macrophages uses adaptors containing immunoreceptor tyrosine-based activation motifs. Nat. Immunol. 7, 1326-1333.
    • (2006) Nat. Immunol , vol.7 , pp. 1326-1333
    • Mocsai, A.1    Abram, C.L.2    Jakus, Z.3    Hu, Y.4    Lanier, L.L.5    Lowell, C.A.6
  • 12
  • 13
    • 34547905051 scopus 로고    scopus 로고
    • Neutrophil activation via beta2 integrins (CD11/CD18): Molecular mechanisms and clinical implications
    • Schymeinsky J., Mocsai A. and Walzog B. (2007) Neutrophil activation via beta2 integrins (CD11/CD18): molecular mechanisms and clinical implications. Thromb. Haemost. 98, 262-273.
    • (2007) Thromb. Haemost , vol.98 , pp. 262-273
    • Schymeinsky, J.1    Mocsai, A.2    Walzog, B.3
  • 14
    • 0033555864 scopus 로고    scopus 로고
    • Adhesion-dependent degranulation of neutrophils requires the Src family kinases Fgr and Hck
    • Mocsai A., Ligeti E., Lowell C. A. and Berton G. (1999) Adhesion-dependent degranulation of neutrophils requires the Src family kinases Fgr and Hck. J. Immunol. 162, 1120-1126.
    • (1999) J. Immunol , vol.162 , pp. 1120-1126
    • Mocsai, A.1    Ligeti, E.2    Lowell, C.A.3    Berton, G.4
  • 15
    • 0033554561 scopus 로고    scopus 로고
    • Novel association of the src family kinases, hck and c-fgr, with CCR3 receptor stimulation: A possible mechanism for eotaxin-induced human eosinophil chemotaxis
    • El-Shazly A., Yamaguchi N., Masuyama K., Suda T. and Ishikawa T. (1999) Novel association of the src family kinases, hck and c-fgr, with CCR3 receptor stimulation: A possible mechanism for eotaxin-induced human eosinophil chemotaxis. Biochem. Biophys. Res. Commun. 264, 163-170.
    • (1999) Biochem. Biophys. Res. Commun , vol.264 , pp. 163-170
    • El-Shazly, A.1    Yamaguchi, N.2    Masuyama, K.3    Suda, T.4    Ishikawa, T.5
  • 17
    • 0142190783 scopus 로고    scopus 로고
    • G-protein-coupled receptor signaling in Syk-deficient neutrophils and mast cells
    • Mocsai A., Zhang H., Jakus Z., Kitaura J., Kawakami T. and Lowell C. A. (2003) G-protein-coupled receptor signaling in Syk-deficient neutrophils and mast cells. Blood. 101, 4155-4163.
    • (2003) Blood , vol.101 , pp. 4155-4163
    • Mocsai, A.1    Zhang, H.2    Jakus, Z.3    Kitaura, J.4    Kawakami, T.5    Lowell, C.A.6
  • 18
    • 34547136955 scopus 로고    scopus 로고
    • M-CSF regulates the cytoskeleton via recruitment of a multimeric signaling complex to c-Fms Tyr-559/697/721
    • Faccio R., Takeshita S., Colaianni G., Chappel J., Zallone A., Teitelbaum S. L. and Ross F. P. (2007) M-CSF regulates the cytoskeleton via recruitment of a multimeric signaling complex to c-Fms Tyr-559/697/721. J. Biol. Chem. 282, 18991-18999.
    • (2007) J. Biol. Chem , vol.282 , pp. 18991-18999
    • Faccio, R.1    Takeshita, S.2    Colaianni, G.3    Chappel, J.4    Zallone, A.5    Teitelbaum, S.L.6    Ross, F.P.7
  • 19
    • 7444254061 scopus 로고    scopus 로고
    • CSF-1 regulation of the wandering macrophage: Complexity in action
    • Pixley F. J. and Stanley E. R. (2004) CSF-1 regulation of the wandering macrophage: complexity in action. Trends Cell Biol. 14, 628-638.
    • (2004) Trends Cell Biol , vol.14 , pp. 628-638
    • Pixley, F.J.1    Stanley, E.R.2
  • 22
    • 33947497852 scopus 로고    scopus 로고
    • Osteoclasts: What do they do and how do they do it?
    • Teitelbaum S. L. (2007) Osteoclasts: what do they do and how do they do it? Am. J. Pathol. 170, 427-435.
    • (2007) Am. J. Pathol , vol.170 , pp. 427-435
    • Teitelbaum, S.L.1
  • 23
    • 0023083976 scopus 로고
    • Leukocyte adhesion deficiency: An inherited defect in the Mac-1, LFA-1, and p150, 95 glycoproteins
    • Anderson D. C. and Springer T. A. (1987) Leukocyte adhesion deficiency: an inherited defect in the Mac-1, LFA-1, and p150, 95 glycoproteins. Annu. Rev. Med. 38, 175-194.
    • (1987) Annu. Rev. Med , vol.38 , pp. 175-194
    • Anderson, D.C.1    Springer, T.A.2
  • 24
    • 34548230927 scopus 로고    scopus 로고
    • Getting to the site of inflammation: The leukocyte adhesion cascade updated
    • Ley K., Laudanna C., Cybulsky M. I. and Nourshargh S. (2007) Getting to the site of inflammation: the leukocyte adhesion cascade updated. Nat. Rev. Immunol. 7, 678-689.
    • (2007) Nat. Rev. Immunol , vol.7 , pp. 678-689
    • Ley, K.1    Laudanna, C.2    Cybulsky, M.I.3    Nourshargh, S.4
  • 25
    • 0346734202 scopus 로고    scopus 로고
    • Regulation of leukocyte transmigration: Cell surface interactions and signaling events
    • Liu Y., Shaw S. K., Ma S., Yang L., Luscinskas F. W. and Parkos C. A. (2004) Regulation of leukocyte transmigration: cell surface interactions and signaling events. J. Immunol. 172, 7-13.
    • (2004) J. Immunol , vol.172 , pp. 7-13
    • Liu, Y.1    Shaw, S.K.2    Ma, S.3    Yang, L.4    Luscinskas, F.W.5    Parkos, C.A.6
  • 27
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk
    • Geiger B., Bershadsky A., Pankov R. and Yamada K. M. (2001) Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk. Nat. Rev. Mol. Cell Biol. 2, 793-805.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 28
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood J. D. and Cheresh D. A. (2002) Role of integrins in cell invasion and migration. Nat. Rev. Cancer. 2, 91-100.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 29
    • 0032731892 scopus 로고    scopus 로고
    • Tumor invasion: Role of growth factor-induced cell motility
    • Wells A. (2000) Tumor invasion: role of growth factor-induced cell motility. Adv. Cancer Res. 78, 31-101.
