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Volumn 7, Issue 6, 2012, Pages

Extracellular IgC2 constant domains of CEACAMs mediate PI3K sensitivity during uptake of pathogens

Author keywords

[No Author keywords available]

Indexed keywords

CARCINOEMBRYONIC ANTIGEN; CARCINOEMBRYONIC ANTIGEN RELATED CELL ADHESION MOLECULE; CARCINOEMBRYONIC ANTIGEN RELATED CELL ADHESION MOLECULE 1; CARCINOEMBRYONIC ANTIGEN RELATED CELL ADHESION MOLECULE 3; CARCINOEMBRYONIC ANTIGEN RELATED CELL ADHESION MOLECULE 6; CHOLESTEROL; IMMUNOGLOBULIN; IMMUNOGLOBULIN C2 CONSTANT DOMAIN; LYMPHOCYTE ANTIGEN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN SHIP; UNCLASSIFIED DRUG; CD66 ANTIGENS; CELL ADHESION MOLECULE; INOSITOL 1,4,5 TRISPHOSPHATE 5 PHOSPHATASE; INOSITOL-1,4,5-TRISPHOSPHATE 5-PHOSPHATASE; LEUKOCYTE ANTIGEN; MUTANT PROTEIN; PHOSPHATASE; PHOSPHATIDYLINOSITOL 3,4,5-TRIPHOSPHATE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; POLYPHOSPHOINOSITIDE; RECOMBINANT PROTEIN;

EID: 84863098023     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0039908     Document Type: Article
Times cited : (18)

References (65)
  • 1
    • 26244455894 scopus 로고    scopus 로고
    • Identification of a novel group of evolutionarily conserved members within the rapidly diverging murine Cea family
    • Zebhauser R, Kammerer R, Eisenried A, McLellan A, Moore T, et al. (2005) Identification of a novel group of evolutionarily conserved members within the rapidly diverging murine Cea family. Genomics 86: 566-580.
    • (2005) Genomics , vol.86 , pp. 566-580
    • Zebhauser, R.1    Kammerer, R.2    Eisenried, A.3    McLellan, A.4    Moore, T.5
  • 2
    • 33748310638 scopus 로고    scopus 로고
    • CEACAMs - their role in physiology and pathophysiology
    • Kuespert K, Pils S, Hauck CR, (2006) CEACAMs - their role in physiology and pathophysiology. Curr. Opin Cell Biol 18: 565-571.
    • (2006) Curr. Opin Cell Biol , vol.18 , pp. 565-571
    • Kuespert, K.1    Pils, S.2    Hauck, C.R.3
  • 3
    • 0042620298 scopus 로고    scopus 로고
    • Membrane proteins with immunoglobulin-like domains-a master superfamily of interaction molecules
    • Barclay AN, (2003) Membrane proteins with immunoglobulin-like domains-a master superfamily of interaction molecules. Semin Immunol 15: 215-223.
    • (2003) Semin Immunol , vol.15 , pp. 215-223
    • Barclay, A.N.1
  • 4
    • 50049112697 scopus 로고    scopus 로고
    • CEACAM3: an innate immune receptor directed against human-resticted bacterial pathogens
    • Pils S, Gerrard D, Meyer A, Hauck CR (2008) CEACAM3: an innate immune receptor directed against human-resticted bacterial pathogens. Intl J Med Microbiol 298: 553-560.
    • (2008) Intl J Med Microbiol , vol.298 , pp. 553-560
    • Pils, S.1    Gerrard, D.2    Meyer, A.3    Hauck, C.R.4
  • 5
    • 0029905022 scopus 로고    scopus 로고
    • CGM1a antigen of neutrophils, a receptor of gonococcal opacity proteins
    • Chen T, Gotschlich EC, (1996) CGM1a antigen of neutrophils, a receptor of gonococcal opacity proteins. Proc Natl Acad Sci USA 93: 14851-14856.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14851-14856
    • Chen, T.1    Gotschlich, E.C.2
  • 6
    • 0029844602 scopus 로고    scopus 로고
    • The N-domain of the human CD66a adhesion molecule is a target for Opa proteins of Neisseria meningitidis and Neisseria gonorrhoeae
    • Virji M, Watt SM, Barker S, Makepeace K, Doyonnas R, (1996) The N-domain of the human CD66a adhesion molecule is a target for Opa proteins of Neisseria meningitidis and Neisseria gonorrhoeae. Mol Microbiol 22: 929-939.
