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Volumn 18, Issue 8, 2006, Pages 1315-1325

Cbl and Akt regulate CXCL8-induced and CXCR1- and CXCR2-mediated chemotaxis

Author keywords

Akt; Cbl; Chemotaxis; CXCL8; CXCR1

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; CBL PROTEIN; CHEMOKINE RECEPTOR CXCR1; CHEMOKINE RECEPTOR CXCR2; INTERLEUKIN 8; LACTACYSTIN; MUTANT PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; PROTEASOME INHIBITOR; PROTEIN KINASE B; PROTEIN P85; PROTEIN TYROSINE KINASE INHIBITOR; TYRPHOSTIN;

EID: 33748473368     PISSN: 09538178     EISSN: 14602377     Source Type: Journal    
DOI: 10.1093/intimm/dxl064     Document Type: Article
Times cited : (29)

References (58)
  • 1
    • 0029856309 scopus 로고    scopus 로고
    • Chemokine receptors: Gateways to inflammation and infection
    • Premack, B. A. and Schall, T. J. 1996. Chemokine receptors: Gateways to inflammation and infection. Nat. Med. 2:1174.
    • (1996) Nat. Med. , vol.2 , pp. 1174
    • Premack, B.A.1    Schall, T.J.2
  • 2
    • 0029811733 scopus 로고    scopus 로고
    • Chemokine receptors and T cell chemotaxis
    • McKay, C. R. 1996. Chemokine receptors and T cell chemotaxis. J. Exp. Med. 84:799.
    • (1996) J. Exp. Med. , vol.84 , pp. 799
    • McKay, C.R.1
  • 3
    • 0030967081 scopus 로고    scopus 로고
    • Chemokines induce migrational responses in human breast carcinoma cell lines
    • Youngs, S. J., Ali, S. A., Taub, D. D. and Rees, R. C. 1997. Chemokines induce migrational responses in human breast carcinoma cell lines. Int. J. Cancer 71:257.
    • (1997) Int. J. Cancer , vol.71 , pp. 257
    • Youngs, S.J.1    Ali, S.A.2    Taub, D.D.3    Rees, R.C.4
  • 5
    • 0029826642 scopus 로고    scopus 로고
    • Eosinophil recruitment to the lung in a murine model of allergic inflammation. The role of T cells, chemokines, and adhesion receptors
    • Gonzalo, J. A., Lloyd, C. M., Kremer, L. et al. 1996. Eosinophil recruitment to the lung in a murine model of allergic inflammation. The role of T cells, chemokines, and adhesion receptors. J. Clin. Invest. 98:2332.
    • (1996) J. Clin. Invest. , vol.98 , pp. 2332
    • Gonzalo, J.A.1    Lloyd, C.M.2    Kremer, L.3
  • 6
    • 0023719346 scopus 로고
    • Molecular cloning of a human monocyte-derived neutrophil chemotactic factor (MDNCF) and the induction of MDNCF mRNA by interleukin 1 and tumor necrosis factor
    • Matsushima, K., Morishita, K., Yoshimura, T. et al. 1988. Molecular cloning of a human monocyte-derived neutrophil chemotactic factor (MDNCF) and the induction of MDNCF mRNA by interleukin 1 and tumor necrosis factor. J. Exp. Med. 167:1883.
    • (1988) J. Exp. Med. , vol.167 , pp. 1883
    • Matsushima, K.1    Morishita, K.2    Yoshimura, T.3
  • 7
    • 0028372188 scopus 로고
    • The immunopathology of chemotactic cytokines: The role of interleukin-8 and monocyte chemoattractant protein-1
    • Strieter, R. M., Koch, A. E., Antony, V. B., Fick, R. B., Jr, Standiford, T. J. and Kunkel, S. L. 1994. The immunopathology of chemotactic cytokines: The role of interleukin-8 and monocyte chemoattractant protein-1. J. Lab. Clin. Med. 123:183.