    • (2000) Adv. Cancer Res , vol.78 , pp. 31-101
    • Wells, A.1
  • 30
    • 0028293147 scopus 로고
    • Functional overlap in the src gene family: Inactivation of hck and fgr impairs natural immunity
    • Lowell C. A., Soriano P. and Varmus H. E. (1994) Functional overlap in the src gene family: inactivation of hck and fgr impairs natural immunity. Genes Dev. 8, 387-398.
    • (1994) Genes Dev , vol.8 , pp. 387-398
    • Lowell, C.A.1    Soriano, P.2    Varmus, H.E.3
  • 31
    • 0032479979 scopus 로고    scopus 로고
    • A beta 1 integrin signaling pathway involving Src-family kinases, Cbl and PI-3 kinase is required for macrophage spreading and migration
    • Meng F. and Lowell C. A. (1998) A beta 1 integrin signaling pathway involving Src-family kinases, Cbl and PI-3 kinase is required for macrophage spreading and migration. Embo J. 17, 4391-4403.
    • (1998) Embo J , vol.17 , pp. 4391-4403
    • Meng, F.1    Lowell, C.A.2
  • 32
    • 0033490109 scopus 로고    scopus 로고
    • Impaired integrin-mediated signal transduction, altered cytoskeletal structure and reduced motility in Hck/Fgr deficient macrophages
    • Suen P. W., Ilic D., Caveggion E., Berton G., Damsky C. H. and Lowell C. A. (1999) Impaired integrin-mediated signal transduction, altered cytoskeletal structure and reduced motility in Hck/Fgr deficient macrophages. J. Cell Sci. 112 (Pt 22), 4067-4078.
    • (1999) J. Cell Sci , vol.112 , Issue.PART 22 , pp. 4067-4078
    • Suen, P.W.1    Ilic, D.2    Caveggion, E.3    Berton, G.4    Damsky, C.H.5    Lowell, C.A.6
  • 34
    • 0033153319 scopus 로고    scopus 로고
    • Urokinase receptor-dependent and -independent p56/59(hck) activation state is a molecular switch between myelomonocytic cell motility and adherence
    • Chiaradonna F., Fontana L., Iavarone C., Carriero M. V., Scholz G., Barone M. V. and Stoppelli M. P. (1999) Urokinase receptor-dependent and -independent p56/59(hck) activation state is a molecular switch between myelomonocytic cell motility and adherence. Embo J. 18, 3013-3023.
    • (1999) Embo J , vol.18 , pp. 3013-3023
    • Chiaradonna, F.1    Fontana, L.2    Iavarone, C.3    Carriero, M.V.4    Scholz, G.5    Barone, M.V.6    Stoppelli, M.P.7
  • 35
    • 0037036415 scopus 로고    scopus 로고
    • p59Hck isoform induces Factin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner
    • Carreno S., Caron E., Cougoule C., Emorine L. J. and Maridonneau-Parini I. (2002) p59Hck isoform induces Factin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner. J. Biol. Chem. 277, 21007-21016.
    • (2002) J. Biol. Chem , vol.277 , pp. 21007-21016
    • Carreno, S.1    Caron, E.2    Cougoule, C.3    Emorine, L.J.4    Maridonneau-Parini, I.5
  • 41
    • 0035825121 scopus 로고    scopus 로고
    • Cbl associates with Pyk2 and Src to regulate Src kinase activity, alpha(v)beta(3) integrin-mediated signaling, cell adhesion, and osteoclast motility
    • Sanjay A., Houghton A., Neff L., DiDomenico E., Bardelay C., Antoine E., Levy J., Gailit J., Bowtell D., Horne W. C. and Baron R. (2001) Cbl associates with Pyk2 and Src to regulate Src kinase activity, alpha(v)beta(3) integrin-mediated signaling, cell adhesion, and osteoclast motility. J. Cell Biol. 152, 181-195.
    • (2001) J. Cell Biol , vol.152 , pp. 181-195
    • Sanjay, A.1    Houghton, A.2    Neff, L.3    DiDomenico, E.4    Bardelay, C.5    Antoine, E.6    Levy, J.7    Gailit, J.8    Bowtell, D.9    Horne, W.C.10    Baron, R.11
  • 42
    • 28544451132 scopus 로고    scopus 로고
    • The role(s) of Src kinase and Cbl proteins in the regulation of osteoclast differentiation and function
    • Horne W. C., Sanjay A., Bruzzaniti A. and Baron R. (2005) The role(s) of Src kinase and Cbl proteins in the regulation of osteoclast differentiation and function. Immunol. Rev. 208, 106-125.
    • (2005) Immunol. Rev , vol.208 , pp. 106-125
    • Horne, W.C.1    Sanjay, A.2    Bruzzaniti, A.3    Baron, R.4
  • 43
    • 19444368311 scopus 로고    scopus 로고
    • BCL6 suppresses RhoA activity to alter macrophage morphology and motility
    • Pixley F. J., Xiong Y., Yu R. Y., Sahai E. A., Stanley E. R. and Ye B. H. (2005) BCL6 suppresses RhoA activity to alter macrophage morphology and motility. J. Cell Sci. 118, 1873-1883.
    • (2005) J. Cell Sci , vol.118 , pp. 1873-1883
    • Pixley, F.J.1    Xiong, Y.2    Yu, R.Y.3    Sahai, E.A.4    Stanley, E.R.5    Ye, B.H.6
  • 44
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger D. A. and Horwitz A. F. (1996) Cell migration: a physically integrated molecular process. Cell. 84, 359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 45
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas S. M. and Brugge J. S. (1997) Cellular functions regulated by Src family kinases. Annu. Rev. Cell Dev. Biol. 13, 513-609.
    • (1997) Annu. Rev. Cell Dev. Biol , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 46
    • 0142149188 scopus 로고    scopus 로고
    • Rac2 specificity in macrophage integrin signaling: Potential role for Syk kinase
    • Pradip D., Peng X. and Durden D. L. (2003) Rac2 specificity in macrophage integrin signaling: potential role for Syk kinase. J. Biol. Chem. 278, 41661-41669.
    • (2003) J. Biol. Chem , vol.278 , pp. 41661-41669
    • Pradip, D.1    Peng, X.2    Durden, D.L.3
  • 47
    • 24744449505 scopus 로고    scopus 로고
    • Syk is required for monocyte/macrophage chemotaxis to CX3CL1 (Fractalkine)
    • Gevrey J. C., Isaac B. M. and Cox D. (2005) Syk is required for monocyte/macrophage chemotaxis to CX3CL1 (Fractalkine). J. Immunol. 175, 3737-3745.
    • (2005) J. Immunol , vol.175 , pp. 3737-3745
    • Gevrey, J.C.1    Isaac, B.M.2    Cox, D.3
  • 48
    • 21644448126 scopus 로고    scopus 로고
    • The non-receptor tyrosine kinase Syk regulates lamellipodium formation and site-directed migration of human leukocytes
    • Schymeinsky J., Then C. and Walzog B. (2005) The non-receptor tyrosine kinase Syk regulates lamellipodium formation and site-directed migration of human leukocytes. J. Cell Physiol. 204, 614-622.