    • (1996) Mol Microbiol , vol.22 , pp. 929-939
    • Virji, M.1    Watt, S.M.2    Barker, S.3    Makepeace, K.4    Doyonnas, R.5
  • 7
    • 0030924679 scopus 로고    scopus 로고
    • Several carcinoembryonic antigens (CD66) serve as receptors for gonococcal opacity proteins
    • Chen T, Grunert F, Medina-Marino A, Gotschlich EC, (1997) Several carcinoembryonic antigens (CD66) serve as receptors for gonococcal opacity proteins. J Exp Med 185: 1557-1564.
    • (1997) J Exp Med , vol.185 , pp. 1557-1564
    • Chen, T.1    Grunert, F.2    Medina-Marino, A.3    Gotschlich, E.C.4
  • 8
    • 0037384724 scopus 로고    scopus 로고
    • A novel cell-binding mechanism of Moraxella catarrhalis ubiquitous surface protein UspA: specific targeting of the N-domain of carcinoembryonic antigen-related cell adhesion molecules by UspA1
    • Hill DJ, Virji M, (2003) A novel cell-binding mechanism of Moraxella catarrhalis ubiquitous surface protein UspA: specific targeting of the N-domain of carcinoembryonic antigen-related cell adhesion molecules by UspA1. Mol Microbiol 48: 117-129.
    • (2003) Mol Microbiol , vol.48 , pp. 117-129
    • Hill, D.J.1    Virji, M.2
  • 9
    • 0035139679 scopus 로고    scopus 로고
    • Expression of pathogen-like Opa adhesins in commensal Neisseria: genetic and functional analysis
    • Toleman M, Aho E, Virji M, (2001) Expression of pathogen-like Opa adhesins in commensal Neisseria: genetic and functional analysis. Cell Microbiol 3: 33-44.
    • (2001) Cell Microbiol , vol.3 , pp. 33-44
    • Toleman, M.1    Aho, E.2    Virji, M.3
  • 10
    • 3142721456 scopus 로고    scopus 로고
    • Differential recognition of members of the carcinoembryonic antigen family by Afa/Dr adhesins of diffusely adhering Escherichia coli (Afa/Dr DAEC)
    • Berger CN, Billker O, Meyer TF, Servin AL, Kansau I, (2004) Differential recognition of members of the carcinoembryonic antigen family by Afa/Dr adhesins of diffusely adhering Escherichia coli (Afa/Dr DAEC). Mol Microbiol 52: 963-983.
    • (2004) Mol Microbiol , vol.52 , pp. 963-983
    • Berger, C.N.1    Billker, O.2    Meyer, T.F.3    Servin, A.L.4    Kansau, I.5
  • 12
    • 24144490843 scopus 로고    scopus 로고
    • CEACAM engagement by human pathogens enhances cell adhesion and counteracts bacteria-induced detachment of epithelial cells
    • Muenzner P, Rohde M, Kneitz S, Hauck CR, (2005) CEACAM engagement by human pathogens enhances cell adhesion and counteracts bacteria-induced detachment of epithelial cells. J Cell Biol 170: 825-836.
    • (2005) J Cell Biol , vol.170 , pp. 825-836
    • Muenzner, P.1    Rohde, M.2    Kneitz, S.3    Hauck, C.R.4
  • 13
    • 77956296581 scopus 로고    scopus 로고
    • Human-specific bacterial pathogens block shedding of epithelial cells by stimulating integrin activation
    • Muenzner P, Bachmann V, Hentschel J, Zimmermann W, Hauck CR, (2010) Human-specific bacterial pathogens block shedding of epithelial cells by stimulating integrin activation. Science 329: 1197-1201.
    • (2010) Science , vol.329 , pp. 1197-1201
    • Muenzner, P.1    Bachmann, V.2    Hentschel, J.3    Zimmermann, W.4    Hauck, C.R.5
  • 14
    • 0031011324 scopus 로고    scopus 로고
    • Differential recognition of members of the carcinoembryonic antigen family by Opa variants of Neisseria gonorrhoeae
    • Bos MP, Grunert F, Belland RJ, (1997) Differential recognition of members of the carcinoembryonic antigen family by Opa variants of Neisseria gonorrhoeae. Infect Immun 65: 2353-2361.
    • (1997) Infect Immun , vol.65 , pp. 2353-2361
    • Bos, M.P.1    Grunert, F.2    Belland, R.J.3
  • 15
    • 0030709395 scopus 로고    scopus 로고
    • Differential Opa specificities for CD66 receptors influence tissue interactions and cellular response to Neisseria gonorrhoeae
    • Gray-Owen SD, Lorenzen DR, Haude A, Meyer TF, Dehio C, (1997) Differential Opa specificities for CD66 receptors influence tissue interactions and cellular response to Neisseria gonorrhoeae. Mol Microbiol 26: 971-980.
