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Volumn 181, Issue 1, 2008, Pages 629-640

Sequential binding of cytosolic phox complex to phagosomes through regulated adaptor proteins: Evaluation using the novel monomeric kusabira-green system and live imaging of phagocytosis

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; FC RECEPTOR; NEUTROPHIL CYTOSOL FACTOR 40K; NEUTROPHIL CYTOSOL FACTOR 67K; NEUTROPHIL CYTOSOLIC FACTOR 1; PHOSPHOPROTEIN; RECOMBINANT PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 47949102446     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.181.1.629     Document Type: Article
Times cited : (52)

References (68)
  • 1
    • 8644255770 scopus 로고    scopus 로고
    • Assembly of the phagocyte NADPH oxidase
    • Nauseef, W M. 2004. Assembly of the phagocyte NADPH oxidase. Histochem. Cell Biol 122: 277-291.
    • (2004) Histochem. Cell Biol , vol.122 , pp. 277-291
    • Nauseef, W.M.1
  • 2
    • 4744349398 scopus 로고    scopus 로고
    • Structure and regulation of the neutrophil respiratory burst oxidase: Comparison with nonphagocyte oxidases
    • Quinn, M. T., and K. A. Gauss. 2004. Structure and regulation of the neutrophil respiratory burst oxidase: comparison with nonphagocyte oxidases. J. Leukocyte Biol. 76: 760-781.
    • (2004) J. Leukocyte Biol , vol.76 , pp. 760-781
    • Quinn, M.T.1    Gauss, K.A.2
  • 4
    • 0025220564 scopus 로고
    • Ultrastructural localization of cytochrome b in the membranes of resting and phagocytosing human granulocytes
    • Jesaitis, A. J., E. S. Buescher, D. Harrison, M. T. Quinn, C. A. Parkos, S. Livesey, and J. Linner. 1990. Ultrastructural localization of cytochrome b in the membranes of resting and phagocytosing human granulocytes. J. Clin. Invest. 85: 821-835.
    • (1990) J. Clin. Invest , vol.85 , pp. 821-835
    • Jesaitis, A.J.1    Buescher, E.S.2    Harrison, D.3    Quinn, M.T.4    Parkos, C.A.5    Livesey, S.6    Linner, J.7
  • 5
    • 0030997435 scopus 로고    scopus 로고
    • Granules of the human neutrophilic polymorphonuclear leukocyte
    • Borregaard, N., and J. B. Cowland. 1997. Granules of the human neutrophilic polymorphonuclear leukocyte. Blood 89: 3503-3521.
    • (1997) Blood , vol.89 , pp. 3503-3521
    • Borregaard, N.1    Cowland, J.B.2
  • 6
    • 0028081350 scopus 로고
    • Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins
    • Bokoch, G. M., B. P. Bohl, and T. H. Chuang. 1994. Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins. J. Biol. Chem. 269: 31674-31679.
    • (1994) J. Biol. Chem , vol.269 , pp. 31674-31679
    • Bokoch, G.M.1    Bohl, B.P.2    Chuang, T.H.3
  • 10
    • 0025203499 scopus 로고
    • Phosphorylation of neutrophil 47-kDa cyto-solic oxidase factor
    • Rotrosen, D., and T. L. Leto. 1990. Phosphorylation of neutrophil 47-kDa cyto-solic oxidase factor. J. Biol. Chem. 265: 19910-19915.
    • (1990) J. Biol. Chem , vol.265 , pp. 19910-19915
    • Rotrosen, D.1    Leto, T.L.2
  • 11
    • 33846781304 scopus 로고    scopus 로고
    • phox. Mol. Biol. Cell 18: 441-454.
    • phox. Mol. Biol. Cell 18: 441-454.
  • 13
    • 23444462664 scopus 로고    scopus 로고
    • Isoform-specific membrane targeting mechanism of Rac during FcγR-mediated phagocytosis: Positive charge-dependent and independent targeting mechanism of Rac to the phagosome
    • Ueyama, T., M. Eto, K. Kami, T. Tatsuno, T. Kobayashi, Y. Shirai, M. R. Lennartz, R. Takeya, H. Sumimoto, and N. Saito. 2005. Isoform-specific membrane targeting mechanism of Rac during FcγR-mediated phagocytosis: positive charge-dependent and independent targeting mechanism of Rac to the phagosome. J. Immunol. 175: 2381-2390.
