메뉴 건너뛰기




Volumn 97, Issue 1-2, 1998, Pages 81-95

The human malaria parasite Plasmodium falciparum exports the ATP-binding cassette protein PFGCN20 to membrane structures in the host red blood cell

Author keywords

ABC protein; Malaria; Plasmodium falciparum; Protein trafficking; Red blood cell

Indexed keywords

ABC TRANSPORTER;

EID: 0032583105     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(98)00135-2     Document Type: Article
Times cited : (32)

References (40)
  • 1
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins C.F. ABC transporters: from microorganisms to man. Ann. Rev. Cell. Biol. 8:1992;67-113.
    • (1992) Ann. Rev. Cell. Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 2
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Saraste M., Runswick M.J., Gay N.J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO. J. 1(8):1982;945-951.
    • (1982) EMBO. J. , vol.1 , Issue.8 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 3
    • 0029001571 scopus 로고
    • GCN20; A novel ATP binding cassette protein: And GCN1 reside in a complex that mediates activation of the eIF-2 alpha kinase GCN2 in amino acid-starved cells
    • Vazquez de Aldana C.R., Marton M.J., Hinnebusch A.G. GCN20; a novel ATP binding cassette protein; and GCN1 reside in a complex that mediates activation of the eIF-2 alpha kinase GCN2 in amino acid-starved cells. EMBO. J. 14:1995;3184-3199.
    • (1995) EMBO. J. , vol.14 , pp. 3184-3199
    • Vazquez de Aldana, C.R.1    Marton, M.J.2    Hinnebusch, A.G.3
  • 4
    • 0025180478 scopus 로고
    • Sequence analysis of the translational elongation factor 3 from Saccharomyces cerevisiae
    • Qin S.L., Xie A.G., Bonato M.C., McLaughlin C.S. Sequence analysis of the translational elongation factor 3 from Saccharomyces cerevisiae. J. Biol. Chem. 265:1990;1903-1912.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1903-1912
    • Qin, S.L.1    Xie, A.G.2    Bonato, M.C.3    McLaughlin, C.S.4
  • 5
    • 0024338609 scopus 로고
    • Amplification of the multidrug resistance gene in some chloroquine-resistant isolates of P. falciparum
    • Foote S.J., Thompson J.K., Cowman A.F., Kemp D.J. Amplification of the multidrug resistance gene in some chloroquine-resistant isolates of P. falciparum. Cell. 57:1989;921-930.
    • (1989) Cell , vol.57 , pp. 921-930
    • Foote, S.J.1    Thompson, J.K.2    Cowman, A.F.3    Kemp, D.J.4
  • 7
    • 0030592439 scopus 로고    scopus 로고
    • Cloning and sequence analysis of a novel member of the ATP-binding cassette (ABC) protein gene family from Plasmodium falciparum
    • Bozdech Z., Delling U., Volkman S.K., Cowman A.F., Schurr E. Cloning and sequence analysis of a novel member of the ATP-binding cassette (ABC) protein gene family from Plasmodium falciparum. Mol. Biochem. Parasitol. 81:1996;41-51.
    • (1996) Mol. Biochem. Parasitol. , vol.81 , pp. 41-51
    • Bozdech, Z.1    Delling, U.2    Volkman, S.K.3    Cowman, A.F.4    Schurr, E.5
  • 8
    • 0026769984 scopus 로고
    • Sequence of a staphylococcal plasmid gene, vga, encoding a putative ATP-binding protein involved in resistance to virginiamycin A-like antibiotics
    • Allignet J., Loncle V., el Sohl N. Sequence of a staphylococcal plasmid gene, vga, encoding a putative ATP-binding protein involved in resistance to virginiamycin A-like antibiotics. Gene. 117:1992;45-51.
    • (1992) Gene , vol.117 , pp. 45-51
    • Allignet, J.1    Loncle, V.2    El Sohl, N.3
  • 9
    • 0027401744 scopus 로고
    • A nutrient-permeable channel on the intraerythrocytic malaria parasite
    • Desai S.A., Krogstad D.J., McCleskey E.W. A nutrient-permeable channel on the intraerythrocytic malaria parasite. Nature. 362:1993;643-649.
    • (1993) Nature , vol.362 , pp. 643-649
    • Desai, S.A.1    Krogstad, D.J.2    McCleskey, E.W.3
  • 10
    • 0027171069 scopus 로고