    • (1997) Mol Microbiol , vol.26 , pp. 971-980
    • Gray-Owen, S.D.1    Lorenzen, D.R.2    Haude, A.3    Meyer, T.F.4    Dehio, C.5
  • 16
    • 0032518818 scopus 로고    scopus 로고
    • CD66-mediated phagocytosis of Opa52 Neisseria gonorrhoeae requires a Src-like tyrosine kinase- and Rac1-dependent signalling pathway
    • Hauck CR, Meyer TF, Lang F, Gulbins E, (1998) CD66-mediated phagocytosis of Opa52 Neisseria gonorrhoeae requires a Src-like tyrosine kinase- and Rac1-dependent signalling pathway. EMBO J 17: 443-454.
    • (1998) EMBO J , vol.17 , pp. 443-454
    • Hauck, C.R.1    Meyer, T.F.2    Lang, F.3    Gulbins, E.4
  • 17
    • 0034079012 scopus 로고    scopus 로고
    • Carcinoembryonic antigen family receptor specificity of Neisseria meningitidis Opa variants influences adherence to and invasion of proinflammatory cytokine-activated endothelial cells
    • Muenzner P, Dehio C, Fujiwara T, Achtman M, Meyer TF, et al. (2000) Carcinoembryonic antigen family receptor specificity of Neisseria meningitidis Opa variants influences adherence to and invasion of proinflammatory cytokine-activated endothelial cells. Infect Immun 68: 3601-3607.
    • (2000) Infect Immun , vol.68 , pp. 3601-3607
    • Muenzner, P.1    Dehio, C.2    Fujiwara, T.3    Achtman, M.4    Meyer, T.F.5
  • 18
    • 33845382232 scopus 로고    scopus 로고
    • Co-ordinate action of bacterial adhesins and human carcinoembryonic antigen receptors in enhanced cellular invasion by capsulate serum resistant Neisseria meningitidis
    • Rowe HA, Griffiths NJ, Hill DJ, Virji M, (2007) Co-ordinate action of bacterial adhesins and human carcinoembryonic antigen receptors in enhanced cellular invasion by capsulate serum resistant Neisseria meningitidis. Cell Microbiol 9: 154-168.
    • (2007) Cell Microbiol , vol.9 , pp. 154-168
    • Rowe, H.A.1    Griffiths, N.J.2    Hill, D.J.3    Virji, M.4
  • 19
    • 0031736077 scopus 로고    scopus 로고
    • Opa binding to cellular CD66 receptors mediates the transcellular traversal of Neisseria gonorrhoeae across polarized T84 epithelial cell monolayers
    • Wang J, Gray-Owen SD, Knorre A, Meyer TF, Dehio C, (1998) Opa binding to cellular CD66 receptors mediates the transcellular traversal of Neisseria gonorrhoeae across polarized T84 epithelial cell monolayers. Mol Microbiol 30: 657-671.
    • (1998) Mol Microbiol , vol.30 , pp. 657-671
    • Wang, J.1    Gray-Owen, S.D.2    Knorre, A.3    Meyer, T.F.4    Dehio, C.5
  • 20
    • 39849096279 scopus 로고    scopus 로고
    • Cytoskeleton and motor proteins are required for the transcytosis of Neisseria gonorrhoeae through polarized epithelial cells
    • Wang JA, Meyer TF, Rudel T, (2007) Cytoskeleton and motor proteins are required for the transcytosis of Neisseria gonorrhoeae through polarized epithelial cells. Int J Med Microbiol 298: 209-221.
    • (2007) Int J Med Microbiol , vol.298 , pp. 209-221
    • Wang, J.A.1    Meyer, T.F.2    Rudel, T.3
  • 21
    • 84862221466 scopus 로고    scopus 로고
    • HemITAM signaling by CEACAM3, a human granulocyte receptor recognizing bacterial pathogens
    • DOI 10.1016/j.abb.2012.03.020
    • Buntru A, Roth A, Nyffenegger-Jann N, Hauck CR, (2012) HemITAM signaling by CEACAM3, a human granulocyte receptor recognizing bacterial pathogens. Archives of Biochemistry & Biophysics, DOI 10.1016/j.abb.2012.03.020.
    • (2012) Archives of Biochemistry & Biophysics
    • Buntru, A.1    Roth, A.2    Nyffenegger-Jann, N.3    Hauck, C.R.4
  • 22
    • 34547647469 scopus 로고    scopus 로고
    • Opa proteins of pathogenic Neisseriae initiate Src-kinase-dependent or lipid raft-mediated uptake via distinct human CEACAM isoforms
    • Schmitter T, Pils S, Weibel S, Agerer F, Buntru A, et al. (2007) Opa proteins of pathogenic Neisseriae initiate Src-kinase-dependent or lipid raft-mediated uptake via distinct human CEACAM isoforms. Infect Immun 75: 4116-4126.
