메뉴 건너뛰기




Volumn 109, Issue 3, 1996, Pages 675-685

Primate homologues of rat TGN38: Primary structure, expression and functional implications

Author keywords

Endosome; Mucin; TGN38; TGN46; Trans Golgi network

Indexed keywords

COMPLEMENTARY DNA; MEMBRANE PROTEIN;

EID: 9044241677     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (96)

References (44)
  • 2
    • 0027639817 scopus 로고
    • Biogenesis of constitutive secretory vesicles, secretory granules and synaptic vesicles
    • Bauerfeind, R. and Huttner, W. B. (1993). Biogenesis of constitutive secretory vesicles, secretory granules and synaptic vesicles. Curr. Opin. Cell Biol. 5, 628-635.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 628-635
    • Bauerfeind, R.1    Huttner, W.B.2
  • 3
    • 0027159260 scopus 로고
    • Tgn38 is maintained in the trans-golgi network by tyrosine-containing motif in the cytoplasmic domain
    • Bos, K., Wraight, C. and Stanley, K. (1993). Tgn38 is maintained in the trans-golgi network by tyrosine-containing motif in the cytoplasmic domain. EMBO J. 12, 2219-2228.
    • (1993) EMBO J. , vol.12 , pp. 2219-2228
    • Bos, K.1    Wraight, C.2    Stanley, K.3
  • 4
    • 0025308561 scopus 로고
    • A new recombinant DNA strategy for the molecular cloning of rare membrane proteins
    • Brake, B., Braghetta, P., Banting, G., Luzio, J. P. and Stanley, K. K. (1990). A new recombinant DNA strategy for the molecular cloning of rare membrane proteins. Biochem. J. 267, 631-637.
    • (1990) Biochem. J. , vol.267 , pp. 631-637
    • Brake, B.1    Braghetta, P.2    Banting, G.3    Luzio, J.P.4    Stanley, K.K.5
  • 6
    • 0028283375 scopus 로고
    • Retrieval of TGN proteins from the cell surface requires endosomal acidification
    • Chapman, R. E. and Munro, S. (1994). Retrieval of TGN proteins from the cell surface requires endosomal acidification EMBO J. 13, 2305-2312.
    • (1994) EMBO J. , vol.13 , pp. 2305-2312
    • Chapman, R.E.1    Munro, S.2
  • 7
    • 0026928690 scopus 로고
    • Mucins, structure, function, and associations with malignancy
    • Devine, P. L. and McKenzie, F. C. (1992). Mucins, structure, function, and associations with malignancy BioEssays 14, 619-625.
    • (1992) BioEssays , vol.14 , pp. 619-625
    • Devine, P.L.1    McKenzie, F.C.2
  • 8
    • 0029053448 scopus 로고
    • The role of N-glycans in the secretory pathway
    • Fiedler, K. and Simons, K. (1995). The role of N-glycans in the secretory pathway. Cell 81, 309-312.
    • (1995) Cell , vol.81 , pp. 309-312
    • Fiedler, K.1    Simons, K.2
  • 9
    • 0026527823 scopus 로고
    • Structure and expression of the rat epididymal secretory protein I gene : An androgen-regulated member of the lipocalin superfamily with a rare splice donor site
    • Girotti, M., Jones, R., Emery, D. C., Chia, W. and Hall, L. (1992). Structure and expression of the rat epididymal secretory protein I gene : an androgen-regulated member of the lipocalin superfamily with a rare splice donor site. Biochem. J. 281, 203-210.
    • (1992) Biochem. J. , vol.281 , pp. 203-210
    • Girotti, M.1    Jones, R.2    Emery, D.C.3    Chia, W.4    Hall, L.5
  • 10
    • 0022975133 scopus 로고
    • The trans-Golgi network: Sorting at the exit site of the Golgi complex
    • Griffiths, G. and Simons, K. (1986). The trans-Golgi network: sorting at the exit site of the Golgi complex. Science 234, 438-443.
    • (1986) Science , vol.234 , pp. 438-443
    • Griffiths, G.1    Simons, K.2
  • 11
    • 0028984235 scopus 로고
    • Immunocytochemical localization of β-COP to the ER-Golgi boundary and the TGN
    • Griffiths, G., Pepperkok, R., Krinjse-Locker, J. and Kreis, T. (1995). Immunocytochemical localization of β-COP to the ER-Golgi boundary and the TGN. J. Cell Sci. 108, 2839-2856.
    • (1995) J. Cell Sci. , vol.108 , pp. 2839-2856
    • Griffiths, G.1    Pepperkok, R.2    Krinjse-Locker, J.3    Kreis, T.4