    • (1994) J Lab. Clin. Med. , vol.123 , pp. 183
    • Strieter, R.M.1    Koch, A.E.2    Antony, V.B.3    Fick Jr., R.B.4    Standiford, T.J.5    Kunkel, S.L.6
  • 8
    • 0037377567 scopus 로고    scopus 로고
    • Pathophysiological roles of interleukin-8/CXCL8 in pulmonary diseases
    • Mukaida, N. 2003. Pathophysiological roles of interleukin-8/CXCL8 in pulmonary diseases. Am. J. Physiol. Lung Cell. Mol. Physiol. 284:L566.
    • (2003) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.284
    • Mukaida, N.1
  • 9
    • 0036149025 scopus 로고    scopus 로고
    • The role of chemokines in human cardiovascular pathology: Enhanced biological insights
    • Shin, W. S., Szuba, A. and Rockson, S. G. 2002. The role of chemokines in human cardiovascular pathology: Enhanced biological insights. Atherosclerosis 160:91.
    • (2002) Atherosclerosis , vol.160 , pp. 91
    • Shin, W.S.1    Szuba, A.2    Rockson, S.G.3
  • 10
    • 0034849755 scopus 로고    scopus 로고
    • Interleukin-8 and human cancer biology
    • Xie, K. 2001. Interleukin-8 and human cancer biology. Cytokine Growth Factor Rev. 12:375.
    • (2001) Cytokine Growth Factor Rev. , vol.12 , pp. 375
    • Xie, K.1
  • 11
    • 1942444566 scopus 로고    scopus 로고
    • Alpha-chemokine-mediated signal transduction in human Kaposi's sarcoma spindle cells
    • Wang, J. F., Liu, Z. Y., Anand, A. R. et al. 2004. Alpha-chemokine-mediated signal transduction in human Kaposi's sarcoma spindle cells. Biochim. Biophys. Acta 1691:129.
    • (2004) Biochim. Biophys. Acta , vol.1691 , pp. 129
    • Wang, J.F.1    Liu, Z.Y.2    Anand, A.R.3
  • 12
    • 0030825407 scopus 로고    scopus 로고
    • Chemokines
    • Rollins, B. J. 1997. Chemokines. Blood 90:909.
    • (1997) Blood , vol.90 , pp. 909
    • Rollins, B.J.1
  • 13
    • 0029073649 scopus 로고
    • Regulation of the expression of the IL-8 receptor A/B by IL-8: Possible functions of each receptor
    • Chuntharapai, A. and Kim, K. J. 1995. Regulation of the expression of the IL-8 receptor A/B by IL-8: Possible functions of each receptor. J. Immunol. 155:2587.
    • (1995) J. Immunol. , vol.155 , pp. 2587
    • Chuntharapai, A.1    Kim, K.J.2
  • 14
    • 0037443760 scopus 로고    scopus 로고
    • IL-8 directly enhanced endothelial cell survival, proliferation, and matrix metalloproteinases production and regulated angiogenesis
    • Li, A., Dubey, S., Varney, M. L., Dave, B. J. and Singh, R. K. 2003. IL-8 directly enhanced endothelial cell survival, proliferation, and matrix metalloproteinases production and regulated angiogenesis. J. Immunol. 170:3369.
    • (2003) J. Immunol. , vol.170 , pp. 3369
    • Li, A.1    Dubey, S.2    Varney, M.L.3    Dave, B.J.4    Singh, R.K.5
  • 15
    • 0034792393 scopus 로고    scopus 로고
    • Expression of interleukin 8 and its receptors in human colon carcinoma cells with different metastatic potentials
    • Li, A., Varney, M. L. and Singh, R. K. 2001. Expression of interleukin 8 and its receptors in human colon carcinoma cells with different metastatic potentials. Clin. Cancer Res. 10:3298.
    • (2001) Clin. Cancer Res. , vol.10 , pp. 3298
    • Li, A.1    Varney, M.L.2    Singh, R.K.3
  • 16
    • 1842474888 scopus 로고    scopus 로고
    • Tissue factor-factor VIIa-specific up-regulation of IL-8 expression in MDAMB-231 cells is mediated by PAR-2 and results in increased cell migration
    • Hjortoe, G. M., Petersen, L. C., Albrektsen, T. et al. 2004. Tissue factor-factor VIIa-specific up-regulation of IL-8 expression in MDAMB-231 cells is mediated by PAR-2 and results in increased cell migration. Blood 103:3029.