    • (2007) Infect Immun , vol.75 , pp. 4116-4126
    • Schmitter, T.1    Pils, S.2    Weibel, S.3    Agerer, F.4    Buntru, A.5
  • 23
    • 0041664023 scopus 로고    scopus 로고
    • Immunoreceptor tyrosine-based activation motif phosphorylation during engulfment of Neisseria gonorrhoeae by the neutrophil-restricted CEACAM3 (CD66d) receptor
    • McCaw SE, Schneider J, Liao EH, Zimmermann W, Gray-Owen SD, (2003) Immunoreceptor tyrosine-based activation motif phosphorylation during engulfment of Neisseria gonorrhoeae by the neutrophil-restricted CEACAM3 (CD66d) receptor. Mol Microbiol 49: 623-637.
    • (2003) Mol Microbiol , vol.49 , pp. 623-637
    • McCaw, S.E.1    Schneider, J.2    Liao, E.H.3    Zimmermann, W.4    Gray-Owen, S.D.5
  • 24
    • 0346554975 scopus 로고    scopus 로고
    • Granulocyte CEACAM3 is a phagocytic receptor of the innate immune system that mediates recognition and elimination of human-specific pathogens
    • Schmitter T, Agerer F, Peterson L, Muenzner P, Hauck CR, (2004) Granulocyte CEACAM3 is a phagocytic receptor of the innate immune system that mediates recognition and elimination of human-specific pathogens. J Exp Med 199: 35-46.
    • (2004) J Exp Med , vol.199 , pp. 35-46
    • Schmitter, T.1    Agerer, F.2    Peterson, L.3    Muenzner, P.4    Hauck, C.R.5
  • 25
    • 71949112027 scopus 로고    scopus 로고
    • FRET-based subcellular visualization of pathogen-induced host receptor signalling
    • Buntru A, Zimmermann T, Hauck CR, (2009) FRET-based subcellular visualization of pathogen-induced host receptor signalling. BMC Biol 7: 81.
    • (2009) BMC Biol , vol.7 , pp. 81
    • Buntru, A.1    Zimmermann, T.2    Hauck, C.R.3
  • 26
    • 33947253224 scopus 로고    scopus 로고
    • The granulocyte receptor CEACAM3 directly associates with Vav to promote phagocytosis of human pathogens
    • Schmitter T, Pils S, Sakk V, Frank R, Fischer KD, et al. (2007) The granulocyte receptor CEACAM3 directly associates with Vav to promote phagocytosis of human pathogens. J Immunol 178: 3797-3805.
    • (2007) J Immunol , vol.178 , pp. 3797-3805
    • Schmitter, T.1    Pils, S.2    Sakk, V.3    Frank, R.4    Fischer, K.D.5
  • 27
    • 84858665656 scopus 로고    scopus 로고
    • The adaptor molecule Nck localizes the WAVE complex to promote actin polymerization during CEACAM3-mediated phagocytosis of bacteria
    • Pils S, Kopp K, Peterson L, Delgado-Tascon J, Nyffenegger-Jann N, et al. (2012) The adaptor molecule Nck localizes the WAVE complex to promote actin polymerization during CEACAM3-mediated phagocytosis of bacteria. PLoS One 7: e32808.
    • (2012) PLoS One , vol.7
    • Pils, S.1    Kopp, K.2    Peterson, L.3    Delgado-Tascon, J.4    Nyffenegger-Jann, N.5
  • 28
    • 42149186384 scopus 로고    scopus 로고
    • The CEACAM1 transmembrane domain, but not the cytoplasmic domain, directs internalization of human pathogens via membrane-microdomains
    • Muenzner P, Bachmann V, Kuespert K, Hauck CR, (2008) The CEACAM1 transmembrane domain, but not the cytoplasmic domain, directs internalization of human pathogens via membrane-microdomains. Cell Microbiol 10: 1074-1092.
    • (2008) Cell Microbiol , vol.10 , pp. 1074-1092
    • Muenzner, P.1    Bachmann, V.2    Kuespert, K.3    Hauck, C.R.4
  • 29
    • 79551552340 scopus 로고    scopus 로고
    • Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1
    • Kuespert K, Roth A, Hauck CR, (2011) Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1. PLoS One 6: e14609.
