메뉴 건너뛰기




Volumn 84, Issue 2, 1997, Pages 247-253

Cloning and characterization of plasmodium falciparum ADP-ribosylation factor and factor-like genes

Author keywords

ARF; ARL; Plasmodium falciparum; Schizogeny; Secretion

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR;

EID: 0031043801     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(96)02803-4     Document Type: Article
Times cited : (8)

References (39)
  • 1
    • 0027456544 scopus 로고
    • Secretory transport in Plasmodium
    • Elmendorf, H.G. and Haldar, K. (1993) Secretory transport in Plasmodium. Parasitol. Today 9, 98-102.
    • (1993) Parasitol. Today , vol.9 , pp. 98-102
    • Elmendorf, H.G.1    Haldar, K.2
  • 3
    • 15844362771 scopus 로고    scopus 로고
    • N-linked glycoproteins are related to schizogeny of the intraerythrocytic stage in Plasmodium falciparum
    • Kimura, E.A., Couto, A.S., Peres, V.J., Casal, O.L. and Katzin, A.M. (1996) N-linked glycoproteins are related to schizogeny of the intraerythrocytic stage in Plasmodium falciparum. J. Biol. Chem. 271, 14452-14461.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14452-14461
    • Kimura, E.A.1    Couto, A.S.2    Peres, V.J.3    Casal, O.L.4    Katzin, A.M.5
  • 4
    • 0028008830 scopus 로고
    • Plasmodium falciparum exports the Golgi marker sphingomyelin synthase into the tubulovesicular network in the cytoplasm of mature erythrocytes
    • Elmendorf, H.G. and Haldar, K. (1994) Plasmodium falciparum exports the Golgi marker sphingomyelin synthase into the tubulovesicular network in the cytoplasm of mature erythrocytes. J. Cell Biol. 124, 449-462.
    • (1994) J. Cell Biol. , vol.124 , pp. 449-462
    • Elmendorf, H.G.1    Haldar, K.2
  • 5
    • 0027501330 scopus 로고
    • Identification and localization of ERD2 in the malaria parasite Plasmodium falciparum: Separation from sites of sphingomyelin synthesis and implications for organization of the Golgi
    • Elmendorf, H.G. and Haldar, K. (1993) Identification and localization of ERD2 in the malaria parasite Plasmodium falciparum: separation from sites of sphingomyelin synthesis and implications for organization of the Golgi. EMBO J. 12, 4763-4773.
    • (1993) EMBO J. , vol.12 , pp. 4763-4773
    • Elmendorf, H.G.1    Haldar, K.2
  • 6
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence of membrane cycling from Golgi to ER
    • Lippincott-Schwartz, J., Yuan, L.C., Bonifacino, J.S. and Klausner, R.D. (1989) Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence of membrane cycling from Golgi to ER. Cell 56, 801-813.
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 7
    • 0023008846 scopus 로고
    • Novel blockade by brefeldin of intracellular transport of secretory proteins in cutured rat hepatocytes
    • Misumi, Y., Weissman, A.M., Samelson, L.E. and Klausner, R.D. (1986) Novel blockade by brefeldin of intracellular transport of secretory proteins in cutured rat hepatocytes. J. Biol. Chem. 261, 11398-11403.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11398-11403
    • Misumi, Y.1    Weissman, A.M.2    Samelson, L.E.3    Klausner, R.D.4
  • 8
    • 0026579552 scopus 로고
    • Synthesis and secretion of proteins by released malarial parasites
    • Elmendorf, H.G., Bangs, J.D. and Haldar, K. (1992) Synthesis and secretion of proteins by released malarial parasites. Mol. Biochem. Parasitol. 52, 215-230.
    • (1992) Mol. Biochem. Parasitol. , vol.52 , pp. 215-230
    • Elmendorf, H.G.1    Bangs, J.D.2    Haldar, K.3
  • 9
    • 0026766151 scopus 로고