    • (2004) Blood , vol.103 , pp. 3029
    • Hjortoe, G.M.1    Petersen, L.C.2    Albrektsen, T.3
  • 17
    • 0032562568 scopus 로고    scopus 로고
    • Independent regulation by phosphorylation. Multiple signaling pathways of human interleukin-8 receptor A. Independent regulation by phosphorylation
    • Richardson, R. M., Ali, H., Pridgen, B. C. et al. 1998. Independent regulation by phosphorylation. Multiple signaling pathways of human interleukin-8 receptor A. Independent regulation by phosphorylation. J. Biol. Chem. 273:10690.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10690
    • Richardson, R.M.1    Ali, H.2    Pridgen, B.C.3
  • 19
    • 0037200090 scopus 로고    scopus 로고
    • Identification of a signal transduction switch in the chemokine receptor CXCR1
    • Suetomi, K., Rojo, D. and Navarro, J. 2002. Identification of a signal transduction switch in the chemokine receptor CXCR1. J. Biol. Chem. 277:1526.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1526
    • Suetomi, K.1    Rojo, D.2    Navarro, J.3
  • 20
    • 0037443490 scopus 로고    scopus 로고
    • Role of the cytoplasmic tails of CXCR1 and CXCR2 in mediating leukocyte migration, activation, and regulation
    • Richardson, R. M., Marjooram, R. J., Barak, L. S. and Snyderman, R. 2003. Role of the cytoplasmic tails of CXCR1 and CXCR2 in mediating leukocyte migration, activation, and regulation. J. Immunol. 170:2904.
    • (2003) J. Immunol. , vol.170 , pp. 2904
    • Richardson, R.M.1    Marjooram, R.J.2    Barak, L.S.3    Snyderman, R.4
  • 21
    • 0035316576 scopus 로고    scopus 로고
    • Cbl: Many adaptations to regulate protein tyrosine kinases
    • Thien, C. B. and Langdon, W. Y. 2001. Cbl: Many adaptations to regulate protein tyrosine kinases. Nat. Rev. Mol. Cell Biol. 2:294.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 294
    • Thien, C.B.1    Langdon, W.Y.2
  • 22
    • 0037401969 scopus 로고    scopus 로고
    • Expression and tyrosine phosphorylation of Cbl regulates macrophage chemokinetic and chemotactic movement
    • Caveggion, E., Continolo, S., Pixley, F. J. et al. 2003. Expression and tyrosine phosphorylation of Cbl regulates macrophage chemokinetic and chemotactic movement. J. Cell Physiol. 195:276.
    • (2003) J. Cell Physiol. , vol.195 , pp. 276
    • Caveggion, E.1    Continolo, S.2    Pixley, F.J.3
  • 23
    • 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. et al. 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.
    • (2001) J. Cell Biol. , vol.152 , pp. 181
    • Sanjay, A.1    Houghton, A.2    Neff, L.3
  • 24
    • 0030903025 scopus 로고    scopus 로고
    • Interleukin 8-stimulated phosphatidylinositol-3-kinase activity regulates the migration of human neutrophils independent of extracellular signal-regulated kinase and p38 mitogen-activated protein kinases
    • Knall, C., Worthen, G. S. and Johnson, G. L. 1997. Interleukin 8-stimulated phosphatidylinositol-3-kinase activity regulates the migration of human neutrophils independent of extracellular signal-regulated kinase and p38 mitogen-activated protein kinases. Proc. Natl Acad. Sci. USA 94:3052.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3052
    • Knall, C.1    Worthen, G.S.2    Johnson, G.L.3
  • 25
    • 0033486065 scopus 로고    scopus 로고
    • The CXC chemokine stromal cell-derived factor activates a Gicoupled phosphoinositide 3-kinase in T lymphocytes
    • Sotsios, Y., Whittaker, G. C., Westwick, J. and Ward, S. G. 1999. The CXC chemokine stromal cell-derived factor activates a Gicoupled phosphoinositide 3-kinase in T lymphocytes. J. Immunol. 163:5954.