    • (2011) PLoS One , vol.6
    • Kuespert, K.1    Roth, A.2    Hauck, C.R.3
  • 30
    • 2142701466 scopus 로고    scopus 로고
    • Engulfment of Neisseria gonorrhoeae: revealing distinct processes of bacterial entry by individual carcinoembryonic antigen-related cellular adhesion molecule family receptors
    • McCaw SE, Liao EH, Gray-Owen SD, (2004) Engulfment of Neisseria gonorrhoeae: revealing distinct processes of bacterial entry by individual carcinoembryonic antigen-related cellular adhesion molecule family receptors. Infect Immun 72: 2742-2752.
    • (2004) Infect Immun , vol.72 , pp. 2742-2752
    • McCaw, S.E.1    Liao, E.H.2    Gray-Owen, S.D.3
  • 31
    • 79953220113 scopus 로고    scopus 로고
    • Phosphatidylinositol-3′ kinase activity is critical for initiating the oxidative burst and bacterial destruction during CEACAM3-mediated phagocytosis
    • Buntru A, Kopp K, Voges M, Frank R, Bachmann V, et al. (2011) Phosphatidylinositol-3′ kinase activity is critical for initiating the oxidative burst and bacterial destruction during CEACAM3-mediated phagocytosis. J Biol Chem 286: 9555-9566.
    • (2011) J Biol Chem , vol.286 , pp. 9555-9566
    • Buntru, A.1    Kopp, K.2    Voges, M.3    Frank, R.4    Bachmann, V.5
  • 32
    • 0028892541 scopus 로고
    • The molecular dissection of Fc gamma receptor mediated phagocytosis
    • Indik ZK, Park JG, Hunter S, Schreiber AD, (1995) The molecular dissection of Fc gamma receptor mediated phagocytosis. Blood 86: 4389-4399.
    • (1995) Blood , vol.86 , pp. 4389-4399
    • Indik, Z.K.1    Park, J.G.2    Hunter, S.3    Schreiber, A.D.4
  • 33
    • 0030459125 scopus 로고    scopus 로고
    • A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages
    • Araki N, Johnson MT, Swanson JA, (1996) A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages. J Cell Biol 135: 1249-1260.
    • (1996) J Cell Biol , vol.135 , pp. 1249-1260
    • Araki, N.1    Johnson, M.T.2    Swanson, J.A.3
  • 34
    • 33847273526 scopus 로고    scopus 로고
    • Profiling of bacterial adhesin - host receptor recognition by soluble immunoglobulin superfamily domains
    • Kuespert K, Weibel S, Hauck CR, (2007) Profiling of bacterial adhesin - host receptor recognition by soluble immunoglobulin superfamily domains. J Microbiol Meth 68: 478-485.
    • (2007) J Microbiol Meth , vol.68 , pp. 478-485
    • Kuespert, K.1    Weibel, S.2    Hauck, C.R.3
  • 35
    • 77951232015 scopus 로고    scopus 로고
    • Entry of N. meningitidis into mammalian cells requires Src family Protein-tyrosine kinases
    • Slanina H, Konig A, Hebling S, Hauck CR, Frosch M, et al. (2010) Entry of N. meningitidis into mammalian cells requires Src family Protein-tyrosine kinases. Infect Immun pp. 1905-1914.
    • (2010) Infect Immun , pp. 1905-1914
    • Slanina, H.1    Konig, A.2    Hebling, S.3    Hauck, C.R.4    Frosch, M.5
  • 36
    • 79551552340 scopus 로고    scopus 로고
    • Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1
    • Kuespert K, Roth A, Hauck CR, (2011) Neisseria meningitidis has two independent modes of recognizing its human receptor CEACAM1. PLoS ONE 6: e14609.
    • (2011) PLoS ONE , vol.6
    • Kuespert, K.1    Roth, A.2    Hauck, C.R.3
  • 37
    • 0037370498 scopus 로고    scopus 로고
    • A lentivirus-based system to functionally silence genes in primary mammalian cells, stem cells and transgenic mice by RNA interference
    • Rubinson DA, Dillon CP, Kwiatkowski AV, Sievers C, Yang L, et al. (2003) A lentivirus-based system to functionally silence genes in primary mammalian cells, stem cells and transgenic mice by RNA interference. Nat Genet 33: 401-406.
    • (2003) Nat Genet , vol.33 , pp. 401-406
    • Rubinson, D.A.1    Dillon, C.P.2    Kwiatkowski, A.V.3    Sievers, C.4    Yang, L.5
  • 38
    • 33645999394 scopus 로고    scopus 로고
    • Quantification of bacterial invasion into adherent cells by flow cytometry
    • Pils S, Schmitter T, Neske F, Hauck CR, (2006) Quantification of bacterial invasion into adherent cells by flow cytometry. J Microbiol Meth 65: 301-310.