    • (2005) J. Cell Physiol , vol.204 , pp. 614-622
    • Schymeinsky, J.1    Then, C.2    Walzog, B.3
  • 49
    • 0035316576 scopus 로고    scopus 로고
    • Thien C. B. and Langdon W. Y. (2001) Cbl: many adaptations to regulate protein tyrosine kinases. Nat. Rev. Mol. Cell Biol. 2, 294-307.
    • Thien C. B. and Langdon W. Y. (2001) Cbl: many adaptations to regulate protein tyrosine kinases. Nat. Rev. Mol. Cell Biol. 2, 294-307.
  • 50
    • 17944366407 scopus 로고    scopus 로고
    • Vines C. M., Potter J. W., Xu Y., Geahlen R. L., Costello P. S., Tybulewicz V. L., Lowell C. A., Chang P. W., Gresham H. D. and Willman C. L. (2001) Inhibition of beta 2 integrin receptor and Syk kinase signaling in monocytes by the Src family kinase Fgr. Immunity. 15, 507-519.
    • Vines C. M., Potter J. W., Xu Y., Geahlen R. L., Costello P. S., Tybulewicz V. L., Lowell C. A., Chang P. W., Gresham H. D. and Willman C. L. (2001) Inhibition of beta 2 integrin receptor and Syk kinase signaling in monocytes by the Src family kinase Fgr. Immunity. 15, 507-519.
  • 51
    • 0031568669 scopus 로고    scopus 로고
    • Signaling by adhesion in human neutrophils: Activation of the p72syk tyrosine kinase and formation of protein complexes containing p72syk and Src family kinases in neutrophils spreading over fibrinogen
    • Yan S. R., Huang M. and Berton G. (1997) Signaling by adhesion in human neutrophils: activation of the p72syk tyrosine kinase and formation of protein complexes containing p72syk and Src family kinases in neutrophils spreading over fibrinogen. J. Immunol. 158, 1902-1910.
    • (1997) J. Immunol , vol.158 , pp. 1902-1910
    • Yan, S.R.1    Huang, M.2    Berton, G.3
  • 54
    • 0042351110 scopus 로고    scopus 로고
    • A role for Syk-kinase in the control of the binding cycle of the beta2 integrins (CD11/CD18) in human polymorphonuclear neutrophils
    • Willeke T., Schymeinsky J., Prange P., Zahler S. and Walzog B. (2003) A role for Syk-kinase in the control of the binding cycle of the beta2 integrins (CD11/CD18) in human polymorphonuclear neutrophils. J. Leukoc. Biol. 74, 260-269.
    • (2003) J. Leukoc. Biol , vol.74 , pp. 260-269
    • Willeke, T.1    Schymeinsky, J.2    Prange, P.3    Zahler, S.4    Walzog, B.5
  • 55
  • 56
    • 14644425319 scopus 로고    scopus 로고
    • Mechanisms of BCR-ABL in the pathogenesis of chronic myelogenous leukaemia
    • Ren R. (2005) Mechanisms of BCR-ABL in the pathogenesis of chronic myelogenous leukaemia. Nat. Rev. Cancer. 5, 172-183.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 172-183
    • Ren, R.1
  • 57
    • 33947376040 scopus 로고    scopus 로고
    • Oncogenic signaling: New insights and controversies from chronic myeloid leukemia
    • Van Etten R. A. (2007) Oncogenic signaling: new insights and controversies from chronic myeloid leukemia. J. Exp. Med. 204, 461-465.
    • (2007) J. Exp. Med , vol.204 , pp. 461-465
    • Van Etten, R.A.1
  • 60
    • 33947198166 scopus 로고    scopus 로고
    • The Src family kinases Hck and Fgr regulate neutrophil responses to N-formyl-methionyl-leucyl-phenylalanine
    • Fumagalli L., Zhang H., Baruzzi A., Lowell C. A. and Berton G. (2007) The Src family kinases Hck and Fgr regulate neutrophil responses to N-formyl-methionyl-leucyl-phenylalanine. J. Immunol. 178, 3874-3885.
    • (2007) J. Immunol , vol.178 , pp. 3874-3885
    • Fumagalli, L.1    Zhang, H.2    Baruzzi, A.3    Lowell, C.A.4    Berton, G.5
  • 61
    • 13844276957 scopus 로고    scopus 로고
    • The Src family kinases Hck and Fgr negatively regulate neutrophil and dendritic cell chemokine signaling via PIR-B
    • Zhang H., Meng F., Chu C. L., Takai T. and Lowell C. A. (2005)The Src family kinases Hck and Fgr negatively regulate neutrophil and dendritic cell chemokine signaling via PIR-B. Immunity. 22, 235-246.
    • (2005) Immunity , vol.22 , pp. 235-246
    • Zhang, H.1    Meng, F.2    Chu, C.L.3    Takai, T.4    Lowell, C.A.5
  • 63
    • 0141889083 scopus 로고    scopus 로고
    • The hemopoietic Rho/Rac guanine nucleotide exchange factor Vav1 regulates N-formyl-methionyl-leucyl-phenylalanine-activated neutrophil functions
    • Kim C., Marchal C. C., Penninger J. and Dinauer M. C. (2003) The hemopoietic Rho/Rac guanine nucleotide exchange factor Vav1 regulates N-formyl-methionyl-leucyl-phenylalanine-activated neutrophil functions. J. Immunol. 171, 4425-4430.
    • (2003) J. Immunol , vol.171 , pp. 4425-4430
    • Kim, C.1    Marchal, C.C.2    Penninger, J.3    Dinauer, M.C.4
  • 64
    • 0342313568 scopus 로고    scopus 로고
    • Kinase pathways in chemoattractant-induced degranulation of neutrophils: The role of p38 mitogen-activated protein kinase activated by Src family kinases
    • Mocsai A., Jakus Z., Vantus T., Berton G., Lowell C. A. and Ligeti E. (2000) Kinase pathways in chemoattractant-induced degranulation of neutrophils: the role of p38 mitogen-activated protein kinase activated by Src family kinases. J. Immunol. 164, 4321-4331.
    • (2000) J. Immunol , vol.164 , pp. 4321-4331
    • Mocsai, A.1    Jakus, Z.2    Vantus, T.3    Berton, G.4    Lowell, C.A.5    Ligeti, E.6
  • 67
    • 33947684328 scopus 로고    scopus 로고
    • Signaling requirements for translocation of P-Rex1, a key Rac2 exchange factor involved in chemoattractant-stimulated human neutrophil function
    • Zhao T., Nalbant P., Hoshino M., Dong X., Wu D. and Bokoch G. M. (2007) Signaling requirements for translocation of P-Rex1, a key Rac2 exchange factor involved in chemoattractant-stimulated human neutrophil function. J. Leukoc. Biol. 81, 1127-1136.
