메뉴 건너뛰기




Volumn 83, Issue 1, 1996, Pages 107-120

Identification and localization of rab6, separation of rab6 from ERD2 and implications for an 'unstacked' Golgi, in Plasmodium falciparum

Author keywords

ERD2; Golgi organization; malaria; rabs; secretion

Indexed keywords

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; GOLGI COMPLEX; IMMUNOELECTRON MICROSCOPY; INTRACELLULAR TRANSPORT; MALARIA; MAMMAL CELL; MOLECULAR CLONING; NONHUMAN; PLASMODIUM FALCIPARUM; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN TRANSPORT;

EID: 0030566712     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(96)02759-4     Document Type: Article
Times cited : (63)

References (52)
  • 1
    • 0023077578 scopus 로고
    • Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi
    • [1] Pfeffer, S.R. and Rothman, J.E. (1987) Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Ann. Rev. Biochem. 56, 829-852.
    • (1987) Ann. Rev. Biochem. , vol.56 , pp. 829-852
    • Pfeffer, S.R.1    Rothman, J.E.2
  • 2
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • [2] Rothman, J.E. and Orci, L. (1992) Molecular dissection of the secretory pathway. Nature 355, 409-415.
    • (1992) Nature , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 3
    • 0025233925 scopus 로고
    • Three-dimensional electron microscopy: Structure of the Golgi apparatus
    • [3] Rambourg, A. and Clermont, Y. (1990) Three-dimensional electron microscopy: structure of the Golgi apparatus. Eur. J. Cell Biol. 51, 189-200.
    • (1990) Eur. J. Cell Biol. , vol.51 , pp. 189-200
    • Rambourg, A.1    Clermont, Y.2
  • 4
    • 0026503134 scopus 로고
    • The Golgi complex: In vitro veritas?
    • [4] Mellman, I. and Simons, K. (1992) The Golgi complex: in vitro veritas?. Cell 68, 829-840.
    • (1992) Cell , vol.68 , pp. 829-840
    • Mellman, I.1    Simons, K.2
  • 5
    • 0027456544 scopus 로고
    • Secretory activities in Plasmodium
    • [5] Elmendorf, H.G. and Haldar, K. (1993) Secretory activities in Plasmodium. Parasitol. Today 9, 98-102.
    • (1993) Parasitol. Today , vol.9 , pp. 98-102
    • Elmendorf, H.G.1    Haldar, K.2
  • 6
    • 0343399662 scopus 로고
    • Plasmodium falciparum gene encoding a protein similar to the 78-kDa rat glucose-regulated stress protein
    • [6] Kumar, N., Syin, C., Carter, R., Quakyi, I., Miller, L.H. (1988) Plasmodium falciparum gene encoding a protein similar to the 78-kDa rat glucose-regulated stress protein. Proc. Natl. Acad. Sci. USA. 85, 6277-6281.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6277-6281
    • Kumar, N.1    Syin, C.2    Carter, R.3    Quakyi, I.4    Miller, L.H.5
  • 7
    • 0025743647 scopus 로고
    • Induction and localization of Plasmodium falciparum stress proteins related to the heat shock protein 70 family
    • [7] Kumar, N., Koski, G., Harada, M., Aikawa, M. and Zheng, H. (1991) Induction and localization of Plasmodium falciparum stress proteins related to the heat shock protein 70 family. Mol. Biochem. Parasitol. 48, 47-58.
    • (1991) Mol. Biochem. Parasitol. , vol.48 , pp. 47-58
    • Kumar, N.1    Koski, G.2    Harada, M.3    Aikawa, M.4    Zheng, H.5
  • 10
    • 0021860850 scopus 로고
    • Acylation of a Plasmodium falciparum merozoitc surface antigen via sn-1.2-diacylglycerol
    • [10] Haldar, K., Ferguson, M.A.J. and Cross, G.A.M. (1985) Acylation of a Plasmodium falciparum merozoitc surface antigen via sn-1.2-diacylglycerol. J. Biol. Chem. 260, 4969-4974.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4969-4974
    • Haldar, K.1    Ferguson, M.A.J.2    Cross, G.A.M.3
  • 12
    • 0029869566 scopus 로고    scopus 로고
    • Structural analysis of the glycosyl-phosphatidylinositol membrane anchor of the merozoite surface proteins-1 and -2 of Plasmodium falciparum
    • [12] Gerold, P., Schofield, L., Blackmail, M.J., Holder, A.A. and Schwarz, R.T. (1996) Structural analysis of the glycosyl-phosphatidylinositol membrane anchor of the merozoite surface proteins-1 and -2 of Plasmodium falciparum. Mol. Biochem. Parasitol. 75, 131-143.