    • (1999) J. Immunol. , vol.163 , pp. 5954
    • Sotsios, Y.1    Whittaker, G.C.2    Westwick, J.3    Ward, S.G.4
  • 26
    • 0034618052 scopus 로고    scopus 로고
    • Signal transduction by CXC chemokine receptor 4. Stromal cell-derived factor 1 stimulates prolonged protein kinase B and extracellular signal regulated kinase 2 activation in T lymphocytes
    • Tilton, B., Ho, L., Oberlin, E. et al. 2000. Signal transduction by CXC chemokine receptor 4. Stromal cell-derived factor 1 stimulates prolonged protein kinase B and extracellular signal regulated kinase 2 activation in T lymphocytes. J. Exp. Med. 192:313.
    • (2000) J. Exp. Med. , vol.192 , pp. 313
    • Tilton, B.1    Ho, L.2    Oberlin, E.3
  • 27
    • 0036172306 scopus 로고    scopus 로고
    • Chemokine signalling: Pivoting around multiple phosphoinositide 3-kinases
    • Curnock, A. P., Logan, M. K. and Ward, S. G. 2002. Chemokine signalling: pivoting around multiple phosphoinositide 3-kinases. Immunology 105:125.
    • (2002) Immunology , vol.105 , pp. 125
    • Curnock, A.P.1    Logan, M.K.2    Ward, S.G.3
  • 28
    • 0037694090 scopus 로고    scopus 로고
    • A regulator of G protein signaling containing kinase is important for chemotaxis and multicellular development in dictyostelium
    • Sun, B. and Firtel, R. A. 2003. A regulator of G protein signaling containing kinase is important for chemotaxis and multicellular development in dictyostelium. Mol. Biol. Cell 14:1727.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1727
    • Sun, B.1    Firtel, R.A.2
  • 29
    • 0034635513 scopus 로고    scopus 로고
    • Polarization of chemoattractant receptor signaling during neutrophil chemotaxis
    • Servant, G., Weiner, O. D., Herzmark, P., Balla, T., Sedat, J. W. and Bourne, H. R. 2000. Polarization of chemoattractant receptor signaling during neutrophil chemotaxis. Science 287:1037.
    • (2000) Science , vol.287 , pp. 1037
    • Servant, G.1    Weiner, O.D.2    Herzmark, P.3    Balla, T.4    Sedat, J.W.5    Bourne, H.R.6
  • 30
    • 0037124110 scopus 로고    scopus 로고
    • CXCR4/CCR5 down-modulation and chemotaxis are regulated by the proteasome pathway
    • Fernandis, A. Z., Cherla, R. P., Chernock, R. D. and Ganju, R. K. 2002. CXCR4/CCR5 down-modulation and chemotaxis are regulated by the proteasome pathway. J. Biol. Chem. 277: 18111.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18111
    • Fernandis, A.Z.1    Cherla, R.P.2    Chernock, R.D.3    Ganju, R.K.4
  • 31
    • 0032752657 scopus 로고    scopus 로고
    • Role of the tyrosine kinase pyk2 in the integrin-dependent activation of human neutrophils by TNF
    • Fuortes, M., Melchior, M., Han, H., Lyon, G. J. and Nathan, C. 1999. Role of the tyrosine kinase pyk2 in the integrin-dependent activation of human neutrophils by TNF. J. Clin. Invest. 104:327.
    • (1999) J. Clin. Invest. , vol.104 , pp. 327
    • Fuortes, M.1    Melchior, M.2    Han, H.3    Lyon, G.J.4    Nathan, C.5
  • 32
    • 0025791955 scopus 로고
    • Separation of leukocytes: Improved cell purity by fine adjustments of gradient medium density and osmolality
    • Boyum, A., Lovhaug, D., Tresland, L. and Nordlie, E. M. 1991. Separation of leukocytes: Improved cell purity by fine adjustments of gradient medium density and osmolality. Scand. J. Immunol. 34:697.