    • (2007) J. Leukoc. Biol , vol.81 , pp. 1127-1136
    • Zhao, T.1    Nalbant, P.2    Hoshino, M.3    Dong, X.4    Wu, D.5    Bokoch, G.M.6
  • 68
    • 33845268014 scopus 로고    scopus 로고
    • The Vav binding site of the non-receptor tyrosine kinase Syk at Tyr 348 is critical for beta2 integrin (CD11/CD18)-mediated neutrophil migration
    • Schymeinsky J., Sindrilaru A., FrommholdD., Sperandio M., Gerstl R., Then C., Mocsai A., Scharffetter-Kochanek K. and Walzog B. (2006) The Vav binding site of the non-receptor tyrosine kinase Syk at Tyr 348 is critical for beta2 integrin (CD11/CD18)-mediated neutrophil migration. Blood. 108, 3919-3927.
    • (2006) Blood , vol.108 , pp. 3919-3927
    • Schymeinsky, J.1    Sindrilaru, A.2    FrommholdD3    Sperandio, M.4    Gerstl, R.5    Then, C.6    Mocsai, A.7    Scharffetter-Kochanek, K.8    Walzog, B.9
  • 69
    • 0032560544 scopus 로고    scopus 로고
    • Resistance to endotoxic shock and reduced neutrophil migration in mice deficient for the Src-family kinases Hck and Fgr
    • Lowell C. A. and Berton G. (1998) Resistance to endotoxic shock and reduced neutrophil migration in mice deficient for the Src-family kinases Hck and Fgr. Proc. Natl. Acad. Sci. U. S. A. 95, 7580-7584.
    • (1998) Proc. Natl. Acad. Sci. U. S. A , vol.95 , pp. 7580-7584
    • Lowell, C.A.1    Berton, G.2
  • 71
    • 0027139765 scopus 로고
    • Anti-CD11b antibody prevents immunopathologic changes in viable moth-eaten bone marrow chimeric mice
    • Koo G. C., Rosen H., Sirotina A., Ma X. D. and Shultz L. D. (1993) Anti-CD11b antibody prevents immunopathologic changes in viable moth-eaten bone marrow chimeric mice. J. Immunol. 151, 6733-6741.
    • (1993) J. Immunol , vol.151 , pp. 6733-6741
    • Koo, G.C.1    Rosen, H.2    Sirotina, A.3    Ma, X.D.4    Shultz, L.D.5
  • 72
    • 0041344445 scopus 로고    scopus 로고
    • The Lyn tyrosine kinase negatively regulates neutrophil integrin signaling
    • Pereira S. and Lowell C. (2003) The Lyn tyrosine kinase negatively regulates neutrophil integrin signaling. J Immunol. 171, 1319-1327.
    • (2003) J Immunol , vol.171 , pp. 1319-1327
    • Pereira, S.1    Lowell, C.2
  • 73
    • 0037438682 scopus 로고    scopus 로고
    • Antiinflammatory effects of genistein, a tyrosine kinase inhibitor, on a guinea pig model of asthma
    • Duan W., Kuo I. C., Selvarajan S., Chua K. Y., Bay B. H. and Wong W. S. (2003) Antiinflammatory effects of genistein, a tyrosine kinase inhibitor, on a guinea pig model of asthma. Am. J. Respir. Crit. Care Med. 167, 185-192.
    • (2003) Am. J. Respir. Crit. Care Med , vol.167 , pp. 185-192
    • Duan, W.1    Kuo, I.C.2    Selvarajan, S.3    Chua, K.Y.4    Bay, B.H.5    Wong, W.S.6
  • 76
    • 34250180872 scopus 로고    scopus 로고
    • Spleen tyrosine kinase Syk is necessary for E-selectin-induced alpha(L)beta(2) integrin-mediated rolling on intercellular adhesion molecule-1
    • Zarbock A., Lowell C. A. and Ley K. (2007) Spleen tyrosine kinase Syk is necessary for E-selectin-induced alpha(L)beta(2) integrin-mediated rolling on intercellular adhesion molecule-1. Immunity. 26, 773-783.
    • (2007) Immunity , vol.26 , pp. 773-783
    • Zarbock, A.1    Lowell, C.A.2    Ley, K.3
  • 77
    • 0030008394 scopus 로고    scopus 로고
    • Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions
    • Lowell C. A., Fumagalli L. and Berton G. (1996) Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions. J. Cell Biol. 133, 895-910.
    • (1996) J. Cell Biol , vol.133 , pp. 895-910
    • Lowell, C.A.1    Fumagalli, L.2    Berton, G.3
  • 78
    • 33745313872 scopus 로고    scopus 로고
    • The Src family kinases Hck and Fgr are dispensable for inside-out, chemoattractant-induced signaling regulating β2 integrin affinity and valency in neutrophils, but are required for β2 integrin-mediated outside-in signaling involved in sustained adhesion
    • Giagulli C L. O., E. Caveggion, B. Rossi, C. A. Lowell, G. Constantin, C. Laudanna, and G. Berton (2006) The Src family kinases Hck and Fgr are dispensable for inside-out, chemoattractant-induced signaling regulating β2 integrin affinity and valency in neutrophils, but are required for β2 integrin-mediated outside-in signaling involved in sustained adhesion. J. Immunol. 177, 604-11.
    • (2006) J. Immunol , vol.177 , pp. 604-611
    • Giagulli, C.L.O.1    Caveggion, E.2    Rossi, B.3    Lowell, C.A.4    Constantin, G.5    Laudanna, C.6    Berton, G.7
  • 79
    • 0032536833 scopus 로고    scopus 로고
    • Neutrophils emigrate from venules by a transendothelial cell pathway in response to FMLP
    • Feng D., Nagy J. A., Pyne K., Dvorak H. F. and Dvorak A. M. (1998) Neutrophils emigrate from venules by a transendothelial cell pathway in response to FMLP. J. Exp. Med. 187, 903-915.
    • (1998) J. Exp. Med , vol.187 , pp. 903-915
    • Feng, D.1    Nagy, J.A.2    Pyne, K.3    Dvorak, H.F.4    Dvorak, A.M.5
  • 81
    • 21044433334 scopus 로고    scopus 로고
    • Podosomes at a glance
    • Linder S. and Kopp P. (2005) Podosomes at a glance. J. Cell Sci. 118, 2079-2082.
    • (2005) J. Cell Sci , vol.118 , pp. 2079-2082
    • Linder, S.1    Kopp, P.2
  • 82
    • 0021723422 scopus 로고
    • Cell-substratum interaction of cultured avian osteoclasts is mediated by specific adhesion structures
    • Marchisio P. C., Cirillo D., Naldini L., Primavera M. V., Teti A. and Zambonin-Zallone A. (1984) Cell-substratum interaction of cultured avian osteoclasts is mediated by specific adhesion structures. J. Cell Biol. 99, 1696-1705.