  • 13
    • 0025281993 scopus 로고
    • Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum
    • Hopkins, C. R., Gibson, A., Shipman, M. and Miller, K. (1990). Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum. Nature 346, 335-339.
    • (1990) Nature , vol.346 , pp. 335-339
    • Hopkins, C.R.1    Gibson, A.2    Shipman, M.3    Miller, K.4
  • 14
    • 0027395956 scopus 로고
    • A tyrosine-containing sequence within the cytoplasmic domain of TGN38 confers localization to the trans-Golgi network
    • Humphrey, J. S., Peters, P. J., Yuan, L. C. and Bonifacino, J. S. (1993). A tyrosine-containing sequence within the cytoplasmic domain of TGN38 confers localization to the trans-Golgi network. J. Cell Biol. 120, 1123-1135.
    • (1993) J. Cell Biol. , vol.120 , pp. 1123-1135
    • Humphrey, J.S.1    Peters, P.J.2    Yuan, L.C.3    Bonifacino, J.S.4
  • 15
    • 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
    • Jones, S. M., Crosby, 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    Crosby, J.R.2    Salamero, J.3    Howell, K.E.4
  • 16
    • 0029041297 scopus 로고
    • Strain-specific presence of two TGN38 isoforms and absence of TGN41 in mouse
    • Kasai, K., Takahashi, S., Murakami, K. and Nakayama, K. (1995) Strain-specific presence of two TGN38 isoforms and absence of TGN41 in mouse J. Biol. Chem 270, 14471-14476.
    • (1995) J. Biol. Chem , vol.270 , pp. 14471-14476
    • Kasai, K.1    Takahashi, S.2    Murakami, K.3    Nakayama, K.4
  • 17
    • 0028123669 scopus 로고
    • A protein-specific monoclonal antibody to rat liver beta-1-4 galactosyltransferase and its application in immunohistochemistry
    • Kawano, J. I., Ide, S., Oinuma, T. and Suganuma, T. (1994) A protein-specific monoclonal antibody to rat liver beta-1-]4 galactosyltransferase and its application in immunohistochemistry. J. Histothem. Cytochem. 42, 363-369.
    • (1994) J. Histothem. Cytochem. , vol.42 , pp. 363-369
    • Kawano, J.I.1    Ide, S.2    Oinuma, T.3    Suganuma, T.4
  • 18
    • 0026637316 scopus 로고
    • Structure and function of the mannose 6-phosphate insulin-like growth factor II receptors
    • Kornfeld, S. (1992) Structure and function of the mannose 6-phosphate insulin-like growth factor II receptors. Annu. Rev Biochem. 61, 307-330.
    • (1992) Annu. Rev Biochem. , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 19
  • 20
    • 0027547466 scopus 로고
    • Molecular biology of neuronal intermediate filaments
    • Liem, R. K. H. (1993). Molecular biology of neuronal intermediate filaments. Curr. Opin. Cell Biol. 5, 12-16.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 12-16
    • Liem, R.K.H.1
  • 21
    • 0025148186 scopus 로고
    • Identification, sequencing and expression of an integral mebrane protein of the trans-Golgi network (TGN38)
    • Luzio, J. P., Brake, B., Banting, G., Howell, K. E., Braghetta, P. and Stanley, K. K. (1990). Identification, sequencing and expression of an integral mebrane protein of the trans-Golgi network (TGN38). Biochem. J. 270, 97-102.
    • (1990) Biochem. J. , vol.270 , pp. 97-102
    • Luzio, J.P.1    Brake, B.2    Banting, G.3    Howell, K.E.4    Braghetta, P.5    Stanley, K.K.6
  • 22
    • 0028920639 scopus 로고
    • Distinct coated vesicles labeled for p200 bud fromtrans-Golgi network membranes
    • Narula, N. and Stow, J. L. (1995). Distinct coated vesicles labeled for p200 bud fromtrans-Golgi network membranes. Proc. Nat. Acad Sci. USA 92, 2874-2878.
    • (1995) Proc. Nat. Acad Sci. USA , vol.92 , pp. 2874-2878
    • Narula, N.1    Stow, J.L.2
  • 23
    • 0024314706 scopus 로고
    • Retrieval of transmembrane proteins to the endoplasmic reticulum
    • Nilsson, T., Jackson, M. R. and Peterson, P. A. (1989) Retrieval of transmembrane proteins to the endoplasmic reticulum. Cell 58, 707-718.
    • (1989) Cell , vol.58 , pp. 707-718
