메뉴 건너뛰기




Volumn 7, Issue 4, 2012, Pages

Regulation of Plasmodium falciparum glideosome associated protein 45 (PfGAP45) phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM DEPENDENT PROTEIN KINASE 1; MEMBRANE PROTEIN; MYOSIN TAIL INTERACTING PROTEIN; PHOSPHOLIPASE C; PLASMODIUM FALCIPARUM GLIDEOSOME ASSOCIATED PROTEIN 45; PROTEIN KINASE; PROTEIN KINASE B; UNCLASSIFIED DRUG; CALCIUM DEPENDENT PROTEIN KINASE 1, PLASMODIUM FALCIPARUM; CALCIUM PROTEIN KINASE; CALCIUM-DEPENDENT PROTEIN KINASE; CALCIUM-DEPENDENT PROTEIN KINASE-1, PLASMODIUM FALCIPARUM; GLIDEOSOME ASSOCIATED PROTEIN 45, PLASMODIUM FALCIPARUM; GLIDEOSOME-ASSOCIATED PROTEIN 45, PLASMODIUM FALCIPARUM; HYBRID PROTEIN; PKB PROTEIN, PLASMODIUM FALCIPARUM; PROTOZOAL PROTEIN;

EID: 84860486844     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0035855     Document Type: Article
Times cited : (24)

References (37)
  • 1
    • 79952193925 scopus 로고    scopus 로고
    • World Health Organization. Global Malaria Program, World Health Organization
    • World Health Organization. Global Malaria Program (2010) World malaria report 2010. World Health Organization.
    • (2010) World malaria report 2010
  • 2
    • 12744268524 scopus 로고    scopus 로고
    • Parasite ligand-host receptor interactions during invasion of erythrocytes by Plasmodium merozoites
    • Gaur D, Mayer DC, Miller LH, (2004) Parasite ligand-host receptor interactions during invasion of erythrocytes by Plasmodium merozoites. International journal for parasitology 34: 1413-1429.
    • (2004) International Journal for Parasitology , vol.34 , pp. 1413-1429
    • Gaur, D.1    Mayer, D.C.2    Miller, L.H.3
  • 3
    • 2442528540 scopus 로고    scopus 로고
    • Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii
    • Gaskins E, Gilk S, DeVore N, Mann T, Ward G, et al. (2004) Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii. J Cell Biol 165: 383-393.
    • (2004) J Cell Biol , vol.165 , pp. 383-393
    • Gaskins, E.1    Gilk, S.2    DeVore, N.3    Mann, T.4    Ward, G.5
  • 4
    • 4644345259 scopus 로고    scopus 로고
    • The glideosome: a molecular machine powering motility and host-cell invasion by Apicomplexa
    • Keeley A, Soldati D, (2004) The glideosome: a molecular machine powering motility and host-cell invasion by Apicomplexa. Trends Cell Biol 14: 528-532.
    • (2004) Trends Cell Biol , vol.14 , pp. 528-532
    • Keeley, A.1    Soldati, D.2
  • 5
    • 33645306878 scopus 로고    scopus 로고
    • A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites
    • Baum J, Richard D, Healer J, Rug M, Krnajski Z, et al. (2006) A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites. J Biol Chem 281: 5197-5208.
    • (2006) J Biol Chem , vol.281 , pp. 5197-5208
    • Baum, J.1    Richard, D.2    Healer, J.3    Rug, M.4    Krnajski, Z.5
  • 7
    • 57649221595 scopus 로고    scopus 로고
    • The motor complex of Plasmodium falciparum: phosphorylation by a calcium-dependent protein kinase
    • Green JL, Rees-Channer RR, Howell SA, Martin SR, Knuepfer E, et al. (2008) The motor complex of Plasmodium falciparum: phosphorylation by a calcium-dependent protein kinase. J Biol Chem 283: 30980-30989.