    • (1984) J. Cell Biol , vol.99 , pp. 1696-1705
    • Marchisio, P.C.1    Cirillo, D.2    Naldini, L.3    Primavera, M.V.4    Teti, A.5    Zambonin-Zallone, A.6
  • 83
    • 0022357441 scopus 로고
    • Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes
    • Tarone G., Cirillo D., Giancotti F. G., Comoglio P. M. and Marchisio P. C. (1985) Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes. Exp. Cell Res. 159, 141-157.
    • (1985) Exp. Cell Res , vol.159 , pp. 141-157
    • Tarone, G.1    Cirillo, D.2    Giancotti, F.G.3    Comoglio, P.M.4    Marchisio, P.C.5
  • 85
    • 34547099351 scopus 로고    scopus 로고
    • Activation of p61Hck triggers WASp- and Arp2/3-dependent actin-comet tail biogenesis and accelerates lysosomes
    • Vincent C., Maridonneau-Parini I., Le Clainche C., Gounon P. and Labrousse A. (2007) Activation of p61Hck triggers WASp- and Arp2/3-dependent actin-comet tail biogenesis and accelerates lysosomes. J. Biol. Chem. 282, 19565-19574.
    • (2007) J. Biol. Chem , vol.282 , pp. 19565-19574
    • Vincent, C.1    Maridonneau-Parini, I.2    Le Clainche, C.3    Gounon, P.4    Labrousse, A.5
  • 86
    • 0037090069 scopus 로고    scopus 로고
    • Role of NADPH oxidase in the mechanism of lung neutrophil sequestration and microvessel injury induced by Gram-negative sepsis: Studies in p47phox-/- and gp91phox-/- mice
    • Gao X. P., Standiford T. J., Rahman A., Newstead M., Holland S. M., Dinauer M. C., Liu Q. H. and Malik A. B. (2002) Role of NADPH oxidase in the mechanism of lung neutrophil sequestration and microvessel injury induced by Gram-negative sepsis: studies in p47phox-/- and gp91phox-/- mice. J. Immunol. 168, 3974-3982.
    • (2002) J. Immunol , vol.168 , pp. 3974-3982
    • Gao, X.P.1    Standiford, T.J.2    Rahman, A.3    Newstead, M.4    Holland, S.M.5    Dinauer, M.C.6    Liu, Q.H.7    Malik, A.B.8
  • 87
    • 0141799937 scopus 로고    scopus 로고
    • Regulation of vascular permeability by neutrophils in acute inflammation
    • Lindbom L. (2003) Regulation of vascular permeability by neutrophils in acute inflammation. Chem. Immunol. Allergy. 83, 146-166.
    • (2003) Chem. Immunol. Allergy , vol.83 , pp. 146-166
    • Lindbom, L.1
  • 88
    • 33745029732 scopus 로고    scopus 로고
    • Venular basement membranes contain specific matrix protein low expression regions that act as exit points for emigrating neutrophils
    • Wang S., Voisin M. B. , Larbi K. Y. , Dangerfield J. , Scheiermann C., Tran M., Maxwell P. H., Sorokin L. and Nourshargh S. (2006) Venular basement membranes contain specific matrix protein low expression regions that act as exit points for emigrating neutrophils. J. Exp. Med. 203, 1519-1532.
    • (2006) J. Exp. Med , vol.203 , pp. 1519-1532
    • Wang, S.1    Voisin, M.B.2    Larbi, K.Y.3    Dangerfield, J.4    Scheiermann, C.5    Tran, M.6    Maxwell, P.H.7    Sorokin, L.8    Nourshargh, S.9
  • 89
    • 35748948971 scopus 로고    scopus 로고
    • ICAM-1-mediated, Src- and Pyk2-dependent vascular endothelial cadherin tyrosine phosphorylation is required for leukocyte transendothelial migration
    • Allingham M. J., van Buul J. D. and Burridge K. (2007) ICAM-1-mediated, Src- and Pyk2-dependent vascular endothelial cadherin tyrosine phosphorylation is required for leukocyte transendothelial migration. J. Immunol. 179, 4053-4064.
    • (2007) J. Immunol , vol.179 , pp. 4053-4064
    • Allingham, M.J.1    van Buul, J.D.2    Burridge, K.3
  • 90
    • 33646784019 scopus 로고    scopus 로고
    • Endothelial cell cortactin phosphorylation by Src contributes to polymorphonuclear leukocyte transmigration in vitro
    • Yang L., Kowalski J. R., Zhan X., Thomas S. M. and Luscinskas F. W. (2006) Endothelial cell cortactin phosphorylation by Src contributes to polymorphonuclear leukocyte transmigration in vitro. Circ. Res. 98, 394-402.
    • (2006) Circ. Res , vol.98 , pp. 394-402
    • Yang, L.1    Kowalski, J.R.2    Zhan, X.3    Thomas, S.M.4    Luscinskas, F.W.5
  • 92
    • 20544462391 scopus 로고    scopus 로고
    • Yokoyama N., deBakker C. D., Zappacosta F., Huddleston M. J., Annan R. S., Ravichandran K. S. and Miller W. T. (2005) Identification of tyrosine residues on ELMO1 that are phosphorylated by the Src-family kinase Hck. Biochemistry. 44, 8841-8849.
    • Yokoyama N., deBakker C. D., Zappacosta F., Huddleston M. J., Annan R. S., Ravichandran K. S. and Miller W. T. (2005) Identification of tyrosine residues on ELMO1 that are phosphorylated by the Src-family kinase Hck. Biochemistry. 44, 8841-8849.
  • 93
    • 0029823946 scopus 로고    scopus 로고
    • A tyrosine kinase signaling pathway accounts for the majority of phosphatidylinositol 3, 4, 5-trisphosphate formation in chemoattractant-stimulated human neutrophils
    • Ptasznik A., Prossnitz E. R., Yoshikawa D., Smrcka A., Traynor-Kaplan A. E. and Bokoch G. M. (1996) A tyrosine kinase signaling pathway accounts for the majority of phosphatidylinositol 3, 4, 5-trisphosphate formation in chemoattractant-stimulated human neutrophils. J. Biol. Chem. 271, 25204-25207.
    • (1996) J. Biol. Chem , vol.271 , pp. 25204-25207
    • Ptasznik, A.1    Prossnitz, E.R.2    Yoshikawa, D.3    Smrcka, A.4    Traynor-Kaplan, A.E.5    Bokoch, G.M.6
  • 94
    • 0029148780 scopus 로고
    • G protein-coupled chemoattractant receptors regulate Lyn tyrosine kinase. Shc adapter protein signaling complexes
    • Ptasznik A., Traynor-Kaplan A. and Bokoch G. M. (1995) G protein-coupled chemoattractant receptors regulate Lyn tyrosine kinase. Shc adapter protein signaling complexes. J. Biol. Chem. 270, 19969-19973.