    • ADP-ribosylation factor is required for vesicular trafficking between the endoplasmic reticulum and the cis-Golgi compartment
    • Balch, W.E., Kahn, R.A. and Schwaninger, R. (1992) ADP-ribosylation factor is required for vesicular trafficking between the endoplasmic reticulum and the cis-Golgi compartment. J. Biol. Chem. 267, 13053-13061.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13053-13061
    • Balch, W.E.1    Kahn, R.A.2    Schwaninger, R.3
  • 10
    • 0026632366 scopus 로고
    • Evidence for ADP-ribosylation factor (ARF) as a regulator for in vitro endosome-endosome fusion
    • Lenhard, J.M., Kahn, R.A. and Stahl, P.D. (1992) Evidence for ADP-ribosylation factor (ARF) as a regulator for in vitro endosome-endosome fusion. J. Biol. Chem. 267, 13047-13052.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13047-13052
    • Lenhard, J.M.1    Kahn, R.A.2    Stahl, P.D.3
  • 11
    • 0028914182 scopus 로고
    • A regulatory role for ARF6 in receptor-mediated endocytosis
    • D'Souza-Shorey, C., Li, G., Colombo, M.I. and Stahl, P.D. (1995) A regulatory role for ARF6 in receptor-mediated endocytosis. Science 267, 1175-1178.
    • (1995) Science , vol.267 , pp. 1175-1178
    • D'Souza-Shorey, C.1    Li, G.2    Colombo, M.I.3    Stahl, P.D.4
  • 12
    • 0026682791 scopus 로고
    • A role for ADP-ribosylation factor in nuclear vesicle dynamics
    • Boman, A.L., Taylor, T.C., Melancon, P. and Wilson, K.L. (1992) A role for ADP-ribosylation factor in nuclear vesicle dynamics. Nature 358, 512-514.
    • (1992) Nature , vol.358 , pp. 512-514
    • Boman, A.L.1    Taylor, T.C.2    Melancon, P.3    Wilson, K.L.4
  • 13
    • 0026327556 scopus 로고
    • Binding of ARF and β-COP to Golgi membranes: Possible regulation by a trimeric G protein
    • Donaldson, J.G., Kahn, R.A., Lippincott-Schwartz, J. and Klausner, R.D. (1991) Binding of ARF and β-COP to Golgi membranes: possible regulation by a trimeric G protein. Science 254, 1197-1199.
    • (1991) Science , vol.254 , pp. 1197-1199
    • Donaldson, J.G.1    Kahn, R.A.2    Lippincott-Schwartz, J.3    Klausner, R.D.4
  • 14
    • 0026623115 scopus 로고
    • ADP-ribosylation factor, a small GTP-binding protein, is required for the binding of the coatomer protein β-COP to Golgi membranes
    • Donaldson, J.G., Cassel, D., Kahn, R.A. and Klausner, R.D. (1992) ADP-ribosylation factor, a small GTP-binding protein, is required for the binding of the coatomer protein β-COP to Golgi membranes. Proc. Natl. Acad. Sci. USA 89, 6408-6412.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6408-6412
    • Donaldson, J.G.1    Cassel, D.2    Kahn, R.A.3    Klausner, R.D.4
  • 15
    • 0026001029 scopus 로고
    • ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein
    • Serafini, T., Orci, L., Amherdt, M., Brunner, M., Kahn, R.A. and Rothman, J.E. (1991) ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell 67, 239-253.
    • (1991) Cell , vol.67 , pp. 239-253
    • Serafini, T.1    Orci, L.2    Amherdt, M.3    Brunner, M.4    Kahn, R.A.5    Rothman, J.E.6
  • 16
    • 0030013233 scopus 로고    scopus 로고
    • Evidence that phospholipase D mediates ADP-ribosylation factor-dependent formation of Golgi-coated vesicles
    • Ktistakis, N.T., Brown, H.A., Waters, M.G., Sternweis, P.C. and Roth, M.G. (1996) Evidence that phospholipase D mediates ADP-ribosylation factor-dependent formation of Golgi-coated vesicles. J. Cell Biol. 134, 295-306.
    • (1996) J. Cell Biol. , vol.134 , pp. 295-306
    • Ktistakis, N.T.1    Brown, H.A.2    Waters, M.G.3    Sternweis, P.C.4    Roth, M.G.5