    • (2008) J Biol Chem , vol.283 , pp. 30980-30989
    • Green, J.L.1    Rees-Channer, R.R.2    Howell, S.A.3    Martin, S.R.4    Knuepfer, E.5
  • 8
    • 33645855615 scopus 로고    scopus 로고
    • Plasmodium falciparum erythrocyte invasion: a conserved myosin associated complex
    • Jones ML, Kitson EL, Rayner JC, (2006) Plasmodium falciparum erythrocyte invasion: a conserved myosin associated complex. Mol Biochem Parasitol 147: 74-84.
    • (2006) Mol Biochem Parasitol , vol.147 , pp. 74-84
    • Jones, M.L.1    Kitson, E.L.2    Rayner, J.C.3
  • 9
    • 79955368787 scopus 로고    scopus 로고
    • Tracking Glideosome-associated protein 50 reveals the development and organization of the inner membrane complex of Plasmodium falciparum
    • Yeoman JA, Hanssen E, Maier AG, Klonis N, Maco B, et al. (2011) Tracking Glideosome-associated protein 50 reveals the development and organization of the inner membrane complex of Plasmodium falciparum. Eukaryot Cell 10: 556-564.
    • (2011) Eukaryot Cell , vol.10 , pp. 556-564
    • Yeoman, J.A.1    Hanssen, E.2    Maier, A.G.3    Klonis, N.4    Maco, B.5
  • 10
    • 68049137458 scopus 로고    scopus 로고
    • Mechanisms controlling glideosome function in apicomplexans
    • Daher W, Soldati-Favre D, (2009) Mechanisms controlling glideosome function in apicomplexans. Curr Opin Microbiol 12: 408-414.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 408-414
    • Daher, W.1    Soldati-Favre, D.2
  • 11
    • 43749109597 scopus 로고    scopus 로고
    • Gene expression signatures and small-molecule compounds link a protein kinase to Plasmodium falciparum motility
    • Kato N, Sakata T, Breton G, Le Roch KG, Nagle A, et al. (2008) Gene expression signatures and small-molecule compounds link a protein kinase to Plasmodium falciparum motility. Nat Chem Biol 4: 347-356.
    • (2008) Nat Chem Biol , vol.4 , pp. 347-356
    • Kato, N.1    Sakata, T.2    Breton, G.3    Le Roch, K.G.4    Nagle, A.5
  • 12
    • 80052704470 scopus 로고    scopus 로고
    • Unusual N-glycan structures required for trafficking Toxoplasma gondii GAP50 to the inner membrane complex regulate host cell entry through parasite motility
    • Fauquenoy S, Hovasse A, Sloves PJ, Morelle W, Dilezitoko AT, et al. (2011) Unusual N-glycan structures required for trafficking Toxoplasma gondii GAP50 to the inner membrane complex regulate host cell entry through parasite motility. Mol Cell Proteomics 10: M111.
    • (2011) Mol Cell Proteomics , vol.10
    • Fauquenoy, S.1    Hovasse, A.2    Sloves, P.J.3    Morelle, W.4    Dilezitoko, A.T.5
  • 14
    • 33745976499 scopus 로고    scopus 로고
    • Dual acylation of the 45 kDa gliding-associated protein (GAP45) in Plasmodium falciparum merozoites
    • Rees-Channer RR, Martin SR, Green JL, Bowyer PW, Grainger M, et al. (2006) Dual acylation of the 45 kDa gliding-associated protein (GAP45) in Plasmodium falciparum merozoites. Mol Biochem Parasitol 149: 113-116.
    • (2006) Mol Biochem Parasitol , vol.149 , pp. 113-116
    • Rees-Channer, R.R.1    Martin, S.R.2    Green, J.L.3    Bowyer, P.W.4    Grainger, M.5
  • 15
    • 59249083317 scopus 로고    scopus 로고
    • GAP45 phosphorylation controls assembly of the Toxoplasma myosin XIV complex
    • Gilk SD, Gaskins E, Ward GE, Beckers CJ, (2009) GAP45 phosphorylation controls assembly of the Toxoplasma myosin XIV complex. Eukaryot Cell 8: 190-196.