    • (1995) J. Biol. Chem , vol.270 , pp. 19969-19973
    • Ptasznik, A.1    Traynor-Kaplan, A.2    Bokoch, G.M.3
  • 95
    • 0032193220 scopus 로고    scopus 로고
    • Essential roles of Lyn in fibronectin-mediated filamentous actin assembly and cell motility in mast cells
    • Suzuki T. , Shoji S. , Yamamoto K. , Nada S. , Okada M., Yamamoto T. and Honda Z. (1998) Essential roles of Lyn in fibronectin-mediated filamentous actin assembly and cell motility in mast cells. J. Immunol. 161, 3694-3701.
    • (1998) J. Immunol , vol.161 , pp. 3694-3701
    • Suzuki, T.1    Shoji, S.2    Yamamoto, K.3    Nada, S.4    Okada, M.5    Yamamoto, T.6    Honda, Z.7
  • 96
    • 0035880224 scopus 로고    scopus 로고
    • O'Laughlin-Bunner B., Radosevic N., Taylor M. L., Shivakrupa, DeBerry C., Metcalfe D. D., Zhou M., Lowell C. and Linnekin D. (2001) Lyn is required for normal stem cell factor-induced proliferation and chemotaxis of primary hematopoietic cells. Blood. 98, 343-350.
    • O'Laughlin-Bunner B., Radosevic N., Taylor M. L., Shivakrupa, DeBerry C., Metcalfe D. D., Zhou M., Lowell C. and Linnekin D. (2001) Lyn is required for normal stem cell factor-induced proliferation and chemotaxis of primary hematopoietic cells. Blood. 98, 343-350.
  • 98
    • 0036566548 scopus 로고    scopus 로고
    • Critical roles of c-Kit tyrosine residues 567 and 719 in stem cell factor-induced chemotaxis: Contribution of src family kinase and PI3-kinase on calcium mobilization and cell migration
    • Ueda S., Mizuki M., Ikeda H., Tsujimura T., Matsumura I., Nakano K., Daino H., Honda Zi Z., Sonoyama J., Shibayama H., Sugahara H., Machii T. and Kanakura Y. (2002) Critical roles of c-Kit tyrosine residues 567 and 719 in stem cell factor-induced chemotaxis: contribution of src family kinase and PI3-kinase on calcium mobilization and cell migration. Blood. 99, 3342-3349.
    • (2002) Blood , vol.99 , pp. 3342-3349
    • Ueda, S.1    Mizuki, M.2    Ikeda, H.3    Tsujimura, T.4    Matsumura, I.5    Nakano, K.6    Daino, H.7    Honda, Z.Z.8    Sonoyama, J.9    Shibayama, H.10    Sugahara, H.11    Machii, T.12    Kanakura, Y.13
  • 100
    • 33744467684 scopus 로고    scopus 로고
    • Integrin inhibition through Lyn-dependent cross talk from CXCR4 chemokine receptors in normal human CD34+ marrow cells
    • Nakata Y., Tomkowicz B., Gewirtz A. M. and Ptasznik A. (2006) Integrin inhibition through Lyn-dependent cross talk from CXCR4 chemokine receptors in normal human CD34+ marrow cells. Blood. 107, 4234-4239.
    • (2006) Blood , vol.107 , pp. 4234-4239
    • Nakata, Y.1    Tomkowicz, B.2    Gewirtz, A.M.3    Ptasznik, A.4
  • 101
    • 33750335844 scopus 로고    scopus 로고
    • CrkL plays a role in SDF-1-induced activation of the Raf-1/MEK/Erk pathway through Ras and Rac to mediate chemotactic signaling in hematopoietic cells
    • Arai A., Aoki M., Weihua Y., Jin A. and Miura O. (2006) CrkL plays a role in SDF-1-induced activation of the Raf-1/MEK/Erk pathway through Ras and Rac to mediate chemotactic signaling in hematopoietic cells. Cell Signal. 18, 2162-2171.
    • (2006) Cell Signal , vol.18 , pp. 2162-2171
    • Arai, A.1    Aoki, M.2    Weihua, Y.3    Jin, A.4    Miura, O.5
  • 102
    • 0035242032 scopus 로고    scopus 로고
    • SHP2 and cbl participate in alpha-chemokine receptor CXCR4-mediated signaling pathways
    • Chernock R. D., Cherla R. P. and Ganju R. K. (2001) SHP2 and cbl participate in alpha-chemokine receptor CXCR4-mediated signaling pathways. Blood. 97, 608-615.
    • (2001) Blood , vol.97 , pp. 608-615
    • Chernock, R.D.1    Cherla, R.P.2    Ganju, R.K.3
  • 103
    • 33744827154 scopus 로고    scopus 로고
    • Fyn kinase acts upstream of Shp2 and p38 mitogen-activated protein kinase to promote chemotaxis of mast cells towards stem cell factor
    • Samayawardhena L. A., Hu J., Stein P. L. and Craig A. W. (2006) Fyn kinase acts upstream of Shp2 and p38 mitogen-activated protein kinase to promote chemotaxis of mast cells towards stem cell factor. Cell Signal. 18, 1447-1454.
    • (2006) Cell Signal , vol.18 , pp. 1447-1454
    • Samayawardhena, L.A.1    Hu, J.2    Stein, P.L.3    Craig, A.W.4
  • 104
    • 34247380314 scopus 로고    scopus 로고
    • Involvement of Fyn kinase in Kit and integrin-mediated Rac activation, cytoskeletal reorganization, and chemotaxis of mast cells
    • Samayawardhena L. A., Kapur R. and Craig A. W. (2007) Involvement of Fyn kinase in Kit and integrin-mediated Rac activation, cytoskeletal reorganization, and chemotaxis of mast cells. Blood. 109, 3679-3686.
    • (2007) Blood , vol.109 , pp. 3679-3686
    • Samayawardhena, L.A.1    Kapur, R.2    Craig, A.W.3
  • 105
    • 23444446015 scopus 로고    scopus 로고
    • Chemoattractant induces LFA-1 associated PI 3K activity and cell migration that are dependent on Fyn signaling
    • Bernardini G., Kim J. Y., Gismondi A., Butcher E. C. and Santoni A. (2005) Chemoattractant induces LFA-1 associated PI 3K activity and cell migration that are dependent on Fyn signaling. Faseb J. 19, 1305-1307.
    • (2005) Faseb J , vol.19 , pp. 1305-1307
    • Bernardini, G.1    Kim, J.Y.2    Gismondi, A.3    Butcher, E.C.4    Santoni, A.5
  • 106
    • 0029092072 scopus 로고    scopus 로고
    • Ryan T. C., Cruikshank W. W., Kornfeld H., Collins T. L. and Center D. M. (1995) The CD4-associated tyrosine kinase p56lck is required for lymphocyte chemoattractant factor-induced T lymphocyte migration. J. Biol. Chem. 270, 17081-17086.