    • Translation of the yeast transcriptional activator GCN4 is stimulated by purine limitation: Implications for activation of the protein kinase GCN2
    • Rolfes R.J., Hinnebusch A.G. Translation of the yeast transcriptional activator GCN4 is stimulated by purine limitation: implications for activation of the protein kinase GCN2. Mol. Cell. Biol. 13:1993;5099-5111.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5099-5111
    • Rolfes, R.J.1    Hinnebusch, A.G.2
  • 11
    • 1842287951 scopus 로고    scopus 로고
    • Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eIF2alpha kinase GCN2
    • Marton M.J., Vazquez de Aldana C.R., Qiu H., Chakraburtty K., Hinnebusch A.G. Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eIF2alpha kinase GCN2. Mol. Cell. Biol. 17:1997;4474-4489.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4474-4489
    • Marton, M.J.1    Vazquez de Aldana, C.R.2    Qiu, H.3    Chakraburtty, K.4    Hinnebusch, A.G.5
  • 12
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager W., Jensen J.B. Human malaria parasites in continuous culture. Science. 193:1976;673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 13
    • 0025786518 scopus 로고
    • A P-glycoprotein homologue of Plasmodium falciparum is localized on the digestive vacuole
    • Cowman A.F., Karcz S., Galatis D., Culvenor J.G. A P-glycoprotein homologue of Plasmodium falciparum is localized on the digestive vacuole. J. Cell. Biol. 113:1991;1033-1042.
    • (1991) J. Cell. Biol. , vol.113 , pp. 1033-1042
    • Cowman, A.F.1    Karcz, S.2    Galatis, D.3    Culvenor, J.G.4
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0027465101 scopus 로고
    • Multiple chromosomal populations of topoisomerase II detected in vivo by time-lapse, three-dimensional wide-field microscopy
    • Swedlow J.R., Sedat J.W., Agard D.A. Multiple chromosomal populations of topoisomerase II detected in vivo by time-lapse, three-dimensional wide-field microscopy. Cell. 73:1993;97-108.
    • (1993) Cell , vol.73 , pp. 97-108
    • Swedlow, J.R.1    Sedat, J.W.2    Agard, D.A.3
  • 16
    • 0027049796 scopus 로고
    • Trafficking of malarial proteins to the host cell cytoplasm and erythrocyte surface membrane involves multiple pathways
    • Gormley J.A., Howard R.J., Tarashi T.F. Trafficking of malarial proteins to the host cell cytoplasm and erythrocyte surface membrane involves multiple pathways. J. Cell. Biol. 119:1992;1481-1495.
    • (1992) J. Cell. Biol. , vol.119 , pp. 1481-1495
    • Gormley, J.A.1    Howard, R.J.2    Tarashi, T.F.3
  • 17
    • 0027456544 scopus 로고
    • Secretory transport in Plasmodium falciparum
    • Elmendorf H.D., Haldar K. Secretory transport in Plasmodium falciparum. Parasitol. Today. 9:1993;98-102.
    • (1993) Parasitol. Today. , vol.9 , pp. 98-102
    • Elmendorf, H.D.1    Haldar, K.2
  • 18
    • 0028037278 scopus 로고
    • Plasmodium falciparum: Protein localization along a novel lipid rich tubovesicular membrane network in infected erythrocytes
    • Behari R., Haldar K. Plasmodium falciparum: protein localization along a novel lipid rich tubovesicular membrane network in infected erythrocytes. Exp. Parasitol. 79:1994;250-259.
    • (1994) Exp. Parasitol. , vol.79 , pp. 250-259
    • Behari, R.1    Haldar, K.2
  • 19
    • 0028008830 scopus 로고
    • Plasmodium falciparum exports the golgi marker sphingomyelin synthase into a tubovesicular network in the cytoplasm of mature erythrocytes
    • Elmendorf H.D., Haldar K. Plasmodium falciparum exports the golgi marker sphingomyelin synthase into a tubovesicular network in the cytoplasm of mature erythrocytes. J. Cell. Biol. 124:1994;449-462.
    • (1994) J. Cell. Biol. , vol.124 , pp. 449-462
    • Elmendorf, H.D.1    Haldar, K.2
  • 20
    • 0022994181 scopus 로고
    • Secretion of a malarial histidine-rich protein (Pf HRP II) from Plasmodium falciparum-infected erythrocytes
