메뉴 건너뛰기




Volumn 21, Issue 19, 2002, Pages 5057-5068

Binding of the PX domain of p47phox to phosphatidylinositol 3, 4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction

Author keywords

NADPH oxidase; p40; Phagocyte; Phosphatidic acid; Phosphoinositide; SH3 domains

Indexed keywords

GLUTAMIC ACID; INOSITOL DERIVATIVE; PHOSPHATIDIC ACID; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; PHOSPHATIDYLINOSITOL 3,4 BISPHOSPHATE; PHOSPHATIDYLSERINE; PROTEIN P47; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SERINE; SULFATE; UNCLASSIFIED DRUG;

EID: 0036791737     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf519     Document Type: Article
Times cited : (274)

References (48)
  • 3
    • 0033105874 scopus 로고    scopus 로고
    • NADPH oxidase: An update
    • Babior, B.M. (1999) NADPH oxidase: an update. Blood, 93, 1464-1476.
    • (1999) Blood , vol.93 , pp. 1464-1476
    • Babior, B.M.1
  • 4
    • 0035830872 scopus 로고    scopus 로고
    • Roles of ionic residues of the C1 domain in protein kinase C-α activation and the origin of phosphatidylserine specificity
    • Bittova, L., Stahelin, R.V. and Cho, W. (2001) Roles of ionic residues of the C1 domain in protein kinase C-α activation and the origin of phosphatidylserine specificity. J. Biol. Chem., 276, 4218-4226.
    • (2001) J. Biol. Chem , vol.276 , pp. 4218-4226
    • Bittova, L.1    Stahelin, R.V.2    Cho, W.3
  • 5
    • 17944367436 scopus 로고    scopus 로고
    • phox bound to phosphatidylinositol 3-phosphate
    • phox bound to phosphatidylinositol 3-phosphate. Mol. Cell, 8, 829-839.
    • (2001) Mol. Cell , vol.8 , pp. 829-839
    • Bravo, J.1
  • 6
    • 0028103275 scopus 로고
    • Collaborative Computing Project Number 4: A suite of programs for protein crystallography
    • CCP4 (1994) Collaborative Computing Project Number 4: a suite of programs for protein crystallography. Acta Crystallogr. D, 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 7
    • 0035884406 scopus 로고    scopus 로고
    • Membrane binding assays for peripheral proteins
    • Cho, W., Bittova, L. and Stahelin, R.V. (2001) Membrane binding assays for peripheral proteins. Anal. Biochem., 296, 153-161.
    • (2001) Anal. Biochem , vol.296 , pp. 153-161
    • Cho, W.1    Bittova, L.2    Stahelin, R.V.3
  • 8
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle, E. and Bricogne, G. (1997) Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol., 276, 472-494.
    • (1997) Methods Enzymol , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 9
    • 0034306455 scopus 로고    scopus 로고
    • Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities
    • Dowler, S., Currie, R.A., Campbell, D.G., Deak, M., Kular, G., Downes, C.P. and Alessi, D.R. (2000) Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem. J., 351, 19-31.
    • (2000) Biochem. J , vol.351 , pp. 19-31
    • Dowler, S.1    Currie, R.A.2    Campbell, D.G.3    Deak, M.4    Kular, G.5    Downes, C.P.6    Alessi, D.R.7
  • 13
    • 0033529533 scopus 로고    scopus 로고
    • Activation of human neutrophil NADPH oxidase by phosphatidic acid or diacylglycerol in a cell-free system. Activity of diacylglycerol is dependent on its conversion to phosphatidic acid
    • Erickson, R.W., Langel-Peveri, P., Traynor-Kaplan, A.E., Heyworth, P.G. and Curnutte, J.T. (1999) Activation of human neutrophil NADPH oxidase by phosphatidic acid or diacylglycerol in a cell-free system. Activity of diacylglycerol is dependent on its conversion to phosphatidic acid. J. Biol. Chem., 274, 22243-22250.
    • (1999) J. Biol. Chem , vol.274 , pp. 22243-22250
    • Erickson, R.W.1    Langel-Peveri, P.2    Traynor-Kaplan, A.E.3    Heyworth, P.G.4    Curnutte, J.T.5
  • 16
    • 0036094545 scopus 로고    scopus 로고
    • Chronic granulomatous disease mutations and the PX domain
    • Heyworth, P.G. and Cross, A.R. (2002) Chronic granulomatous disease mutations and the PX domain. Nat. Cell Biol., 4, E110.