  • 17
    • 0023928057 scopus 로고
    • Chemical and immunological characterization of the 21 kDa ADP-ribosylation factor of adenylate cyclase
    • Kahn, R.A., Goddard, C. and Newkirk, M. (1988) Chemical and immunological characterization of the 21 kDa ADP-ribosylation factor of adenylate cyclase. J. Biol. Chem. 263, 8282-8287.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8282-8287
    • Kahn, R.A.1    Goddard, C.2    Newkirk, M.3
  • 18
    • 0021250807 scopus 로고
    • Purification of a protein cofactor required for ADP-ribosylation of the stimulatory regulatory component of adenylate cyclase by cholera toxin
    • Kahn, R.A. and Gilman, A.G. (1984) Purification of a protein cofactor required for ADP-ribosylation of the stimulatory regulatory component of adenylate cyclase by cholera toxin. J. Biol. Chem. 259, 6228-6234.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6228-6234
    • Kahn, R.A.1    Gilman, A.G.2
  • 20
    • 0027142022 scopus 로고
    • ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity
    • Brown, H.A., Gutowski, S., Moomaw, C.R., Slaughter, C. and Sternweis, P.C. (1993) ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell 75, 1137-1144.
    • (1993) Cell , vol.75 , pp. 1137-1144
    • Brown, H.A.1    Gutowski, S.2    Moomaw, C.R.3    Slaughter, C.4    Sternweis, P.C.5
  • 21
    • 0027482720 scopus 로고
    • Selective amplification of additional members of the ADP-ribosylation (ARF) family: Cloning of additional human and Drosophila ARF-like genes
    • Clark, J., Moore, L., Krasinskas, A., Way, J., Battey, J., Tamkun, J. and Kahn, R.A. (1993) Selective amplification of additional members of the ADP-ribosylation (ARF) family: cloning of additional human and Drosophila ARF-like genes. Proc. Natl. Acad. Sci. USA 90, 8952-8956.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8952-8956
    • Clark, J.1    Moore, L.2    Krasinskas, A.3    Way, J.4    Battey, J.5    Tamkun, J.6    Kahn, R.A.7
  • 23
    • 0029022643 scopus 로고
    • Myristoylation and ADP-ribosylation factor function
    • Randazzo, P.A. and Kahn, R.A. (1995) Myristoylation and ADP-ribosylation factor function. Methods Enzymol. 250, 394-405.
    • (1995) Methods Enzymol. , vol.250 , pp. 394-405
    • Randazzo, P.A.1    Kahn, R.A.2
  • 24
    • 0029027560 scopus 로고
    • Functional significance of myristoyl moiety in N-myristoylated proteins
    • Knoll, L.J., Johnson, D.R., Bryant, M.L. and Gordon, J.I. (1995) Functional significance of myristoyl moiety in N-myristoylated proteins. Methods Enzymol. 250, 405-435.
    • (1995) Methods Enzymol. , vol.250 , pp. 405-435
    • Knoll, L.J.1    Johnson, D.R.2    Bryant, M.L.3    Gordon, J.I.4
  • 25
    • 0003705448 scopus 로고
    • N-myristoylation of proteins: Studies with Saccharomyces cerevisiae as a model system
    • (M.J. Schlesinger, eds.), Boca Raton. CRC Press
    • Duronio, R.J., Rudnick, D.A., Knoll, L.J., Johnson, D.R. and Gordon, J.I. (1992) N-myristoylation of proteins: studies with Saccharomyces cerevisiae as a model system. In: Lipid Modifications of Proteins (M.J. Schlesinger, eds.), pp. 21-58. Boca Raton. CRC Press.
    • (1992) Lipid Modifications of Proteins , pp. 21-58
    • Duronio, R.J.1    Rudnick, D.A.2    Knoll, L.J.3    Johnson, D.R.4    Gordon, J.I.5
  • 26
    • 0028221481 scopus 로고
    • Cloning of two novel ADP-ribosylation factor-like proteins and characterization of their differential expression in 3T3-L1 Cells