    • Nilsson, T.1    Jackson, M.R.2    Peterson, P.A.3
  • 24
    • 0027472941 scopus 로고
    • Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells
    • Nilsson, T., Pypaert, M., Hoe, M. H., Slusarewicz, P., Berger, E. G. and Warren, G. (1993). Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells. J. Cell Biol. 120, 5-13.
    • (1993) J. Cell Biol. , vol.120 , pp. 5-13
    • Nilsson, T.1    Pypaert, M.2    Hoe, M.H.3    Slusarewicz, P.4    Berger, E.G.5    Warren, G.6
  • 25
    • 0027978637 scopus 로고
    • Retention and retrieval in the endoplasmic reticulum and Golgi apparatus
    • Nilsson, T. and Warren, G. (1994). Retention and retrieval in the endoplasmic reticulum and Golgi apparatus. Curr. Opin. Cell Biol. 6, 517-521.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 517-521
    • Nilsson, T.1    Warren, G.2
  • 26
    • 0027499531 scopus 로고
    • β-COP localizes mainly to the cis-Golgi side in exocrine pancreas
    • Oprins, A., Duden, R., Kreis, T., Geuze, H. J. and Slot, J. W. (1993). β-COP localizes mainly to the cis-Golgi side in exocrine pancreas. J. Cell Biol. 121, 49-59
    • (1993) J. Cell Biol. , vol.121 , pp. 49-59
    • Oprins, A.1    Duden, R.2    Kreis, T.3    Geuze, H.J.4    Slot, J.W.5
  • 27
    • 9044243060 scopus 로고
    • The role of the cytoplasmic tail domain in actin interactions and in the polarized localization of cell-associated mucin
    • Pemberton, L., Taylor-Papadimitriou, J. and Gendler, S. J. (1992). The role of the cytoplasmic tail domain in actin interactions and in the polarized localization of cell-associated mucin. MUCl. Biol. Cell 3, 266A.
    • (1992) MUCl. Biol. Cell , vol.3
    • Pemberton, L.1    Taylor-Papadimitriou, J.2    Gendler, S.J.3
  • 28
    • 0027220591 scopus 로고
    • b-cop is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo
    • Pepperkok, R., Scheel, J., Horstmann, H., Hauri, H. P., Griffiths, G., Kreis, T. E. (1993). b-cop is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell 74, 11-82.
    • (1993) Cell , vol.74 , pp. 11-82
    • Pepperkok, R.1    Scheel, J.2    Horstmann, H.3    Hauri, H.P.4    Griffiths, G.5    Kreis, T.E.6
  • 29
    • 0026714544 scopus 로고
    • Genetic-evidence for an androgen-regulated epididymal secretory glutathione-peroxidase whose transcript does not contain a selenocysteine codon
    • Perry, A. C. F., Jones, R., Niang, L. S. P., Jackson, R. M. and Hall, L. (1992). Genetic-evidence for an androgen-regulated epididymal secretory glutathione-peroxidase whose transcript does not contain a selenocysteine codon. Biochem. J. 285, 863-870.
    • (1992) Biochem. J. , vol.285 , pp. 863-870
    • Perry, A.C.F.1    Jones, R.2    Niang, L.S.P.3    Jackson, R.M.4    Hall, L.5
  • 30
    • 0028352920 scopus 로고
    • Sequence analysis of a mammalian phospholipid-binding protein from testis and epididymis and its distribution between spermatozoa and extracellular secretions
    • Perry, A. C. F., Hall, L., Bell, A. E. and Jones, R. (1994). Sequence analysis of a mammalian phospholipid-binding protein from testis and epididymis and its distribution between spermatozoa and extracellular secretions. Biochem. J. 301, 235-242.
    • (1994) Biochem. J. , vol.301 , pp. 235-242
    • Perry, A.C.F.1    Hall, L.2    Bell, A.E.3    Jones, R.4
  • 31
    • 0028351154 scopus 로고
    • The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network
    • Ponnambalam, S., Rabouille, C., Luzio, J. P., Nilsson, T. and Warren, G. (1994). The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network. J. Cell Biol. 125, 253-268.
    • (1994) J. Cell Biol. , vol.125 , pp. 253-268
    • Ponnambalam, S.1    Rabouille, C.2    Luzio, J.P.3    Nilsson, T.4    Warren, G.5
  • 32
    • 0028905820 scopus 로고
    • Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides
    • Rabouille, C., Hui, N. H., Watson, R., Hunte, F., Berger, E., Warren, G. and Nilsson, T. (1995). Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J. Cell Sci. 108, 1617-1627.