    • (2006) J Microbiol Meth , vol.65 , pp. 301-310
    • Pils, S.1    Schmitter, T.2    Neske, F.3    Hauck, C.R.4
  • 39
    • 33747685367 scopus 로고    scopus 로고
    • Characterization of the stomatin domain involved in homo-oligomerization and lipid raft association
    • Umlauf E, Mairhofer M, Prohaska R, (2006) Characterization of the stomatin domain involved in homo-oligomerization and lipid raft association. J Biol Chem 281: 23349-23356.
    • (2006) J Biol Chem , vol.281 , pp. 23349-23356
    • Umlauf, E.1    Mairhofer, M.2    Prohaska, R.3
  • 40
    • 0042978825 scopus 로고    scopus 로고
    • Role of lipid-mediated signal transduction in bacterial internalization
    • Brumell JH, Grinstein S, (2003) Role of lipid-mediated signal transduction in bacterial internalization. Cell Microbiol 5: 287-297.
    • (2003) Cell Microbiol , vol.5 , pp. 287-297
    • Brumell, J.H.1    Grinstein, S.2
  • 41
    • 0037177352 scopus 로고    scopus 로고
    • Visualizing cellular phosphoinositide pools with GFP-fused protein-modules
    • Balla T, Varnai P, (2002) Visualizing cellular phosphoinositide pools with GFP-fused protein-modules. Sci STKE 2002: PL3.
    • (2002) Sci STKE , vol.2002
    • Balla, T.1    Varnai, P.2
  • 42
    • 0035968308 scopus 로고    scopus 로고
    • Pathogenic Neisseria trigger expression of their Carcinoembryonic antigen-related cellular adhesion molecule 1 (CEACAM1; previously CD66a) receptor on primary endothelial cells by activating the immediate early response transcription factor, Nuclear Factor-kappa B
    • Muenzner P, Naumann M, Meyer TF, Gray-Owen SD, (2001) Pathogenic Neisseria trigger expression of their Carcinoembryonic antigen-related cellular adhesion molecule 1 (CEACAM1; previously CD66a) receptor on primary endothelial cells by activating the immediate early response transcription factor, Nuclear Factor-kappa B. J Biol Chem 276: 24331-24340.
    • (2001) J Biol Chem , vol.276 , pp. 24331-24340
    • Muenzner, P.1    Naumann, M.2    Meyer, T.F.3    Gray-Owen, S.D.4
  • 43
    • 0029978202 scopus 로고    scopus 로고
    • The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase
    • Damen JE, Liu L, Rosten P, Humphries RK, Jefferson AB, et al. (1996) The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase. Proc Natl Acad Sci U S A 93: 1689-1693.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 1689-1693
    • Damen, J.E.1    Liu, L.2    Rosten, P.3    Humphries, R.K.4    Jefferson, A.B.5
  • 44
    • 0029665083 scopus 로고    scopus 로고
    • p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity
    • Lioubin MN, Algate PA, Schickwann T, Carlberg K, Aebersold R, et al. (1996) p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. Genes & Dev 10: 1084-1095.
    • (1996) Genes & Dev , vol.10 , pp. 1084-1095
    • Lioubin, M.N.1    Algate, P.A.2    Schickwann, T.3    Carlberg, K.4    Aebersold, R.5
  • 45
    • 33745684548 scopus 로고    scopus 로고
    • CEACAM1: contact-dependent control of immunity
    • Gray-Owen SD, Blumberg RS, (2006) CEACAM1: contact-dependent control of immunity. Nat Rev Immunol 6: 433-446.
    • (2006) Nat Rev Immunol , vol.6 , pp. 433-446
    • Gray-Owen, S.D.1    Blumberg, R.S.2
  • 46
    • 0033188169 scopus 로고    scopus 로고
    • Molecular analysis of neisserial Opa protein interactions with the CEA family of receptors: identification of determinants contributing to the differential specificities of binding
    • Popp A, Dehio C, Grunert F, Meyer TF, Gray-Owen SD, (1999) Molecular analysis of neisserial Opa protein interactions with the CEA family of receptors: identification of determinants contributing to the differential specificities of binding. Cell Microbiol 1: 169-181.
    • (1999) Cell Microbiol , vol.1 , pp. 169-181
    • Popp, A.1    Dehio, C.2    Grunert, F.3    Meyer, T.F.4    Gray-Owen, S.D.5
  • 47
    • 0037083747 scopus 로고    scopus 로고
    • Distinct mechanisms of internalization of Neisseria gonorrhoeae by members of the CEACAM receptor family involving Rac1- and Cdc42- dependent and -independent pathways
    • Billker O, Popp A, Brinkmann V, Wenig G, Schneider J, et al. (2002) Distinct mechanisms of internalization of Neisseria gonorrhoeae by members of the CEACAM receptor family involving Rac1- and Cdc42- dependent and-independent pathways. EMBO J 21: 560-571.