    • (2002) Nat. Cell Biol , vol.4 , pp. E110
    • Heyworth, P.G.1    Cross, A.R.2
  • 17
    • 0024334744 scopus 로고
    • Localization of the 47 kDa phosphoprotein involved in the respiratory-burst NADPH oxidase of phagocytic cells
    • Heyworth, P.G., Shrimpton, C.F. and Segal, A.W. (1989) Localization of the 47 kDa phosphoprotein involved in the respiratory-burst NADPH oxidase of phagocytic cells. Biochem. J., 260, 243-248.
    • (1989) Biochem. J , vol.260 , pp. 243-248
    • Heyworth, P.G.1    Shrimpton, C.F.2    Segal, A.W.3
  • 18
    • 0025970033 scopus 로고
    • Neutrophil nicotinamide adenine dinucleotide phosphate oxidase assembly. Translocation of p47-phox and p67-phox requires interaction between p47-phox and cytochrome b558
    • Heyworth, P.G., Curnutte, J.T., Nauseef, W.M., Volpp, B.D., Pearson, D.W., Rosen, H. and Clark, R.A. (1991) Neutrophil nicotinamide adenine dinucleotide phosphate oxidase assembly. Translocation of p47-phox and p67-phox requires interaction between p47-phox and cytochrome b558. J. Clin. Invest., 87, 352-356.
    • (1991) J. Clin. Invest , vol.87 , pp. 352-356
    • Heyworth, P.G.1    Curnutte, J.T.2    Nauseef, W.M.3    Volpp, B.D.4    Pearson, D.W.5    Rosen, H.6    Clark, R.A.7
  • 19
    • 0034995037 scopus 로고    scopus 로고
    • Solution structure of the PX domain, a target of the SH3 domain
    • Hiroaki, H., Ago, T., Ito, T., Sumimoto, H., and Kohda, D. (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
  • 20
    • 0033538550 scopus 로고    scopus 로고
    • Activation of the phagocyte NADPH oxidase protein p47(phox). Phosphorylation controls SH3 domain-dependent binding to p22(phox)
    • Huang, J. and Kleinberg, M.E. (1999) Activation of the phagocyte NADPH oxidase protein p47(phox). Phosphorylation controls SH3 domain-dependent binding to p22(phox). J. Biol. Chem., 274, 19731-19737.
    • (1999) J. Biol. Chem , vol.274 , pp. 19731-19737
    • Huang, J.1    Kleinberg, M.E.2
  • 21
    • 0032567417 scopus 로고    scopus 로고
    • Activation of p47(PHOX), a cytosolic subunit of the leukocyte NADPH oxidase-phosphorylation of Ser-359 or Ser-370 precedes phosphorylation at other sites and is required for activity
    • Johnson, J.L., Park, J.W., El Benna, J., Faust, L.P., Inanami, O. and Babior, B.M. (1998) Activation of p47(PHOX), a cytosolic subunit of the leukocyte NADPH oxidase-phosphorylation of Ser-359 or Ser-370 precedes phosphorylation at other sites and is required for activity. J. Biol. Chem., 273, 35147-35152.
    • (1998) J. Biol. Chem , vol.273 , pp. 35147-35152
    • Johnson, J.L.1    Park, J.W.2    El Benna, J.3    Faust, L.P.4    Inanami, O.5    Babior, B.M.6
  • 24
    • 0031570794 scopus 로고    scopus 로고
    • A phospholipase A2 kinetic and binding assay using phospholipid-coated hydrophobic beads
    • Kim, Y., Lichtenbergova, L., Snitko, Y. and Cho, W. (1997) A phospholipase A2 kinetic and binding assay using phospholipid-coated hydrophobic beads. Anal. Biochem., 250, 109-116.
    • (1997) Anal. Biochem , vol.250 , pp. 109-116
    • Kim, Y.1    Lichtenbergova, L.2    Snitko, Y.3    Cho, W.4
  • 25
    • 0036471945 scopus 로고    scopus 로고
    • Evidence that the tandem-pleckstrin-homology-domain-containing protein TAPP1 interacts with Ptd(3, 4)P2 and the multi-PDZ-domain-containing protein MUPPI in vivo
    • Kimber, W.A. et al. (2002) Evidence that the tandem-pleckstrin-homology-domain-containing protein TAPP1 interacts with Ptd(3, 4)P2 and the multi-PDZ-domain-containing protein MUPPI in vivo. Biochem. J., 361, 525-536.
    • (2002) Biochem. J , vol.361 , pp. 525-536
    • Kimber, W.A.1
  • 27
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Daresbury Laboratory, Warrington, UK
    • Leslie, A.G.W. (1992) Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 and ESF-EACMB Newsletter on Protein Crystallography, Daresbury Laboratory, Warrington, UK, Vol. 26.
    • (1992) Joint CCP4 and ESF-EACMB Newsletter on Protein Crystallography , pp. 26