    • (2005) J. Immunol , vol.175 , pp. 2381-2390
    • Ueyama, T.1    Eto, M.2    Kami, K.3    Tatsuno, T.4    Kobayashi, T.5    Shirai, Y.6    Lennartz, M.R.7    Takeya, R.8    Sumimoto, H.9    Saito, N.10
  • 15
    • 0346690398 scopus 로고    scopus 로고
    • The molecular basis for adhesion-mediated suppression of reactive oxygen species generation by human neutrophils
    • Zhao, T., V. Benard, B. P. Bohl, and G. M. Bokoch. 2003. The molecular basis for adhesion-mediated suppression of reactive oxygen species generation by human neutrophils. J. Clin. Invest. 112: 1732-1740.
    • (2003) J. Clin. Invest , vol.112 , pp. 1732-1740
    • Zhao, T.1    Benard, V.2    Bohl, B.P.3    Bokoch, G.M.4
  • 17
    • 0034283717 scopus 로고    scopus 로고
    • Dominant negative mutation of the hematopoietic-specific Rho GTPase, Rac2, is associated with a human phagocyte immunodeficiency
    • Williams, D. A., W. Tao, F. Yang, C. Kim, Y. Gu, P. Mansfield, J. E. Levine, B. Petryniak, C. W. Derrow, C. Harris, et al. 2000. Dominant negative mutation of the hematopoietic-specific Rho GTPase, Rac2, is associated with a human phagocyte immunodeficiency. Blood 96: 1646-1654.
    • (2000) Blood , vol.96 , pp. 1646-1654
    • Williams, D.A.1    Tao, W.2    Yang, F.3    Kim, C.4    Gu, Y.5    Mansfield, P.6    Levine, J.E.7    Petryniak, B.8    Derrow, C.W.9    Harris, C.10
  • 18
    • 0033082165 scopus 로고    scopus 로고
    • Deficiency of the he-matopoietic cell-specific Rho family GTPase Rac2 is characterized by abnormalities in neutrophil function and host defense
    • Roberts, A. W., C. Kim, L. Zhen, J. B. Lowe, R. Kapur, B. Petryniak, A. Spaetti, J. D. Pollock, J. B. Borneo, G. B. Bradford, et al. 1999. Deficiency of the he-matopoietic cell-specific Rho family GTPase Rac2 is characterized by abnormalities in neutrophil function and host defense. Immunity 10: 183-196.
    • (1999) Immunity , vol.10 , pp. 183-196
    • Roberts, A.W.1    Kim, C.2    Zhen, L.3    Lowe, J.B.4    Kapur, R.5    Petryniak, B.6    Spaetti, A.7    Pollock, J.D.8    Borneo, J.B.9    Bradford, G.B.10
  • 20
    • 0037108109 scopus 로고    scopus 로고
    • Current molecular models for NADPH oxidase regulation by Rac GTPase
    • Bokoch, G. M., and B. A. Diebold. 2002. Current molecular models for NADPH oxidase regulation by Rac GTPase. Blood 100: 2692-2695.
    • (2002) Blood , vol.100 , pp. 2692-2695
    • Bokoch, G.M.1    Diebold, B.A.2
  • 23
    • 0027973549 scopus 로고
    • Assembly of the phagocyte NADPH oxidase: Binding of Src homoloay 3 domains to proline-rich targets
    • Leto, T. L., A. G. Adams, and I. de Mendez. 1994. Assembly of the phagocyte NADPH oxidase: binding of Src homoloay 3 domains to proline-rich targets. Proc. Natl. Acad. Sci. USA 91: 10650-10654.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10650-10654
    • Leto, T.L.1    Adams, A.G.2    de Mendez, I.3
  • 24
    • 85177159023 scopus 로고    scopus 로고
    • Sumimoto, H., Y. Kage, H. Nunoi, H. Sasaki, T. Nose, Y. Fukumaki, M. Ohno, S. Minakami, and K. Takeshige. 1994. Role of Src homology 3 domains in assembly and activation of the phagocyte NADPH oxidase. Proc. Nail. Acad. Sci. 7X4 91:5345-5349.