    • (2002) EMBO J , vol.21 , pp. 560-571
    • Billker, O.1    Popp, A.2    Brinkmann, V.3    Wenig, G.4    Schneider, J.5
  • 49
    • 0037195267 scopus 로고    scopus 로고
    • Dynamin2 and cortactin regulate actin assembly and filament organization
    • Schafer DA, Weed SA, Binns D, Karginov AV, Parsons JT, et al. (2002) Dynamin2 and cortactin regulate actin assembly and filament organization. Curr Biol 12: 1852-1857.
    • (2002) Curr Biol , vol.12 , pp. 1852-1857
    • Schafer, D.A.1    Weed, S.A.2    Binns, D.3    Karginov, A.V.4    Parsons, J.T.5
  • 50
    • 0032736675 scopus 로고    scopus 로고
    • Essential role of phosphoinositide metabolism in synaptic vesicle recycling
    • Cremona O, Di Paolo G, Wenk MR, Luthi A, Kim WT, et al. (1999) Essential role of phosphoinositide metabolism in synaptic vesicle recycling. Cell 99: 179-188.
    • (1999) Cell , vol.99 , pp. 179-188
    • Cremona, O.1    Di Paolo, G.2    Wenk, M.R.3    Luthi, A.4    Kim, W.T.5
  • 51
    • 84857257172 scopus 로고    scopus 로고
    • Yersinia entry into host cells requires Rab5-dependent dephosphorylation of PI(4,5)P and membrane scission
    • Sarantis H, Balkin DM, De Camilli P, Isberg RR, Brumell JH, et al. (2012) Yersinia entry into host cells requires Rab5-dependent dephosphorylation of PI(4,5)P and membrane scission. Cell Host Microbe 11: 117-128.
    • (2012) Cell Host Microbe , vol.11 , pp. 117-128
    • Sarantis, H.1    Balkin, D.M.2    de Camilli, P.3    Isberg, R.R.4    Brumell, J.H.5
  • 52
    • 0029958304 scopus 로고    scopus 로고
    • A role for phosphoinositide 3-kinase in bacterial invasion
    • Ireton K, Payrastre B, Chap H, Ogawa W, Sakaue H, et al. (1996) A role for phosphoinositide 3-kinase in bacterial invasion. Science 274: 780-782.
    • (1996) Science , vol.274 , pp. 780-782
    • Ireton, K.1    Payrastre, B.2    Chap, H.3    Ogawa, W.4    Sakaue, H.5
  • 53
    • 83755177932 scopus 로고    scopus 로고
    • Illuminating the landscape of host-pathogen interactions with the bacterium Listeria monocytogenes
    • Cossart P, (2011) Illuminating the landscape of host-pathogen interactions with the bacterium Listeria monocytogenes. Proc Natl Acad Sci U S A 108: 19484-19491.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 19484-19491
    • Cossart, P.1
  • 54
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon MA, Schlessinger J, (2010) Cell signaling by receptor tyrosine kinases. Cell 141: 1117-1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 55
    • 0028822686 scopus 로고
    • Receptor-mediated internalization of insulin. Potential role of pp120/HA4, a substrate of the insulin receptor kinase
    • Formisano P, Najjar SM, Gross CN, Philippe N, Oriente F, et al. (1995) Receptor-mediated internalization of insulin. Potential role of pp120/HA4, a substrate of the insulin receptor kinase. J Biol Chem 270: 24073-24077.
    • (1995) J Biol Chem , vol.270 , pp. 24073-24077
    • Formisano, P.1    Najjar, S.M.2    Gross, C.N.3    Philippe, N.4    Oriente, F.5
  • 56
    • 0034077136 scopus 로고    scopus 로고
    • The differential effects of pp120 (Ceacam 1) on the mitogenic action of insulin and insulin-like growth factor 1 are regulated by the nonconserved tyrosine 1316 in the insulin receptor
    • Soni P, Lakkis M, Poy MN, Fernstrom MA, Najjar SM, (2000) The differential effects of pp120 (Ceacam 1) on the mitogenic action of insulin and insulin-like growth factor 1 are regulated by the nonconserved tyrosine 1316 in the insulin receptor. Mol Cell Biol 20: 3896-3905.