    • Ryan T. C., Cruikshank W. W., Kornfeld H., Collins T. L. and Center D. M. (1995) The CD4-associated tyrosine kinase p56lck is required for lymphocyte chemoattractant factor-induced T lymphocyte migration. J. Biol. Chem. 270, 17081-17086.
  • 107
    • 0037097588 scopus 로고    scopus 로고
    • Lck is required for stromal cell-derived factor 1 alpha (CXCL12)-induced lymphoid cell chemotaxis
    • Inngjerdingen M., Torgersen K. M. and Maghazachi A. A. (2002) Lck is required for stromal cell-derived factor 1 alpha (CXCL12)-induced lymphoid cell chemotaxis. Blood. 99, 4318-4325.
    • (2002) Blood , vol.99 , pp. 4318-4325
    • Inngjerdingen, M.1    Torgersen, K.M.2    Maghazachi, A.A.3
  • 108
    • 11244275367 scopus 로고    scopus 로고
    • Stromal cell-derived factor-1alpha/CXCL12-induced chemotaxis of T cells involves activation of the RasGAP-associated docking protein p62Dok-1
    • Okabe S., Fukuda S., Kim Y. J., Niki M., Pelus L. M., Ohyashiki K., Pandolfi P. P. and Broxmeyer H. E. (2005) Stromal cell-derived factor-1alpha/CXCL12-induced chemotaxis of T cells involves activation of the RasGAP-associated docking protein p62Dok-1. Blood. 105, 474-480.
    • (2005) Blood , vol.105 , pp. 474-480
    • Okabe, S.1    Fukuda, S.2    Kim, Y.J.3    Niki, M.4    Pelus, L.M.5    Ohyashiki, K.6    Pandolfi, P.P.7    Broxmeyer, H.E.8
  • 111
    • 0032864092 scopus 로고    scopus 로고
    • LFA-1 to LFA-1 signals involve zeta-associated protein-70 (ZAP-70) tyrosine kinase: Relevance for invasion and migration of a T cell hybridoma
    • Soede R. D., Driessens M. H., Ruuls-Van Stalle L., Van Hulten P. E., Brink A. and Roos E. (1999) LFA-1 to LFA-1 signals involve zeta-associated protein-70 (ZAP-70) tyrosine kinase: relevance for invasion and migration of a T cell hybridoma. J. Immunol. 163, 4253-4261.
    • (1999) J. Immunol , vol.163 , pp. 4253-4261
    • Soede, R.D.1    Driessens, M.H.2    Ruuls-Van Stalle, L.3    Van Hulten, P.E.4    Brink, A.5    Roos, E.6
  • 112
    • 0035881927 scopus 로고    scopus 로고
    • Cutting edge: T cell migration regulated by CXCR4 chemokine receptor signaling to ZAP-70 tyrosine kinase
    • Ottoson N. C., Pribila J. T., Chan A. S. and Shimizu Y. (2001) Cutting edge: T cell migration regulated by CXCR4 chemokine receptor signaling to ZAP-70 tyrosine kinase. J. Immunol. 167, 1857-1861.
    • (2001) J. Immunol , vol.167 , pp. 1857-1861
    • Ottoson, N.C.1    Pribila, J.T.2    Chan, A.S.3    Shimizu, Y.4
  • 113
    • 0036566221 scopus 로고    scopus 로고
    • Signaling through ZAP-70 is required for CXCL12-mediated T-cell transendothelial migration
    • Ticchioni M., Charvet C., Noraz N., Lamy L., Steinberg M., Bernard A. and Deckert M. (2002) Signaling through ZAP-70 is required for CXCL12-mediated T-cell transendothelial migration. Blood. 99, 3111-3118.
    • (2002) Blood , vol.99 , pp. 3111-3118
    • Ticchioni, M.1    Charvet, C.2    Noraz, N.3    Lamy, L.4    Steinberg, M.5    Bernard, A.6    Deckert, M.7
  • 117
    • 33746648129 scopus 로고    scopus 로고
    • To stabilize neutrophil polarity, PIP3 and Cdc42 augment RhoA activity at the back as well as signals at the front
    • Van Keymeulen A., Wong K., Knight Z. A., Govaerts C., Hahn K. M., Shokat K. M. and Bourne H. R. (2006) To stabilize neutrophil polarity, PIP3 and Cdc42 augment RhoA activity at the back as well as signals at the front. J. Cell Biol. 174, 437-445.
    • (2006) J. Cell Biol , vol.174 , pp. 437-445
    • Van Keymeulen, A.1    Wong, K.2    Knight, Z.A.3    Govaerts, C.4    Hahn, K.M.5    Shokat, K.M.6    Bourne, H.R.7
  • 119
    • 22044432145 scopus 로고    scopus 로고
    • p85alpha subunit of class IA PI-3 kinase is crucial for macrophage growth and migration
    • Munugalavadla V., Borneo J., Ingram D. A. and Kapur R. (2005) p85alpha subunit of class IA PI-3 kinase is crucial for macrophage growth and migration. Blood. 106, 103-109.
    • (2005) Blood , vol.106 , pp. 103-109
    • Munugalavadla, V.1    Borneo, J.2    Ingram, D.A.3    Kapur, R.4
  • 121
    • 34250310465 scopus 로고    scopus 로고
    • Blockade of class IA phosphoinositide 3-kinase in neutrophils prevents NADPH oxidase activation- and adhesion-dependent inflammation
    • Gao X. P., Zhu X., Fu J., Liu Q., Frey R. S. and Malik A. B. (2007) Blockade of class IA phosphoinositide 3-kinase in neutrophils prevents NADPH oxidase activation- and adhesion-dependent inflammation. J. Biol. Chem. 282, 6116-6125.
    • (2007) J. Biol. Chem , vol.282 , pp. 6116-6125
    • Gao, X.P.1    Zhu, X.2    Fu, J.3    Liu, Q.4    Frey, R.S.5    Malik, A.B.6
  • 122
    • 0036631548 scopus 로고    scopus 로고
    • VAV proteins as signal integrators for multi-subunit immune-recognition receptors
    • Turner M. and Billadeau D. D. (2002) VAV proteins as signal integrators for multi-subunit immune-recognition receptors. Nat. Rev. Immunol. 2, 476-486.
    • (2002) Nat. Rev. Immunol , vol.2 , pp. 476-486
    • Turner, M.1    Billadeau, D.D.2
  • 123
    • 18144378805 scopus 로고    scopus 로고
    • Vav activation and function as a rac guanine nucleotide exchange factor in macrophage colony-stimulating factor-induced macrophage chemotaxis
    • Vedham V., Phee H. and Coggeshall K. M. (2005) Vav activation and function as a rac guanine nucleotide exchange factor in macrophage colony-stimulating factor-induced macrophage chemotaxis. Mol. Cell. Biol. 25, 4211-4220.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 4211-4220
    • Vedham, V.1    Phee, H.2    Coggeshall, K.M.3
  • 124
    • 0030221475 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinases
    • Banin S., Truong O., Katz D. R., Waterfield M. D., Brickell P. M. and Gout I. (1996) Wiskott-Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinases. Curr. Biol. 6, 981-988.