    • (1996) Mol. Biochem. Parasitol. , vol.75 , pp. 131-143
    • Gerold, P.1    Schofield, L.2    Blackmail, M.J.3    Holder, A.A.4    Schwarz, R.T.5
  • 13
    • 0026691491 scopus 로고
    • Brefeldin A inhibits protein secretion and parasite maturation in the ring stage of Plasmodium falciparum
    • [13] Crary, J.L. and Haldar, K. (1992) Brefeldin A inhibits protein secretion and parasite maturation in the ring stage of Plasmodium falciparum. Mol. Biochem. Parasitol. 53, 185-192.
    • (1992) Mol. Biochem. Parasitol. , vol.53 , pp. 185-192
    • Crary, J.L.1    Haldar, K.2
  • 14
    • 0026579552 scopus 로고
    • Synthesis and secretion of proteins by released malarial parasites
    • [14] 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
  • 15
    • 0028130379 scopus 로고
    • Plasmodium voelii: Brefeldin A-sensitive processing of proteins targeted to the rhoptries
    • [15] Ogun, S.A. and Holder, A.A. (1994) Plasmodium voelii: brefeldin A-sensitive processing of proteins targeted to the rhoptries. Exp. Parasitol. 79, 270-278.
    • (1994) Exp. Parasitol. , vol.79 , pp. 270-278
    • Ogun, S.A.1    Holder, A.A.2
  • 16
    • 0029415127 scopus 로고
    • The secretory pathway of Plasmodium falciparum regulates transport of p82 Rap-1 to the rhoptries
    • [16] Howard, R.F. and Schmidt, C.M. (1995) The secretory pathway of Plasmodium falciparum regulates transport of p82 Rap-1 to the rhoptries. Mol. Biochem. Parasitol. 74, 43-54.
    • (1995) Mol. Biochem. Parasitol. , vol.74 , pp. 43-54
    • Howard, R.F.1    Schmidt, C.M.2
  • 17
    • 0028131368 scopus 로고
    • Biosynthetic export and processing of a 45 kDa protein detected in membrane clefts of erythrocytes infected with Plasmodium falciparum
    • [17] Das, A., Elmendorf, H.G., Li, W-I. and Haldar, K. (1994) Biosynthetic export and processing of a 45 kDa protein detected in membrane clefts of erythrocytes infected with Plasmodium falciparum. Biochem. J. 302, 487-496.
    • (1994) Biochem. J. , vol.302 , pp. 487-496
    • Das, A.1    Elmendorf, H.G.2    Li, W.-I.3    Haldar, K.4
  • 18
    • 0027501330 scopus 로고
    • Identification and localization of ERD2 in the malaria parasite Plasmodium falciparum: Separation of sites of sphingomyelin synthesis and implications for the organization of the Golgi
    • [18] Elmendorf, H.G. and Haldar, K. (1993) Identification and localization of ERD2 in the malaria parasite Plasmodium falciparum: separation of sites of sphingomyelin synthesis and implications for the organization of the Golgi. EMBO J. 12, 4763-4773.
    • (1993) EMBO J. , vol.12 , pp. 4763-4773
    • Elmendorf, H.G.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
    • [19] Elmendorf, H.G. and Haldar, K. (1994) Plasmodium falciparum exports the Golgi marker sphingomyelin synthase into a tubovesicular 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
  • 20
    • 0025940095 scopus 로고
    • The accumulation and metabolism of a fluorescent ceramide derivative in Plasmodium falciparum-infected erythrocytes
    • [20] Haldar, K., Uyetake, E., Ghori, N., Elmendorf, H.G. and Li, W-I. (1991) The accumulation and metabolism of a fluorescent ceramide derivative in Plasmodium falciparum-infected erythrocytes. Mol. Biochem. Parasitol. 49, 143-156.