    • Schurmann, A., Breiner, M., Becker, W., Huppertz, C., Kainulainen, H., Kentrup, H. and Joost, H.-G. (1994) Cloning of two novel ADP-ribosylation factor-like proteins and characterization of their differential expression in 3T3-L1 Cells. J. Biol. Chem. 269, 15683-15688.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15683-15688
    • Schurmann, A.1    Breiner, M.2    Becker, W.3    Huppertz, C.4    Kainulainen, H.5    Kentrup, H.6    Joost, H.-G.7
  • 28
    • 0025773893 scopus 로고
    • Differential expression during development of ADP-ribosylation factors, 20-kDa guanine nucleotide-binding protein activators of cholera toxin
    • Tsai, S.-C., Adamik, R., Tsuchiya, M., Chang, P.P., Moss, J. and Vaughan, M. (1991) Differential expression during development of ADP-ribosylation factors, 20-kDa guanine nucleotide-binding protein activators of cholera toxin. J. Biol. Chem. 266, 8213-8219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8213-8219
    • Tsai, S.-C.1    Adamik, R.2    Tsuchiya, M.3    Chang, P.P.4    Moss, J.5    Vaughan, M.6
  • 29
    • 0014106537 scopus 로고
    • Fine structure of the asexual stages of Plasmodium elongatum
    • Aikawa, M., Huff, C.G. and Sprinz, H. (1967) Fine structure of the asexual stages of Plasmodium elongatum. J. Cell Biol. 34, 229-249.
    • (1967) J. Cell Biol. , vol.34 , pp. 229-249
    • Aikawa, M.1    Huff, C.G.2    Sprinz, H.3
  • 30
    • 0343780855 scopus 로고
    • Fine structure of malaria parasites in the various stages of development
    • Malaria (W.H. Wensdorfer and I. McGregor, eds.) New York
    • Aikawa, M. (1988) Fine structure of malaria parasites in the various stages of development. In: Malaria (W.H. Wensdorfer and I. McGregor, eds.) pp. 104-106. Churchill Livingstone. Vol. 1. New York.
    • (1988) Churchill Livingstone , vol.1 , pp. 104-106
    • Aikawa, M.1
  • 31
    • 0024276910 scopus 로고
    • Do GTPases direct membrane traffic in secretion?
    • Bourne, H.R. (1988) Do GTPases direct membrane traffic in secretion? Cell 53, 669-671.
    • (1988) Cell , vol.53 , pp. 669-671
    • Bourne, H.R.1
  • 32
    • 0028908248 scopus 로고
    • Development induction of Golgi structure and function in the primitive eukaryote Giardia lamblia
    • Lujan, H.D., Marotta, A., Mowatt, M.R., Sciaky, N., Lippincott-Schwartz, J. and Nash, T.E. (1995) Development induction of Golgi structure and function in the primitive eukaryote Giardia lamblia. J. Biol. Chem. 270, 4612-4618.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4612-4618
    • Lujan, H.D.1    Marotta, A.2    Mowatt, M.R.3    Sciaky, N.4    Lippincott-Schwartz, J.5    Nash, T.E.6
  • 34
    • 0025908897 scopus 로고
    • The ras protein family: Evolutionary tree and role of conserved amino acids
    • Valencia, A., Chardin, P., Wittinghofer, A. and Sander, C. (1991) The ras protein family: evolutionary tree and role of conserved amino acids. Biochemistry 30, 4637-4648.
    • (1991) Biochemistry , vol.30 , pp. 4637-4648
    • Valencia, A.1    Chardin, P.2    Wittinghofer, A.3    Sander, C.4
  • 39
    • 0027146287 scopus 로고
    • Cloning and characterization of subunit genes of ribonucleotide reductase, a cell cycle-regulated enzyme, from Plasmodium falciparum
    • Chakrabarti, D., Schuster, S.M. and Chakrabarti, R. (1993) Cloning and characterization of subunit genes of ribonucleotide reductase, a cell cycle-regulated enzyme, from Plasmodium falciparum. Proc. Natl. Acad. Sci. USA 90, 12020-12024.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 12020-12024
    • Chakrabarti, D.1    Schuster, S.M.2    Chakrabarti, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.