    • Leslie, A.G.W.1
  • 28
    • 0027973549 scopus 로고
    • Assembly of the phagocyte NADPH oxidase: Binding of Src homology 3 domains to proline-rich targets
    • Leto, T.L., Adams, A.G. and de Mendez, I. (1994) Assembly of the phagocyte NADPH oxidase: binding of Src homology 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
  • 29
    • 0002501831 scopus 로고    scopus 로고
    • Interactions between the components of the human NADPH oxidase: A review about the intrigues in the phox family
    • Leusen, J.H.W., Verhoeven, A.J. and Roos, D. (1996) Interactions between the components of the human NADPH oxidase: a review about the intrigues in the phox family. Frontiers Biosci., 1, d72-d90.
    • (1996) Frontiers Biosci , vol.1 , pp. d72-d90
    • Leusen, J.H.W.1    Verhoeven, A.J.2    Roos, D.3
  • 31
    • 0035030510 scopus 로고    scopus 로고
    • SH3 domains: Complexity in moderation
    • Mayer, B.J. (2001) SH3 domains: complexity in moderation. J. Cell Sci., 114, 1253-1263.
    • (2001) J. Cell Sci , vol.114 , pp. 1253-1263
    • Mayer, B.J.1
  • 32
    • 0035379643 scopus 로고    scopus 로고
    • JFC1, a novel tandem C2 domain-containing protein associated with the leukocyte NADPH oxidase
    • McAdara Berkowitz, J.K., Catz, S.D., Johnson, J.L., Ruedi, J.M., Thon, V. and Babior, B.M. (2001) JFC1, a novel tandem C2 domain-containing protein associated with the leukocyte NADPH oxidase. J. Biol. Chem., 276, 18855-18862.
    • (2001) J. Biol. Chem , vol.276 , pp. 18855-18862
    • McAdara Berkowitz, J.K.1    Catz, S.D.2    Johnson, J.L.3    Ruedi, J.M.4    Thon, V.5    Babior, B.M.6
  • 33
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., Vagin, A.A. and Dodson, E.J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D, 53, 240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 34
    • 0035793541 scopus 로고    scopus 로고
    • Phosphatidic acid and diacylglycerol directly activate NADPH oxidase by interacting with enzyme components
    • Palicz, A., Foubert, T.R., Jesaitis, A.J., Marodi, L. and McPhail, L.C. (2001) Phosphatidic acid and diacylglycerol directly activate NADPH oxidase by interacting with enzyme components. J. Biol. Chem., 276, 3090-3097.
    • (2001) J. Biol. Chem , vol.276 , pp. 3090-3097
    • Palicz, A.1    Foubert, T.R.2    Jesaitis, A.J.3    Marodi, L.4    McPhail, L.C.5
  • 35
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R. and Lamzin, V.S. (1999) Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol., 6, 458-463.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 36
    • 0037149510 scopus 로고    scopus 로고
    • + flux
    • + flux. Nature, 416, 291-297.
    • (2002) Nature , vol.416 , pp. 291-297
    • Reeves, E.P.1
  • 37
    • 0025203499 scopus 로고
    • Phosphorylation of neutrophil 47-kDa cytosolic oxidase factor
    • Rotrosen, D. and Leto, T.L. (1990) Phosphorylation of neutrophil 47-kDa cytosolic oxidase factor. J. Biol. Chem., 265, 19910-19915.
    • (1990) J. Biol. Chem , vol.265 , pp. 19910-19915
    • Rotrosen, D.1    Leto, T.L.2
  • 38
    • 0036241542 scopus 로고    scopus 로고
    • Study of NADPH oxidase-activated sites in human neutrophils
    • Seguchi, H. and Kobayashi, T. (2002) Study of NADPH oxidase-activated sites in human neutrophils. J. Electron Microsc., 51, 87-91.
    • (2002) J. Electron Microsc , vol.51 , pp. 87-91
    • Seguchi, H.1    Kobayashi, T.2
  • 39
    • 0035901553 scopus 로고    scopus 로고
    • Differential roles of ionic, aliphatic and aromatic residues in membrane-protein interactions: A surface plasmon resonance study on phospholipases A2
    • Stahelin, R.V. and Cho, W. (2001) Differential roles of ionic, aliphatic and aromatic residues in membrane-protein interactions: a surface plasmon resonance study on phospholipases A2. Biochemistry, 40, 4672-4678.
    • (2001) Biochemistry , vol.40 , pp. 4672-4678
    • Stahelin, R.V.1    Cho, W.2
  • 40
    • 0037135529 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs
    • Stahelin, R.V., Long, F., Diraviyam, K., Bruzik, K.S., Murray, D. and Cho, W. (2002) Phosphatidylinositol-3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs. J. Biol. Chem., 277, 26379-26388.
    • (2002) J. Biol. Chem , vol.277 , pp. 26379-26388
    • Stahelin, R.V.1    Long, F.2    Diraviyam, K.3    Bruzik, K.S.4    Murray, D.5    Cho, W.6
  • 42
    • 0029806925 scopus 로고    scopus 로고
    • Assembly and activation of the phagocyte NADPH oxidase-specific interaction of the N-terminal Src homology 3 domain of p47(phox) with p22(phox) is required for activation of the NADPH oxidase
    • Sumimoto, H., Hata, K., Mizuki, K., Ito, T., Kage, Y., Sakaki, Y., Fukumaki, Y., Nakamura, M. and Takeshige, K. (1996) Assembly and activation of the phagocyte NADPH oxidase-specific interaction of the N-terminal Src homology 3 domain of p47(phox) with p22(phox) is required for activation of the NADPH oxidase. J. Biol. Chem., 271, 22152-22158.
    • (1996) J. Biol. Chem , vol.271 , pp. 22152-22158
    • Sumimoto, H.1    Hata, K.2    Mizuki, K.3    Ito, T.4    Kage, Y.5    Sakaki, Y.6    Fukumaki, Y.7    Nakamura, M.8    Takeshige, K.9
  • 43
    • 0030682421 scopus 로고    scopus 로고
    • Analysis of activation-induced conformational changes in p47phox using tryptophan fluorescence spectroscopy
    • Swain, S.D., Helgerson, S.L., Davis, A.R., Nelson, L.K. and Quinn, M.T. (1997) Analysis of activation-induced conformational changes in p47phox using tryptophan fluorescence spectroscopy. J. Biol. Chem., 272, 29502-29510.
    • (1997) J. Biol. Chem , vol.272 , pp. 29502-29510
    • Swain, S.D.1    Helgerson, S.L.2    Davis, A.R.3    Nelson, L.K.4    Quinn, M.T.5
  • 44
    • 0035447056 scopus 로고    scopus 로고
    • Crystal structure of the phosphatidylinositol 3, 4-bisphosphate-binding pleckstrin homology (PH) domain of tandem PH-domain-containing protein 1 (TAPP1): Molecular basis of lipid specificity
    • Thomas, C.C., Dowler, S., Deak, M., Alessi, D.R. and van Aalten, D.M. (2001) Crystal structure of the phosphatidylinositol 3, 4-bisphosphate-binding pleckstrin homology (PH) domain of tandem PH-domain-containing protein 1 (TAPP1): molecular basis of lipid specificity. Biochem. J., 358, 287-294.
    • (2001) Biochem. J , vol.358 , pp. 287-294
    • Thomas, C.C.1    Dowler, S.2    Deak, M.3    Alessi, D.R.4    Van Aalten, D.M.5
  • 45
    • 0027418759 scopus 로고
    • The respiratory burst oxidase of human neutrophils. Guanine nucleotides and arachidonate regulate the assembly of a multicomponent complex in a semirecombinant cell-free system
    • Uhlinger, D.J., Tyagi, S.R., Inge, K.L. and Lambeth, J.D. (1993) The respiratory burst oxidase of human neutrophils. Guanine nucleotides and arachidonate regulate the assembly of a multicomponent complex in a semirecombinant cell-free system. J. Biol. Chem., 268, 8624-8631.
    • (1993) J. Biol. Chem , vol.268 , pp. 8624-8631
    • Uhlinger, D.J.1    Tyagi, S.R.2    Inge, K.L.3    Lambeth, J.D.4
  • 46
  • 47
    • 0035941208 scopus 로고    scopus 로고
    • All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate
    • Yu, J.W. and Lemmon, M.A. (2001) All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate. J. Biol. Chem., 276, 44179-44184.
    • (2001) J. Biol. Chem , vol.276 , pp. 44179-44184
    • Yu, J.W.1    Lemmon, M.A.2
  • 48
    • 0037039667 scopus 로고    scopus 로고
    • The p40phox and p47phox PX domains of NADPH oxidase target cell membranes via direct and indirect recruitment by phosphoinositides
    • Zhan, Y., Virbasius, J.V., Song, X., Pomerleau, D.P. and Zhou, G.W. (2002) The p40phox and p47phox PX domains of NADPH oxidase target cell membranes via direct and indirect recruitment by phosphoinositides. J. Biol. Chem., 277, 4512-4518.
    • (2002) J. Biol. Chem , vol.277 , pp. 4512-4518
    • Zhan, Y.1    Virbasius, J.V.2    Song, X.3    Pomerleau, D.P.4    Zhou, G.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.