    • (2009) Eukaryot Cell , vol.8 , pp. 190-196
    • Gilk, S.D.1    Gaskins, E.2    Ward, G.E.3    Beckers, C.J.4
  • 16
    • 80053458415 scopus 로고    scopus 로고
    • Quantitative in vivo analyses reveal calcium-dependent phosphorylation sites and identifies a novel component of the Toxoplasma invasion motor complex
    • Nebl T, Prieto JH, Kapp E, Smith BJ, Williams MJ, et al. (2011) Quantitative in vivo analyses reveal calcium-dependent phosphorylation sites and identifies a novel component of the Toxoplasma invasion motor complex. PLoS Pathog 7: e1002222.
    • (2011) PLoS Pathog , vol.7
    • Nebl, T.1    Prieto, J.H.2    Kapp, E.3    Smith, B.J.4    Williams, M.J.5
  • 17
    • 41949086426 scopus 로고    scopus 로고
    • Role of Ca2+/calmodulin-PfPKB signaling pathway in erythrocyte invasion by Plasmodium falciparum
    • Vaid A, Thomas DC, Sharma P, (2008) Role of Ca2+/calmodulin-PfPKB signaling pathway in erythrocyte invasion by Plasmodium falciparum. J Biol Chem 283: 5589-5597.
    • (2008) J Biol Chem , vol.283 , pp. 5589-5597
    • Vaid, A.1    Thomas, D.C.2    Sharma, P.3
  • 18
    • 23944494434 scopus 로고    scopus 로고
    • Products of tryptophan catabolism induce Ca2+ release and modulate the cell cycle of Plasmodium falciparum malaria parasites
    • Beraldo FH, Garcia CR, (2005) Products of tryptophan catabolism induce Ca2+ release and modulate the cell cycle of Plasmodium falciparum malaria parasites. J Pineal Res 39: 224-230.
    • (2005) J Pineal Res , vol.39 , pp. 224-230
    • Beraldo, F.H.1    Garcia, C.R.2
  • 19
    • 77649263117 scopus 로고    scopus 로고
    • Distinct external signals trigger sequential release of apical organelles during erythrocyte invasion by malaria parasites
    • Singh S, Alam MM, Pal-Bhowmick I, Brzostowski JA, Chitnis CE, (2010) Distinct external signals trigger sequential release of apical organelles during erythrocyte invasion by malaria parasites. PLoS Pathog 6: e1000746.
    • (2010) PLoS Pathog , vol.6
    • Singh, S.1    Alam, M.M.2    Pal-Bhowmick, I.3    Brzostowski, J.A.4    Chitnis, C.E.5
  • 20
    • 68749112446 scopus 로고    scopus 로고
    • Effects of calcium signaling on Plasmodium falciparum erythrocyte invasion and post-translational modification of gliding-associated protein 45 (PfGAP45)
    • Jones ML, Cottingham C, Rayner JC, (2009) Effects of calcium signaling on Plasmodium falciparum erythrocyte invasion and post-translational modification of gliding-associated protein 45 (PfGAP45). Mol Biochem Parasitol 168: 55-62.
    • (2009) Mol Biochem Parasitol , vol.168 , pp. 55-62
    • Jones, M.L.1    Cottingham, C.2    Rayner, J.C.3
  • 21
    • 33748753548 scopus 로고    scopus 로고
    • PfPKB, a protein kinase B-like enzyme from Plasmodium falciparum: II. Identification of calcium/calmodulin as its upstream activator and dissection of a novel signaling pathway
    • Vaid A, Sharma P, (2006) PfPKB, a protein kinase B-like enzyme from Plasmodium falciparum: II. Identification of calcium/calmodulin as its upstream activator and dissection of a novel signaling pathway. J Biol Chem 281: 27126-27133.