    • (1991) Mol. Biochem. Parasitol. , vol.49 , pp. 143-156
    • Haldar, K.1    Uyetake, E.2    Ghori, N.3    Elmendorf, H.G.4    Li, W.-I.5
  • 21
    • 0026016879 scopus 로고
    • Intracellular transport and metabolism of sphingomyelin
    • [21] Koval, M. and Pagano, R.E. (1991) Intracellular transport and metabolism of sphingomyelin. Biochim. Biophys. Acta 1082, 113-125.
    • (1991) Biochim. Biophys. Acta , vol.1082 , pp. 113-125
    • Koval, M.1    Pagano, R.E.2
  • 22
    • 0025323167 scopus 로고
    • Sphingomyelin synthesis in rat liver occurs predominantly at the cis and medial cisternae of the Golgi apparatus
    • [22] Futerman, A.H., Stieger, B., Hubbard, A.L. and Pagano, R.E. (1990) Sphingomyelin synthesis in rat liver occurs predominantly at the cis and medial cisternae of the Golgi apparatus. J. Biol. Chem. 265, 8650-8657.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8650-8657
    • Futerman, A.H.1    Stieger, B.2    Hubbard, A.L.3    Pagano, R.E.4
  • 24
    • 0029022032 scopus 로고
    • Sphingolipid synthesis as a novel target for chemotherapy against malaria parasites
    • [24] Lauer, S., Ghori, N. and Haldar, K. (1995) Sphingolipid synthesis as a novel target for chemotherapy against malaria parasites. Proc. Natl. Acad. Sci. USA. 92, 9181-9185.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9181-9185
    • Lauer, S.1    Ghori, N.2    Haldar, K.3
  • 25
    • 0025289981 scopus 로고
    • The ERD2 gene determines the specificity of the luminal ER protein retention system
    • [25] Lewis, M.J., Sweet, D.J. and Pelham, H.R.B. (1990) The ERD2 gene determines the specificity of the luminal ER protein retention system. Cell 61, 1359-1363.
    • (1990) Cell , vol.61 , pp. 1359-1363
    • Lewis, M.J.1    Sweet, D.J.2    Pelham, H.R.B.3
  • 26
    • 0026604647 scopus 로고
    • Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum
    • [26] Lewis, M.J. and Pelham, H.R.B. (1992) Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum. Cell 68, 353-364.
    • (1992) Cell , vol.68 , pp. 353-364
    • Lewis, M.J.1    Pelham, H.R.B.2
  • 28
    • 0029101662 scopus 로고
    • A minimalist view of the secretory pathway in Plasmodium falciparum
    • [28] Banting, G., Benting, J. and Lingelbach, K. (1995) A minimalist view of the secretory pathway in Plasmodium falciparum. Trends Cell Biol., 340-343.
    • (1995) Trends Cell Biol. , pp. 340-343
    • Banting, G.1    Benting, J.2    Lingelbach, K.3
  • 29
    • 0027333422 scopus 로고
    • The role of GTP binding proteins in transport along the exocytic pathway
    • [29] Ferro-Novick, S. and Novick, P. (1993) The role of GTP binding proteins in transport along the exocytic pathway. Ann. Rev. Cell Biol. 9, 575-599.
    • (1993) Ann. Rev. Cell Biol. , vol.9 , pp. 575-599
    • Ferro-Novick, S.1    Novick, P.2
  • 30
    • 0025363426 scopus 로고
    • Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments
    • [30] Chavrier, P., Parton, R.G., Hauri, H-P., Simons, K. and Zerial, M. (1990) Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell 62, 317-329.
    • (1990) Cell , vol.62 , pp. 317-329
    • Chavrier, P.1    Parton, R.G.2    Hauri, H.-P.3    Simons, K.4    Zerial, M.5
  • 31
    • 0027525103 scopus 로고
    • Friends and family: The role of the Rab GTPases in vesicular traffic
    • [31] Novick, P. and Brennwald, P. (1993) Friends and family: The role of the Rab GTPases in vesicular traffic. Cell 75, 597-601.