    • (1991) Scand. J. Immunol. , vol.34 , pp. 697
    • Boyum, A.1    Lovhaug, D.2    Tresland, L.3    Nordlie, E.M.4
  • 33
    • 1842591231 scopus 로고    scopus 로고
    • Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases
    • Marmor, M. D. and Yarden, Y. 2004. Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases. Oncogene 23:2057.
    • (2004) Oncogene , vol.23 , pp. 2057
    • Marmor, M.D.1    Yarden, Y.2
  • 34
    • 0037146798 scopus 로고    scopus 로고
    • Immunoblotting and sequential lysis protocols for the analysis of tyrosine phosphorylation-dependent signaling
    • Gilbert, C., Rollet-Labelle, E., Caon, A. C. and Naccache, P. H. 2002. Immunoblotting and sequential lysis protocols for the analysis of tyrosine phosphorylation-dependent signaling. J. Immunol. Methods 271:185.
    • (2002) J. Immunol. Methods , vol.271 , pp. 185
    • Gilbert, C.1    Rollet-Labelle, E.2    Caon, A.C.3    Naccache, P.H.4
  • 35
    • 0031818061 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase activation mediates PDGF-directed migration of RPE cells
    • Hinton, D. R., He, S., Graf, K. et al. 1998. Mitogen-activated protein kinase activation mediates PDGF-directed migration of RPE cells. Exp. Cell Res. 239:11.
    • (1998) Exp. Cell Res. , vol.239 , pp. 11
    • Hinton, D.R.1    He, S.2    Graf, K.3
  • 36
    • 0033179690 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase regulates eotaxin-induced eosinophil migration
    • Boehme, S. A., Sullivan, S. K., Crowe, P. D. et al. 1999. Activation of mitogen-activated protein kinase regulates eotaxin-induced eosinophil migration. J. Immunol. 163:1611.
    • (1999) J. Immunol. , vol.163 , pp. 1611
    • Boehme, S.A.1    Sullivan, S.K.2    Crowe, P.D.3
  • 38
    • 0028958812 scopus 로고
    • A comparison of post-receptor signal transduction events in Jurkat cells transfected with either IL-8R1 or IL-8R2. Chemokine mediated activation of p42/p44 MAP-kinase (ERK-2)
    • Jones, S. A., Moser, B. and Thelen, M. 1995. A comparison of post-receptor signal transduction events in Jurkat cells transfected with either IL-8R1 or IL-8R2. Chemokine mediated activation of p42/p44 MAP-kinase (ERK-2). FEBS Lett. 364:211.
    • (1995) FEBS Lett. , vol.364 , pp. 211
    • Jones, S.A.1    Moser, B.2    Thelen, M.3
  • 40
    • 0037126634 scopus 로고    scopus 로고
    • The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation
    • Rao, N., Ghosh, A. K., Ota, S. et al. 2001. The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation. EMBO J. 20:7085.
    • (2001) EMBO J. , vol.20 , pp. 7085
    • Rao, N.1    Ghosh, A.K.2    Ota, S.3
  • 41
    • 0032217156 scopus 로고    scopus 로고
    • c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor
    • Levkowitz, G., Waterman, H., Zamir, E. et al. 1998. c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor. Genes Dev. 12:3663.
    • (1998) Genes Dev. , vol.12 , pp. 3663
    • Levkowitz, G.1    Waterman, H.2    Zamir, E.3
  • 42
    • 0034680045 scopus 로고    scopus 로고
    • The protooncogene c-Cbl is a positive regulator of Met-induced MAP kinase activation: A role for the adaptor protein Crk
    • Garcia-Guzman, M., Larsen, E. and Vuori, K. 2000. The protooncogene c-Cbl is a positive regulator of Met-induced MAP kinase activation: A role for the adaptor protein Crk. Oncogene 19:4058.