    • (2006) J Biol Chem , vol.281 , pp. 27126-27133
    • Vaid, A.1    Sharma, P.2
  • 22
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager W, Jensen JB, (1976) Human malaria parasites in continuous culture. Science 193: 673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 23
    • 30544443567 scopus 로고    scopus 로고
    • Re-defining the Golgi complex in Plasmodium falciparum using the novel Golgi marker PfGRASP
    • Struck NS, de Souza DS, Langer C, Marti M, Pearce JA, et al. (2005) Re-defining the Golgi complex in Plasmodium falciparum using the novel Golgi marker PfGRASP. J Cell Sci 118: 5603-5613.
    • (2005) J Cell Sci , vol.118 , pp. 5603-5613
    • Struck, N.S.1    de Souza, D.S.2    Langer, C.3    Marti, M.4    Pearce, J.A.5
  • 25
    • 0030885188 scopus 로고    scopus 로고
    • Transformation with human dihydrofolate reductase renders malaria parasites insensitive to WR99210 but does not affect the intrinsic activity of proguanil
    • Fidock DA, Wellems TE, (1997) Transformation with human dihydrofolate reductase renders malaria parasites insensitive to WR99210 but does not affect the intrinsic activity of proguanil. Proc Natl Acad Sci U S A 94: 10931-10936.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10931-10936
    • Fidock, D.A.1    Wellems, T.E.2
  • 26
    • 2642554720 scopus 로고    scopus 로고
    • PfPKB, a novel protein kinase B-like enzyme from Plasmodium falciparum: I. Identification, characterization, and possible role in parasite development
    • Kumar A, Vaid A, Syin C, Sharma P, (2004) PfPKB, a novel protein kinase B-like enzyme from Plasmodium falciparum: I. Identification, characterization, and possible role in parasite development. J Biol Chem 279: 24255-24264.
    • (2004) J Biol Chem , vol.279 , pp. 24255-24264
    • Kumar, A.1    Vaid, A.2    Syin, C.3    Sharma, P.4
  • 27
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Boyle WJ, van der GP, Hunter T, (1991) Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol 201: 110-149.
    • (1991) Methods Enzymol , vol.201 , pp. 110-149
    • Boyle, W.J.1    van der, G.P.2    Hunter, T.3
  • 28
    • 3343010591 scopus 로고    scopus 로고
    • Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method
    • Tonkin CJ, van Dooren GG, Spurck TP, Struck NS, Good RT, et al. (2004) Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method. Mol Biochem Parasitol 137: 13-21.
    • (2004) Mol Biochem Parasitol , vol.137 , pp. 13-21
    • Tonkin, C.J.1    van Dooren, G.G.2    Spurck, T.P.3    Struck, N.S.4    Good, R.T.5
  • 29
    • 0035117158 scopus 로고    scopus 로고
    • Plasmodium protein phosphatase 2C dephosphorylates translation elongation factor 1beta and inhibits its PKC-mediated nucleotide exchange activity in vitro
    • Mamoun CB, Goldberg DE, (2001) Plasmodium protein phosphatase 2C dephosphorylates translation elongation factor 1beta and inhibits its PKC-mediated nucleotide exchange activity in vitro. Mol Microbiol 39: 973-981.
    • (2001) Mol Microbiol , vol.39 , pp. 973-981
    • Mamoun, C.B.1    Goldberg, D.E.2
  • 30
    • 67651004664 scopus 로고    scopus 로고
    • Protein phosphorylation influences proteolytic cleavage and kinase substrate properties exemplified by analysis of in vitro phosphorylated Plasmodium falciparum glideosome-associated protein 45 by nano-ultra performance liquid chromatography-tandem mass spectrometry
    • Winter D, Kugelstadt D, Seidler J, Kappes B, Lehmann WD, (2009) Protein phosphorylation influences proteolytic cleavage and kinase substrate properties exemplified by analysis of in vitro phosphorylated Plasmodium falciparum glideosome-associated protein 45 by nano-ultra performance liquid chromatography-tandem mass spectrometry. Anal Biochem 393: 41-47.