    • (1993) Cell , vol.75 , pp. 597-601
    • Novick, P.1    Brennwald, P.2
  • 32
    • 0027640399 scopus 로고
    • Rab GTPases in vesicular transport
    • [32] Zerial, M. and Stenmark, H. (1993) Rab GTPases in vesicular transport. Curr. Opin. Cell Biol. 5, 613-620.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 613-620
    • Zerial, M.1    Stenmark, H.2
  • 33
    • 0027095750 scopus 로고
    • The small GTP binding protein rab6p is distributed from medial Golgi to the trans-Golgi network as determined by a confocal microscopic approach
    • [33] Antony, C., Cibert, C., Geraud, G., Santa Maria, A., Maro, B., Mayau, V. and Goud, B. (1992) The small GTP binding protein rab6p is distributed from medial Golgi to the trans-Golgi network as determined by a confocal microscopic approach. J. Cell Sci. 103, 785-796.
    • (1992) J. Cell Sci. , vol.103 , pp. 785-796
    • Antony, C.1    Cibert, C.2    Geraud, G.3    Santa Maria, A.4    Maro, B.5    Mayau, V.6    Goud, B.7
  • 34
    • 0027997071 scopus 로고
    • The small GTP binding protein rab6p functions in intra-Golgi transport
    • [34] Martinez, O., Schmidt, A., Salamero, J., Hoflack, B., Roa, M. and Goud, B. (1994) The small GTP binding protein rab6p functions in intra-Golgi transport. J. Cell Biol. 127, 1575-1588.
    • (1994) J. Cell Biol. , vol.127 , pp. 1575-1588
    • Martinez, O.1    Schmidt, A.2    Salamero, J.3    Hoflack, B.4    Roa, M.5    Goud, B.6
  • 35
    • 0028926819 scopus 로고
    • Localization of the small GTP-binding rab1p to early compartments of the secretory pathway
    • [35] Saraste, J., Lahtinen, U. and Goud, B. (1995) Localization of the small GTP-binding rab1p to early compartments of the secretory pathway. J. Cell Sci. 108, 1541-1552.
    • (1995) J. Cell Sci. , vol.108 , pp. 1541-1552
    • Saraste, J.1    Lahtinen, U.2    Goud, B.3
  • 36
    • 0023619395 scopus 로고
    • Investigations of avidin and biotin for imaging applications
    • [36] Hnatowich, D.J., Virzi, F. and Rusckowski, M. (1987) Investigations of avidin and biotin for imaging applications. J. Nucl. Med. 28, 1294-1302.
    • (1987) J. Nucl. Med. , vol.28 , pp. 1294-1302
    • Hnatowich, D.J.1    Virzi, F.2    Rusckowski, M.3
  • 37
    • 0017311840 scopus 로고
    • Human malaria in continuous culture
    • [37] Trager, W. and Jensen, J.B. (1976) Human malaria in continuous culture. Science 193, 673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 38
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythrocytic stages in culture
    • [38] Lambros, C. and Vanderberg, J.P. (1979) Synchronization of Plasmodium falciparum erythrocytic stages in culture. J. Parasitol. 65, 418-420.
    • (1979) J. Parasitol. , vol.65 , pp. 418-420
    • Lambros, C.1    Vanderberg, J.P.2
  • 39
    • 0027465101 scopus 로고
    • Multiple chromosomal populations of topisomerase II detected in vivo by time-lapse, three dimensional wide field microscopy
    • [39] Swedlow, J.R., Sedat, J.W. and Agard, D.A. (1993) Multiple chromosomal populations of topisomerase II detected in vivo by time-lapse, three dimensional wide field microscopy. Cell 9, 97-108.