    • (2000) Oncogene , vol.19 , pp. 4058
    • Garcia-Guzman, M.1    Larsen, E.2    Vuori, K.3
  • 43
    • 0033602144 scopus 로고    scopus 로고
    • A direct interaction between the adaptor protein Cbl-b and the kinase zap-70 induces a positive signal in T cells
    • Zhang, Z., Elly, C., Qiu, L., Altman, A. and Liu, Y. C. 1999. A direct interaction between the adaptor protein Cbl-b and the kinase zap-70 induces a positive signal in T cells. Curr. Biol. 9:203.
    • (1999) Curr. Biol. , vol.9 , pp. 203
    • Zhang, Z.1    Elly, C.2    Qiu, L.3    Altman, A.4    Liu, Y.C.5
  • 44
    • 0141866846 scopus 로고    scopus 로고
    • Cbl-mediated ubiquitinylation and negative regulation of Vav
    • Miura-Shimura, Y., Duan, L., Rao, N. L. et al. 2003. Cbl-mediated ubiquitinylation and negative regulation of Vav. J. Biol. Chem. 278:38495.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38495
    • Miura-Shimura, Y.1    Duan, L.2    Rao, N.L.3
  • 45
    • 3142618052 scopus 로고    scopus 로고
    • Regulation of ubiquitin protein-ligase activity in c-Cbl by phosphorylation-induced conformational change, and constitutive activation by tyrosine to glutamate point mutations
    • Kassenbrock, C. K. and Anderson, S. M. 2004. Regulation of ubiquitin protein-ligase activity in c-Cbl by phosphorylation-induced conformational change, and constitutive activation by tyrosine to glutamate point mutations. J. Biol. Chem. 279:28017.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28017
    • Kassenbrock, C.K.1    Anderson, S.M.2
  • 46
    • 1942484383 scopus 로고    scopus 로고
    • Engagement of beta2 integrins recruits 14-3-3 proteins to c-Cbl in human neutrophils
    • Melander, F., Andersson, T. and Dib, K. 2004. Engagement of beta2 integrins recruits 14-3-3 proteins to c-Cbl in human neutrophils. Biochem. Biophys. Res. Commun. 317:1000.
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 1000
    • Melander, F.1    Andersson, T.2    Dib, K.3
  • 47
    • 0033615732 scopus 로고    scopus 로고
    • Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7
    • Yokouchi, M., Kondo, T., Houghton, A. et al. 1999. Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7. J. Biol. Chem. 274:31707.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31707
    • Yokouchi, M.1    Kondo, T.2    Houghton, A.3
  • 48
    • 2542501657 scopus 로고    scopus 로고
    • Ubiquitin ligases and the immune response
    • Liu, Y. C. 2004. Ubiquitin ligases and the immune response. Annu. Rev. Immunol. 22:81.
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 81
    • Liu, Y.C.1
  • 49
    • 0033574539 scopus 로고    scopus 로고
    • Role of clathrin-mediated endocytosis in CXCR2 sequestration, resensitization, and signal transduction
    • Yang, W., Wang, D. and Richmond, A. 1999. Role of clathrin-mediated endocytosis in CXCR2 sequestration, resensitization, and signal transduction. J. Biol. Chem. 274:11328.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11328
    • Yang, W.1    Wang, D.2    Richmond, A.3
  • 50
    • 0034161622 scopus 로고    scopus 로고
    • GCP-2-induced internalization of IL-8 receptors: Hierarchical relationships between GCP-2 and other ELR(+)-CXC chemokines and mechanisms regulating CXCR2 internalization and recycling
    • Feniger-Barish, R., Belkin, D., Zaslaver, A. et al. 2002. GCP-2-induced internalization of IL-8 receptors: Hierarchical relationships between GCP-2 and other ELR(+)-CXC chemokines and mechanisms regulating CXCR2 internalization and recycling. Blood 95:1551.