    • Sumimoto, H., Y. Kage, H. Nunoi, H. Sasaki, T. Nose, Y. Fukumaki, M. Ohno, S. Minakami, and K. Takeshige. 1994. Role of Src homology 3 domains in assembly and activation of the phagocyte NADPH oxidase. Proc. Nail. Acad. Sci. 7X4 91:5345-5349.
  • 37
    • 0035899869 scopus 로고    scopus 로고
    • Ellson, C. D., K., E. Anderson, G. Morgan, E. R. Chilvers, P. Lipp, L. R. Stephens, and P. T. Hawkins. 2001. Phosphatidylinositol 3-phosphate is generated in phagosomal membranes. Curr. Biol. 11: 1631-1635.
    • Ellson, C. D., K., E. Anderson, G. Morgan, E. R. Chilvers, P. Lipp, L. R. Stephens, and P. T. Hawkins. 2001. Phosphatidylinositol 3-phosphate is generated in phagosomal membranes. Curr. Biol. 11: 1631-1635.
  • 40
    • 0025988892 scopus 로고    scopus 로고
    • phox from recombinant baculoviruses. J. Biol Chem. 266: 19812-19818.
    • phox from recombinant baculoviruses. J. Biol Chem. 266: 19812-19818.
  • 41
    • 33644750712 scopus 로고    scopus 로고
    • Involvement of Racl in activation of multicomponent Noxl- and Nox3-based NADPH oxidases
    • Ueyama, T., M. Geiszt, and T. L. Leto. 2006. Involvement of Racl in activation of multicomponent Noxl- and Nox3-based NADPH oxidases. Mol. Cell. Biol. 26: 2160-2174.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 2160-2174
    • Ueyama, T.1    Geiszt, M.2    Leto, T.L.3
  • 42
    • 3142736368 scopus 로고    scopus 로고
    • Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer
    • Karasawa, S., T. Araki, T. Nagai, H. Mizuno, and A. Miyawaki. 2004. Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer. Biochem. J. 381: 307-312.
    • (2004) Biochem. J , vol.381 , pp. 307-312
    • Karasawa, S.1    Araki, T.2    Nagai, T.3    Mizuno, H.4    Miyawaki, A.5
  • 43
    • 0034662681 scopus 로고    scopus 로고
    • Directed evolution of green fluorescent protein by a new versatile PCR strategy for site-directed and semi-random mu-tagenesis
    • Sawano, A., and A. Miyawaki. 2000. Directed evolution of green fluorescent protein by a new versatile PCR strategy for site-directed and semi-random mu-tagenesis. Nucleic Acids Res. 28: E78.
    • (2000) Nucleic Acids Res , vol.28
    • Sawano, A.1    Miyawaki, A.2
  • 45
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • Hu, C. D., and T. K. Kerppola. 2003. Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat. Bioteclmol. 21: 539-545.
    • (2003) Nat. Bioteclmol , vol.21 , pp. 539-545
    • Hu, C.D.1    Kerppola, T.K.2
  • 47
    • 33845635605 scopus 로고    scopus 로고
    • Subcellular localization and function of alternatively spliced Noxol isoforms
    • Ueyama, T., K. Lckstrom, S. Tsujibe, N. Saito, and T. L. Leto. 2007. Subcellular localization and function of alternatively spliced Noxol isoforms. Free Radic. Biol. Med. 42: 180-190.
    • (2007) Free Radic. Biol. Med , vol.42 , pp. 180-190
    • Ueyama, T.1    Lckstrom, K.2    Tsujibe, S.3    Saito, N.4    Leto, T.L.5
  • 50
    • 15944372262 scopus 로고    scopus 로고
    • Activation and assembly of the NADPH oxidase: A structural perspective
    • Groemping, Y., and K. Rittingcr. 2005. Activation and assembly of the NADPH oxidase: a structural perspective. Biochem. J. 386: 401-416.