    • Howard R.J., Uni S., Aikawa M. et al. Secretion of a malarial histidine-rich protein (Pf HRP II) from Plasmodium falciparum-infected erythrocytes. J. Cell. Biol. 103:1986;1269-1277.
    • (1986) J. Cell. Biol. , vol.103 , pp. 1269-1277
    • Howard, R.J.1    Uni, S.2    Aikawa, M.3
  • 21
    • 0023335234 scopus 로고
    • r∼300 000 Plasmodium falciparum protein (PfEMP 2) from the intraerythrocytic asexual parasite to the cytolplasmic face of the host cell mambrane
    • r∼300 000 Plasmodium falciparum protein (PfEMP 2) from the intraerythrocytic asexual parasite to the cytolplasmic face of the host cell mambrane. J. Cell. Biol. 104:1987;1269-1280.
    • (1987) J. Cell. Biol. , vol.104 , pp. 1269-1280
    • Howard, R.J.1    Lyon, J.A.2    Uni, S.3
  • 25
    • 0028131368 scopus 로고
    • Biosynthesis; Export and processing of a 45 kDa protein detected in membrane clefts of erythrocytes infected with Plasmodium falciparum
    • Das A., Elmendorf H.D., Haldar K. Biosynthesis; export and processing of a 45 kDa protein detected in membrane clefts of erythrocytes infected with Plasmodium falciparum. Biochem. J. 302:1994;487-496.
    • (1994) Biochem. J. , vol.302 , pp. 487-496
    • Das, A.1    Elmendorf, H.D.2    Haldar, K.3
  • 26
    • 0030745899 scopus 로고    scopus 로고
    • A novel alternate secretory pathway for the export of Plasmodium proteins into the host erythrocyte
    • Wiser M.F., Lanners H.N., Bafford R.A., Favaloro J.M. A novel alternate secretory pathway for the export of Plasmodium proteins into the host erythrocyte. Proc. Natl. Acad. Sci. USA. 94:1997;9108-9113.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9108-9113
    • Wiser, M.F.1    Lanners, H.N.2    Bafford, R.A.3    Favaloro, J.M.4
  • 27
    • 0025954269 scopus 로고
    • Structure-function analysis of the histidine permease and comparison with cystic fibrosis mutations
    • Shyamala V., Baichwal V., Beall E., Ames G.F. Structure-function analysis of the histidine permease and comparison with cystic fibrosis mutations. J. Biol. Chem. 266:1991;18714-19719.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18714-19719
    • Shyamala, V.1    Baichwal, V.2    Beall, E.3    Ames, G.F.4
  • 28
    • 0025738363 scopus 로고
    • Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli
    • Davidson A.L., Nikaido H. Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli. J. Biol. Chem. 266:1991;8946-8951.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8946-8951
    • Davidson, A.L.1    Nikaido, H.2
  • 29
    • 0025033814 scopus 로고
    • Bacterial periplasmic permeases belong to a family of transport proteins operating from Escherichia coli to human: Traffic ATPases
    • Ames G.F., Mimura C.S., Shyamala V. Bacterial periplasmic permeases belong to a family of transport proteins operating from Escherichia coli to human: Traffic ATPases. FEMS. Microbiol. Rev. 6:1990;429-446.
    • (1990) FEMS. Microbiol. Rev. , vol.6 , pp. 429-446
    • Ames, G.F.1    Mimura, C.S.2    Shyamala, V.3
  • 31
    • 0025257358 scopus 로고
    • Protease secretion by Erwinia chrysanthemi: The specific secretion functions are analogous to those of Escherichia coli alpha-haemolysin
    • Letoffe S., Delepelaire P., Wandersman C. Protease secretion by Erwinia chrysanthemi: the specific secretion functions are analogous to those of Escherichia coli alpha-haemolysin. EMBO. J. 9:1990;1375-1382.
    • (1990) EMBO. J. , vol.9 , pp. 1375-1382
    • Letoffe, S.1    Delepelaire, P.2    Wandersman, C.3
  • 32
    • 0028842445 scopus 로고
    • The three genes lipB; lipC; and lipD involved in the extracellular secretion of the Serratia marcescens lipase which lacks an N-terminal signal peptide
    • Akatsuka H., Kawai E., Omori K., Shibatani T. The three genes lipB; lipC; and lipD involved in the extracellular secretion of the Serratia marcescens lipase which lacks an N-terminal signal peptide. J. Bacteriol. 177:1995;6381-6389.