    • (2002) Blood , vol.95 , pp. 1551
    • Feniger-Barish, R.1    Belkin, D.2    Zaslaver, A.3
  • 51
    • 0035936552 scopus 로고    scopus 로고
    • Identification of a motif in the carboxyl terminus of CXCR2 that is involved in adaptin 2 binding and receptor internalization
    • Fan, G. H., Yang,W., Wang, X. J., Qian, Q. and Richmond, A. 2001. Identification of a motif in the carboxyl terminus of CXCR2 that is involved in adaptin 2 binding and receptor internalization. Biochemistry 40:791.
    • (2001) Biochemistry , vol.40 , pp. 791
    • Fan, G.H.1    Yang, W.2    Wang, X.J.3    Qian, Q.4    Richmond, A.5
  • 52
    • 0037155284 scopus 로고    scopus 로고
    • Hsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and trafficking
    • Fan, G. H., Yang, W., Sai, J. and Richmond, A. 2002. Hsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and trafficking. J. Biol. Chem. 277:6590.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6590
    • Fan, G.H.1    Yang, W.2    Sai, J.3    Richmond, A.4
  • 53
    • 2342570318 scopus 로고    scopus 로고
    • Rab11-family interacting protein 2 and myosin Vb are required for CXCR2 recycling and receptor-mediated chemotaxis
    • Fan, G. H., Lapierre, L. A., Goldenring, J. R., Sai, J. and Richmond, A. 2004. Rab11-family interacting protein 2 and myosin Vb are required for CXCR2 recycling and receptor-mediated chemotaxis. Mol. Biol. Cell 15:2456.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2456
    • Fan, G.H.1    Lapierre, L.A.2    Goldenring, J.R.3    Sai, J.4    Richmond, A.5
  • 54
    • 0036497956 scopus 로고    scopus 로고
    • Dysregulation of phosphatidylinositol 3-kinase and downstream effectors in human breast cancer
    • Salh, B., Marotta, A., Wagey, R., Sayed, M. and Pelech, S. 2002. Dysregulation of phosphatidylinositol 3-kinase and downstream effectors in human breast cancer. Int. J. Cancer 98:148.
    • (2002) Int. J. Cancer , vol.98 , pp. 148
    • Salh, B.1    Marotta, A.2    Wagey, R.3    Sayed, M.4    Pelech, S.5
  • 56
    • 0033980846 scopus 로고    scopus 로고
    • c-Cbl localizes to actin lamellae and regulates lamellipodia formation and cell morphology
    • Scaife, R. M. and Langdon, W. Y. 2000. c-Cbl localizes to actin lamellae and regulates lamellipodia formation and cell morphology. J. Cell Sci. 113:215.
    • (2000) J. Cell Sci. , vol.113 , pp. 215
    • Scaife, R.M.1    Langdon, W.Y.2
  • 57
    • 21844437618 scopus 로고    scopus 로고
    • Dynamin forms a Src kinase-sensitive complex with Cbl and regulates podosomes and osteoclast activity
    • Bruzzanitim, A., Neff, L., Sanjay, A., Horne,W. C., De Camilli, P. and Baron, R. 2005. Dynamin forms a Src kinase-sensitive complex with Cbl and regulates podosomes and osteoclast activity. Mol. Biol. Cell 16:3301.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3301
    • Bruzzanitim, A.1    Neff, L.2    Sanjay, A.3    Horne, W.C.4    De Camilli, P.5    Baron, R.6
  • 58
    • 0032509512 scopus 로고    scopus 로고
    • Growth hormone stimulates the formation of a multiprotein signaling complex involving p130(Cas) and Crk II. Resultant activation of c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK)
    • Zhu, T., Goh, E. L., LeRoith, D. and Lobie, P. E. 1998. Growth hormone stimulates the formation of a multiprotein signaling complex involving p130(Cas) and Crk II. Resultant activation of c-Jun N-terminal kinase/ stress-activated protein kinase (JNK/SAPK). J. Biol. Chem. 273:33864
    • (1998) J. Biol. Chem. , vol.273 , pp. 33864
    • Zhu, T.1    Goh, E.L.2    LeRoith, D.3    Lobie, P.E.4


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