    • (1996) Curr. Biol , vol.6 , pp. 981-988
    • Banin, S.1    Truong, O.2    Katz, D.R.3    Waterfield, M.D.4    Brickell, P.M.5    Gout, I.6
  • 125
    • 0037160142 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein
    • Cory G. O., Garg R., Cramer R. and Ridley A. J. (2002) Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein. J. Biol. Chem. 277, 45115-45121.
    • (2002) J. Biol. Chem , vol.277 , pp. 45115-45121
    • Cory, G.O.1    Garg, R.2    Cramer, R.3    Ridley, A.J.4
  • 126
    • 4644328892 scopus 로고    scopus 로고
    • Paxillin: Adapting to change
    • Brown M. C. and Turner C. E. (2004) Paxillin: adapting to change. Physiol. Rev. 84, 1315-1339.
    • (2004) Physiol. Rev , vol.84 , pp. 1315-1339
    • Brown, M.C.1    Turner, C.E.2
  • 127
    • 0034651941 scopus 로고    scopus 로고
    • Lipopolysaccharide induces actin reorganization and tyrosine phosphorylation of Pyk2 and paxillin in monocytes and macrophages
    • Williams L. M. and Ridley A. J. (2000) Lipopolysaccharide induces actin reorganization and tyrosine phosphorylation of Pyk2 and paxillin in monocytes and macrophages. J. Immunol. 164, 2028-2036.
    • (2000) J. Immunol , vol.164 , pp. 2028-2036
    • Williams, L.M.1    Ridley, A.J.2
  • 128
    • 33750972608 scopus 로고    scopus 로고
    • CpG DNA enhances macrophage cell spreading by promoting the Src-family kinase-mediated phosphorylation of paxillin
    • Achuthan A., Elsegood C., Masendycz P., Hamilton J. A. and Scholz G. M. (2006) CpG DNA enhances macrophage cell spreading by promoting the Src-family kinase-mediated phosphorylation of paxillin. Cell Signal. 18, 2252-2261.
    • (2006) Cell Signal , vol.18 , pp. 2252-2261
    • Achuthan, A.1    Elsegood, C.2    Masendycz, P.3    Hamilton, J.A.4    Scholz, G.M.5
  • 129
    • 4344674527 scopus 로고    scopus 로고
    • Cortactin signalling and dynamic actin networks
    • Daly R. J. (2004) Cortactin signalling and dynamic actin networks. Biochem. J. 382, 13-25.
    • (2004) Biochem. J , vol.382 , pp. 13-25
    • Daly, R.J.1
  • 131
    • 47749084127 scopus 로고    scopus 로고
    • Pendergast A. M. and Zipfel P. (2006) Abl. UCSD-Nature Molecule Pages.
    • Pendergast A. M. and Zipfel P. (2006) Abl. UCSD-Nature Molecule Pages.
  • 132
    • 3342956520 scopus 로고    scopus 로고
    • Requirement for Abl kinases in T cell receptor signaling
    • Zipfel P. A., Zhang W., Quiroz M. and Pendergast A. M. (2004) Requirement for Abl kinases in T cell receptor signaling. Curr. Biol. 14, 1222-1231.
    • (2004) Curr. Biol , vol.14 , pp. 1222-1231
    • Zipfel, P.A.1    Zhang, W.2    Quiroz, M.3    Pendergast, A.M.4
  • 133
    • 34548492241 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated STAT5 accumulates on podosomes in Hck-transformed fibroblasts and chronic myeloid leukemia cells
    • Poincloux R., Cougoule C., Daubon T., Maridonneau-Parini I. and Le Cabec V. (2007) Tyrosine-phosphorylated STAT5 accumulates on podosomes in Hck-transformed fibroblasts and chronic myeloid leukemia cells. J. Cell Physiol. 213, 212-220.
    • (2007) J. Cell Physiol , vol.213 , pp. 212-220
    • Poincloux, R.1    Cougoule, C.2    Daubon, T.3    Maridonneau-Parini, I.4    Le Cabec, V.5
  • 134
    • 33847284434 scopus 로고    scopus 로고
    • A critical role for cortactin phosphorylation by Abl-family kinases in PDGF-induced dorsal-wave formation
    • Boyle S. N., Michaud G. A., Schweitzer B., Predki P. F. and Koleske A. J. (2007) A critical role for cortactin phosphorylation by Abl-family kinases in PDGF-induced dorsal-wave formation. Curr. Biol. 17, 445-451.
    • (2007) Curr. Biol , vol.17 , pp. 445-451
    • Boyle, S.N.1    Michaud, G.A.2    Schweitzer, B.3    Predki, P.F.4    Koleske, A.J.5
  • 135
    • 0028239549 scopus 로고
    • Physical and functional association of Src-related protein tyrosine kinases with Fc gamma RII in monocytic THP-1 cells
    • Ghazizadeh S., Bolen J. B. and Fleit H. B. (1994) Physical and functional association of Src-related protein tyrosine kinases with Fc gamma RII in monocytic THP-1 cells. J. Biol. Chem. 269, 8878-8884.
    • (1994) J. Biol. Chem , vol.269 , pp. 8878-8884
    • Ghazizadeh, S.1    Bolen, J.B.2    Fleit, H.B.3
  • 136
    • 0027318774 scopus 로고
    • Association of immunoglobulin GFc receptor II with Src-like protein-tyrosine kinase Fgr in neutrophils
    • Hamada F., Aoki M., Akiyama T. and Toyoshima K. (1993) Association of immunoglobulin GFc receptor II with Src-like protein-tyrosine kinase Fgr in neutrophils. Proc. Natl. Acad. Sci. U. S. A. 90, 6305-6309.
    • (1993) Proc. Natl. Acad. Sci. U. S. A , vol.90 , pp. 6305-6309
    • Hamada, F.1    Aoki, M.2    Akiyama, T.3    Toyoshima, K.4
  • 137
    • 0038549478 scopus 로고    scopus 로고
    • Signal transduction by immunoglobulin Fc receptors
    • Sanchez-Mejorada G. and Rosales C. (1998) Signal transduction by immunoglobulin Fc receptors. J. Leukoc. Biol. 63, 521-533.
    • (1998) J. Leukoc. Biol , vol.63 , pp. 521-533
    • Sanchez-Mejorada, G.1    Rosales, C.2
  • 138
    • 0028106837 scopus 로고
    • Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn
    • Wang A. V., Scholl P. R. and Geha R. S. (1994) Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn. J. Exp. Med. 180, 1165-1170.
    • (1994) J. Exp. Med , vol.180 , pp. 1165-1170
    • Wang, A.V.1    Scholl, P.R.2    Geha, R.S.3


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