    • (1993) Cell , vol.9 , pp. 97-108
    • Swedlow, J.R.1    Sedat, J.W.2    Agard, D.A.3
  • 40
    • 0027438327 scopus 로고
    • Gene sequence tags from Plasmodium falciparum genomic DNA fragments prepared by the genease activity of mung bean nuclease
    • [40] Reddy, G.R., Chakrabarti, D., Schuster, S.M., Ferl, R.J., Almira, E.C. and Dame, J.B. (1993) Gene sequence tags from Plasmodium falciparum genomic DNA fragments prepared by the genease activity of mung bean nuclease. Proc. Natl. Acad. Sci. 90, 9867-9871.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 9867-9871
    • Reddy, G.R.1    Chakrabarti, D.2    Schuster, S.M.3    Ferl, R.J.4    Almira, E.C.5    Dame, J.B.6
  • 41
    • 0025200302 scopus 로고
    • Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell line
    • [41] Chavrier, P., Vingron, M., Sander, C., Simons, K. and Zerial, M. (1990) Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell line. Mol. Cell Biol. 10, 6578-6585.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 6578-6585
    • Chavrier, P.1    Vingron, M.2    Sander, C.3    Simons, K.4    Zerial, M.5
  • 42
    • 0028170814 scopus 로고
    • Role of protein modification reactions in programming interactions between ras related GTPases and cell membranes
    • [42] Glomset, J.A. and Farnesworth, C.C. (1994) Role of protein modification reactions in programming interactions between ras related GTPases and cell membranes. Ann. Rev. Cell Biol 10, 181-205.
    • (1994) Ann. Rev. Cell Biol , vol.10 , pp. 181-205
    • Glomset, J.A.1    Farnesworth, C.C.2
  • 43
    • 0026554965 scopus 로고
    • GTP binding proteins in intracellular transport
    • [43] Pfeffer, S.R. (1992) GTP binding proteins in intracellular transport. Trends Cell Biol. 2, 41-46.
    • (1992) Trends Cell Biol. , vol.2 , pp. 41-46
    • Pfeffer, S.R.1
  • 45
    • 0027240379 scopus 로고
    • A cytosolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans Golgi network
    • [45] Jones, S.M., Crossby, J.R., Salamero, J. and Howell, K.E. (1993) A cytosolic complex of p62 and rab6 associates with TGN38/41 and is involved in budding of exocytic vesicles from the trans Golgi network. J. Cell Biol. 122, 775-788.
    • (1993) J. Cell Biol. , vol.122 , pp. 775-788
    • Jones, S.M.1    Crossby, J.R.2    Salamero, J.3    Howell, K.E.4
  • 46
    • 0028008838 scopus 로고
    • A small rabGTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells
    • [46] Zahraoui, A., Joberty, G., Arpin, M., Fontaine, J.J., Hellio, R., Tavitian, A. and Louvard, D. (1994) A small rabGTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells. J. Cell Biol. 124, 101-115.
    • (1994) J. Cell Biol. , vol.124 , pp. 101-115
    • Zahraoui, A.1    Joberty, G.2    Arpin, M.3    Fontaine, J.J.4    Hellio, R.5    Tavitian, A.6    Louvard, D.7
  • 47
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • [47] Rothman, J.E. and Wieland, F.T. (1996) Protein sorting by transport vesicles. Science 272, 227-234.
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 49
    • 0028908248 scopus 로고
    • Developmental induction of Golgi structure and function in the primitive eukaryote Giardia lamblia
    • [49] Lujan, H.D., Marotta, A., Mowatt, M.R., Sciaky, N., Lippincott-Schwarz, J. and Nash, T.E. (1995) Developmental 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-Schwarz, J.5    Nash, T.E.6
  • 50
    • 0028153084 scopus 로고
    • Giardia Lamblia: Ultrastructural basis of protein transport during growth and encystation
    • [50] McCaffery, J.M. and Gillin, F.D. (1994) Giardia Lamblia: ultrastructural basis of protein transport during growth and encystation. Exp. Parasitol. 79, 220-235.
    • (1994) Exp. Parasitol. , vol.79 , pp. 220-235
    • McCaffery, J.M.1    Gillin, F.D.2
  • 51
    • 0026633791 scopus 로고
    • A brefeldin A-like phenotype is induced by the overexpression of a human ERD-2-like protein, ELP-1
    • [51] Hsu, V.W., Shah, N. and Klausner, R.D. (1992) A brefeldin A-like phenotype is induced by the overexpression of a human ERD-2-like protein, ELP-1. Cell 69, 625-635.
    • (1992) Cell , vol.69 , pp. 625-635
    • Hsu, V.W.1    Shah, N.2    Klausner, R.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.