    • (2005) Biochem. J , vol.386 , pp. 401-416
    • Groemping, Y.1    Rittingcr, K.2
  • 51
    • 0034995037 scopus 로고    scopus 로고
    • Solution structure of the PX domain, a target of the SH3 domain
    • Hiroaki, H., T. Ago, T. Ito, H. Sumimoto, and D. Kohda. 2001. Solution structure of the PX domain, a target of the SH3 domain. Nat. Struct. Biol. 8: 526-530.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 526-530
    • Hiroaki, H.1    Ago, T.2    Ito, T.3    Sumimoto, H.4    Kohda, D.5
  • 52
    • 0037722978 scopus 로고    scopus 로고
    • Molecular basis of phosphorylation-induced activation of the NADPH oxidase
    • Groemping, Y., K. Lapouge, S. J. Smerdon, and K. Rittinger. 2003. Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell 113: 343-355.
    • (2003) Cell , vol.113 , pp. 343-355
    • Groemping, Y.1    Lapouge, K.2    Smerdon, S.J.3    Rittinger, K.4
  • 54
    • 0028080090 scopus 로고
    • Split ubiquitin as a sensor of protein interactions in vivo
    • Johnsson, N., and A. Varshavsky. 1994. Split ubiquitin as a sensor of protein interactions in vivo. Proc. Natl. Acad. Sci. USA 91: 10340-10344.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10340-10344
    • Johnsson, N.1    Varshavsky, A.2
  • 55
    • 0030738524 scopus 로고    scopus 로고
    • Monitoring protein-protein interactions in intact eukaryotic cells by β-galactosidasc complementation
    • Rossi, F., C. A. Charlton, and H. M. Blau. 1997. Monitoring protein-protein interactions in intact eukaryotic cells by β-galactosidasc complementation. Proc. Natl. Acad. Sci. USA 94: 8405-8410.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8405-8410
    • Rossi, F.1    Charlton, C.A.2    Blau, H.M.3
  • 56
    • 0032514623 scopus 로고    scopus 로고
    • Oligomcriza-tion domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments
    • Pelletier, J. N., F. X. Campbell-Valois, and S. W. Michnick. 1998. Oligomcriza-tion domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments. Proc. Natl. Acad. Sci. USA 95: 12141-12146.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12141-12146
    • Pelletier, J.N.1    Campbell-Valois, F.X.2    Michnick, S.W.3
  • 57
    • 33751213120 scopus 로고    scopus 로고
    • Complementary methods for studies of protein interactions in living cells
    • Kerppola, T. K. 2006. Complementary methods for studies of protein interactions in living cells. Nat. Methods 3: 969-971.
    • (2006) Nat. Methods , vol.3 , pp. 969-971
    • Kerppola, T.K.1
  • 58
    • 33751208345 scopus 로고    scopus 로고
    • A highly sensitive protein-protein interaction assay based on Gaussia luciferase
    • Remy, I., and S. W. Michnick. 2006. A highly sensitive protein-protein interaction assay based on Gaussia luciferase. Nat. Methods 3: 977-979.
    • (2006) Nat. Methods , vol.3 , pp. 977-979
    • Remy, I.1    Michnick, S.W.2
  • 60
    • 0034647238 scopus 로고    scopus 로고
    • Antiparallel leucine zipper-directed protein reassembly: Application to the green fluorescent protein
    • Ghosh, I., A. D. Hamilton, and L. Regan. 2000. Antiparallel leucine zipper-directed protein reassembly: application to the green fluorescent protein. J. Am. Chem. Soc. 122: 5658-5659.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 5658-5659
    • Ghosh, I.1    Hamilton, A.D.2    Regan, L.3
  • 61
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu, C.-D., Y. Chinenov, and T. K. Kerppola. 2002. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9: 789-798.
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.-D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 64
    • 0028170628 scopus 로고    scopus 로고
    • phox. J. Exp. Med. 180: 2329-2334.
    • phox. J. Exp. Med. 180: 2329-2334.
  • 65
  • 67
    • 34347375817 scopus 로고    scopus 로고
    • Differential association of phosphatidylinositol 3-kinase, SIHP-1, and PTEN with forming phasosomes
    • Kamen, L. A., J. Levinsohn, and J. A. Swanson. 2007. Differential association of phosphatidylinositol 3-kinase, SIHP-1, and PTEN with forming phasosomes. Mol. Biol. Cell. 18: 2463-2472.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2463-2472
    • Kamen, L.A.1    Levinsohn, J.2    Swanson, J.A.3


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