    • (2000) Mol Cell Biol , vol.20 , pp. 3896-3905
    • Soni, P.1    Lakkis, M.2    Poy, M.N.3    Fernstrom, M.A.4    Najjar, S.M.5
  • 57
    • 0032575650 scopus 로고    scopus 로고
    • Insulin stimulates pp120 endocytosis in cells co-expressing insulin receptors
    • Choice CV, Howard MJ, Poy MN, Hankin MH, Najjar SM, (1998) Insulin stimulates pp120 endocytosis in cells co-expressing insulin receptors. J Biol Chem 273: 22194-22200.
    • (1998) J Biol Chem , vol.273 , pp. 22194-22200
    • Choice, C.V.1    Howard, M.J.2    Poy, M.N.3    Hankin, M.H.4    Najjar, S.M.5
  • 59
    • 0034711289 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase activation and interaction with focal adhesion kinase in Escherichia coli K1 invasion of human brain microvascular endothelial cells
    • Reddy MA, Prasadarao NV, Wass CA, Kim KS, (2000) Phosphatidylinositol 3-kinase activation and interaction with focal adhesion kinase in Escherichia coli K1 invasion of human brain microvascular endothelial cells. J Biol Chem 275: 36769-36774.
    • (2000) J Biol Chem , vol.275 , pp. 36769-36774
    • Reddy, M.A.1    Prasadarao, N.V.2    Wass, C.A.3    Kim, K.S.4
  • 60
    • 0345700251 scopus 로고    scopus 로고
    • Cloning and expression of the Escherichia coli K1 outer membrane protein A receptor, a gp96 homologue
    • Prasadarao NV, Srivastava PK, Rudrabhatla RS, Kim KS, Huang SH, et al. (2003) Cloning and expression of the Escherichia coli K1 outer membrane protein A receptor, a gp96 homologue. Infect Immun 71: 1680-1688.
    • (2003) Infect Immun , vol.71 , pp. 1680-1688
    • Prasadarao, N.V.1    Srivastava, P.K.2    Rudrabhatla, R.S.3    Kim, K.S.4    Huang, S.H.5
  • 61
    • 0345035504 scopus 로고    scopus 로고
    • Cell surface expression of the endoplasmic reticular heat shock protein gp96 is phylogenetically conserved
    • Robert J, Menoret A, Cohen N, (1999) Cell surface expression of the endoplasmic reticular heat shock protein gp96 is phylogenetically conserved. J Immunol 163: 4133-4139.
    • (1999) J Immunol , vol.163 , pp. 4133-4139
    • Robert, J.1    Menoret, A.2    Cohen, N.3
  • 62
    • 84863115806 scopus 로고    scopus 로고
    • The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domain
    • Wu S, Hong F, Gewirth D, Guo B, Liu B, et al. (2012) The molecular chaperone gp96/GRP94 interacts with Toll-like receptors and integrins via its C-terminal hydrophobic domain. J Biol Chem 287: 6735-6742.
    • (2012) J Biol Chem , vol.287 , pp. 6735-6742
    • Wu, S.1    Hong, F.2    Gewirth, D.3    Guo, B.4    Liu, B.5
  • 63
    • 67749142290 scopus 로고    scopus 로고
    • Cdc42 and the phosphatidylinositol 3-kinase-Akt pathway are essential for PspC-mediated internalization of pneumococci by respiratory epithelial cells
    • Agarwal V, Hammerschmidt S, (2009) Cdc42 and the phosphatidylinositol 3-kinase-Akt pathway are essential for PspC-mediated internalization of pneumococci by respiratory epithelial cells. J Biol Chem 284: 19427-19436.
    • (2009) J Biol Chem , vol.284 , pp. 19427-19436
    • Agarwal, V.1    Hammerschmidt, S.2
  • 64
    • 0034664821 scopus 로고    scopus 로고
    • The polymeric immunoglobulin receptor translocates pneumococci across human nasopharyngeal epithelial cells
    • Zhang JR, Mostov KE, Lamm ME, Nanno M, Shimida S, et al. (2000) The polymeric immunoglobulin receptor translocates pneumococci across human nasopharyngeal epithelial cells. Cell 102: 827-837.
    • (2000) Cell , vol.102 , pp. 827-837
    • Zhang, J.R.1    Mostov, K.E.2    Lamm, M.E.3    Nanno, M.4    Shimida, S.5
  • 65
    • 0036902323 scopus 로고    scopus 로고
    • Immunoglobulin transport across polarized epithelial cells
    • Rojas R, Apodaca G, (2002) Immunoglobulin transport across polarized epithelial cells. Nat Rev Mol Cell Biol 3: 944-955.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 944-955
    • Rojas, R.1    Apodaca, G.2


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