    • (1995) J. Cell Sci. , vol.108 , pp. 1617-1627
    • Rabouille, C.1    Hui, N.H.2    Watson, R.3    Hunte, F.4    Berger, E.5    Warren, G.6    Nilsson, T.7
  • 33
    • 0028305440 scopus 로고
    • Vacuolar ATPase inactivation blocks recycling to thetrans-golgi network from the plasma-membrane
    • Reaves, B. and Banting, G. (1994a). Vacuolar ATPase inactivation blocks recycling to thetrans-golgi network from the plasma-membrane. FEBS Lett. 345, 61-66.
    • (1994) FEBS Lett. , vol.345 , pp. 61-66
    • Reaves, B.1    Banting, G.2
  • 34
    • 0027968347 scopus 로고
    • Over-expression of TGN38/41 leads to mislocalisation of γ-adaptin
    • Reaves, B. and Banting, G. (1994b). Over-expression of TGN38/41 leads to mislocalisation of γ-adaptin. FEBS Lett. 351, 448-456.
    • (1994) FEBS Lett. , vol.351 , pp. 448-456
    • Reaves, B.1    Banting, G.2
  • 35
    • 0026606854 scopus 로고
    • Identification, molecular characterization and immunolocalization of an isoform of the trans-golgi network (TGN)-specific integral membrane-protein TGN38
    • Reaves, B., Wilde, A. and Banting, G. (1992). Identification, molecular characterization and immunolocalization of an isoform of the trans-golgi network (TGN)-specific integral membrane-protein TGN38 Biochem. J. 283, 313-316.
    • (1992) Biochem. J. , vol.283 , pp. 313-316
    • Reaves, B.1    Wilde, A.2    Banting, G.3
  • 36
    • 0027447921 scopus 로고
    • TGN38/41 recycles between the cell surface and the TGN: Brefeldin a affects its rate of return to the TGN
    • Reaves, B., Horn, M. and Banting, G. (1993). TGN38/41 recycles between the cell surface and the TGN: Brefeldin A affects its rate of return to the TGN. Mol. Biol. Cell 4, 93-105.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 93-105
    • Reaves, B.1    Horn, M.2    Banting, G.3
  • 37
    • 0028143698 scopus 로고
    • Mechanism of intracellular protein transport
    • Rothman, J. E. (1994). Mechanism of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 39
    • 0029100187 scopus 로고
    • The role of coat proteins in the biosynthesis of secretory proteins
    • Salama, N. R. and Schekman, R. W. (1995). The role of coat proteins in the biosynthesis of secretory proteins. Curr. Opin Cell Biol. 7, 536-543.
    • (1995) Curr. Opin Cell Biol. , vol.7 , pp. 536-543
    • Salama, N.R.1    Schekman, R.W.2
  • 41
    • 0027178838 scopus 로고
    • TGN38/41 - A molecule on the move?
    • Stanley, K. K. and Howell, K. E. (1993). TGN38/41 - A molecule on the move? Trends Cell Biol. 3, 252-255.
    • (1993) Trends Cell Biol. , vol.3 , pp. 252-255
    • Stanley, K.K.1    Howell, K.E.2
  • 42
    • 0027519431 scopus 로고
    • The SXYQRL sequence in the cytoplasmic domain of TGN38 plays a major role in trans-Golgi network localization
    • Wong, S. II. and Hong, W. (1993). The SXYQRL sequence in the cytoplasmic domain of TGN38 plays a major role in trans-Golgi network localization. J. Biol. Chem. 268, 22853-22862.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22853-22862
    • Wong, S.I.I.1    Hong, W.2
  • 43
    • 0029057892 scopus 로고
    • Control of p62 binding to tgn38/41 by phosphorylation
    • Zehavifeferman, R., Burgess, J. W. and Stanley, K. K. (1995). Control of p62 binding to tgn38/41 by phosphorylation. FEBS Lett 368, 122-124.
    • (1995) FEBS Lett , vol.368 , pp. 122-124
    • Zehavifeferman, R.1    Burgess, J.W.2    Stanley, K.K.3
  • 44
    • 0028762437 scopus 로고
    • The reference library system - Sharing biological material and experimental data
    • Zehetner, G. and Lehrach, H. ( 1994). The reference library system - sharing biological material and experimental data. Nature 367, 489-491.
    • (1994) Nature , vol.367 , pp. 489-491
    • Zehetner, G.1    Lehrach, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.