    • (1995) J. Bacteriol. , vol.177 , pp. 6381-6389
    • Akatsuka, H.1    Kawai, E.2    Omori, K.3    Shibatani, T.4
  • 33
    • 0029036498 scopus 로고
    • Parasite-regulated membrane transport processes and metabolic control in malaria-infected erythrocytes
    • Elford B.C., Cowan G.M., Ferguson D.J. Parasite-regulated membrane transport processes and metabolic control in malaria-infected erythrocytes. Biochem. J. 308:1995;361-374.
    • (1995) Biochem. J. , vol.308 , pp. 361-374
    • Elford, B.C.1    Cowan, G.M.2    Ferguson, D.J.3
  • 34
    • 0026318656 scopus 로고
    • New nucleoside transport pathways induced in the host erythrocyte membrane of malaria and Babesia infected cells
    • Gero A.M., Wood A.M. New nucleoside transport pathways induced in the host erythrocyte membrane of malaria and Babesia infected cells. Adv. Exp. Med. Biol. 309A:1991;169-172.
    • (1991) Adv. Exp. Med. Biol. , vol.309 A , pp. 169-172
    • Gero, A.M.1    Wood, A.M.2
  • 35
    • 0026027304 scopus 로고
    • Lipid traffic between high density lipoproteins and Plasmodium falciparum-infected red blood cells
    • Grellier P., Rigomier D., Clavey V., Fruchart J.C., Schrevel J. Lipid traffic between high density lipoproteins and Plasmodium falciparum-infected red blood cells. J. Cell. Biol. 112:1991;267-277.
    • (1991) J. Cell. Biol. , vol.112 , pp. 267-277
    • Grellier, P.1    Rigomier, D.2    Clavey, V.3    Fruchart, J.C.4    Schrevel, J.5
  • 36
    • 0025824734 scopus 로고
    • Transport of lactate in Plasmodium falciparum-infected human erythrocytes
    • Kanaani J., Ginsburg H. Transport of lactate in Plasmodium falciparum-infected human erythrocytes. J. Cell. Physiol. 149:1991;469-476.
    • (1991) J. Cell. Physiol. , vol.149 , pp. 469-476
    • Kanaani, J.1    Ginsburg, H.2
  • 37
    • 0021797609 scopus 로고
    • Selective stage-specific changes in the permeability to small hydrophilic solutes of human erythrocytes infected with Plasmodium falciparum
    • Elford B.C., Haynes J.D., Chulay J.D., Wilson R.J. Selective stage-specific changes in the permeability to small hydrophilic solutes of human erythrocytes infected with Plasmodium falciparum. Mol. Biochem. Parasitol. 16:1985;43-60.
    • (1985) Mol. Biochem. Parasitol. , vol.16 , pp. 43-60
    • Elford, B.C.1    Haynes, J.D.2    Chulay, J.D.3    Wilson, R.J.4
  • 38
    • 0021992698 scopus 로고
    • Characterization of permeation pathways appearing in the host membrane of Plasmodium falciparum infected red blood cells
    • Ginsburg H., Kutner S., Krugliak M., Cabantchik Z.I. Characterization of permeation pathways appearing in the host membrane of Plasmodium falciparum infected red blood cells. Mol. Biochem. Parasitol. 14:1985;313-322.
    • (1985) Mol. Biochem. Parasitol. , vol.14 , pp. 313-322
    • Ginsburg, H.1    Kutner, S.2    Krugliak, M.3    Cabantchik, Z.I.4
  • 39
    • 0030953287 scopus 로고    scopus 로고
    • A membrane network for nutrient import in red cells infected with the malaria parasite
    • Lauer S.A., Rathod P.K., Ghori N., Haldar K. A membrane network for nutrient import in red cells infected with the malaria parasite. Science. 276:1997;1122-1125.
    • (1997) Science , vol.276 , pp. 1122-1125
    • Lauer, S.A.1    Rathod, P.K.2    Ghori, N.3    Haldar, K.4
  • 40
    • 0023616658 scopus 로고
    • Comparative analysis of the Plasmodium falciparum histidine-rich proteins HRP-I, HRP-II and HRP-III in malaria parasites of diverse origin
    • Rock E.P., Marsh K., Saul A.J. et al. Comparative analysis of the Plasmodium falciparum histidine-rich proteins HRP-I, HRP-II and HRP-III in malaria parasites of diverse origin. Par. 95:1987;209-227.
    • (1987) Par , vol.95 , pp. 209-227
    • Rock, E.P.1    Marsh, K.2    Saul, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.