    • (2009) Anal Biochem , vol.393 , pp. 41-47
    • Winter, D.1    Kugelstadt, D.2    Seidler, J.3    Kappes, B.4    Lehmann, W.D.5
  • 31
    • 0001061413 scopus 로고    scopus 로고
    • Intracellular calcium-release channels: regulators of cell life and death
    • Marks AR, (1997) Intracellular calcium-release channels: regulators of cell life and death. Am J Physiol 272: H597-H605.
    • (1997) Am J Physiol , vol.272
    • Marks, A.R.1
  • 32
    • 20344384859 scopus 로고    scopus 로고
    • Potent and selective inhibitors of Akt kinases slow the progress of tumors in vivo
    • Luo Y, Shoemaker AR, Liu X, Woods KW, Thomas SA, et al. (2005) Potent and selective inhibitors of Akt kinases slow the progress of tumors in vivo. Mol Cancer Ther 4: 977-986.
    • (2005) Mol Cancer Ther , vol.4 , pp. 977-986
    • Luo, Y.1    Shoemaker, A.R.2    Liu, X.3    Woods, K.W.4    Thomas, S.A.5
  • 33
    • 69949148305 scopus 로고    scopus 로고
    • A novel family of Apicomplexan glideosome-associated proteins with an inner membrane-anchoring role
    • Bullen HE, Tonkin CJ, O'Donnell RA, Tham WH, Papenfuss AT, et al. (2009) A novel family of Apicomplexan glideosome-associated proteins with an inner membrane-anchoring role. J Biol Chem 284: 25353-25363.
    • (2009) J Biol Chem , vol.284 , pp. 25353-25363
    • Bullen, H.E.1    Tonkin, C.J.2    O'Donnell, R.A.3    Tham, W.H.4    Papenfuss, A.T.5
  • 34
    • 79959240876 scopus 로고    scopus 로고
    • Multiple roles for Plasmodium berghei phosphoinositide-specific phospholipase C in regulating gametocyte activation and differentiation
    • Raabe AC, Wengelnik K, Billker O, Vial HJ, (2011) Multiple roles for Plasmodium berghei phosphoinositide-specific phospholipase C in regulating gametocyte activation and differentiation. Cell Microbiol 13: 955-966.
    • (2011) Cell Microbiol , vol.13 , pp. 955-966
    • Raabe, A.C.1    Wengelnik, K.2    Billker, O.3    Vial, H.J.4
  • 35
    • 0344805645 scopus 로고    scopus 로고
    • Calcium signaling in a low calcium environment: how the intracellular malaria parasite solves the problem
    • Gazarini ML, Thomas AP, Pozzan T, Garcia CR, (2003) Calcium signaling in a low calcium environment: how the intracellular malaria parasite solves the problem. J Cell Biol 161: 103-110.
    • (2003) J Cell Biol , vol.161 , pp. 103-110
    • Gazarini, M.L.1    Thomas, A.P.2    Pozzan, T.3    Garcia, C.R.4
  • 36
    • 0242490894 scopus 로고    scopus 로고
    • Melatonin and N-acetyl-serotonin cross the red blood cell membrane and evoke calcium mobilization in malarial parasites
    • Hotta CT, Markus RP, Garcia CR, (2003) Melatonin and N-acetyl-serotonin cross the red blood cell membrane and evoke calcium mobilization in malarial parasites. Braz J Med Biol Res 36: 1583-1587.
    • (2003) Braz J Med Biol Res , vol.36 , pp. 1583-1587
    • Hotta, C.T.1    Markus, R.P.2    Garcia, C.R.3
  • 37
    • 80054901700 scopus 로고    scopus 로고
    • The phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii reveal unusual adaptations within and beyond the parasites' boundaries
    • Treeck M, Sanders JL, Elias JE, Boothroyd JC, (2011) The phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii reveal unusual adaptations within and beyond the parasites' boundaries. Cell Host Microbe 10: 410-419.
    • (2011) Cell Host Microbe , vol.10 , pp. 410-419
    • Treeck, M.1    Sanders, J.L.2    Elias, J.E.3    Boothroyd, J.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.