메뉴 건너뛰기




Volumn 109, Issue 12, 1996, Pages 2915-2926

TGN38-green fluorescent protein hybrid proteins expressed in stably transfected eukaryotic cells provide a tool for the real-time, in vivo study of membrane traffic pathways and suggest a possible role for ratTGN38

Author keywords

Brefeldin A; Green fluorescent protein; Trans Golgi network

Indexed keywords

BREFELDIN A; CELL MEMBRANE PROTEIN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN;

EID: 0030451424     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (76)

References (26)
  • 1
    • 0345012707 scopus 로고
    • Structural relationships between clathrin assembly proteins from the Golgi and the plasma-membrane
    • Ahle, S., Mann, A., Eichelsbacher, U. and Ungewickel, E. (1988). Structural relationships between clathrin assembly proteins from the Golgi and the plasma-membrane. EMBO J. 7, 919-929.
    • (1988) EMBO J. , vol.7 , pp. 919-929
    • Ahle, S.1    Mann, A.2    Eichelsbacher, U.3    Ungewickel, E.4
  • 2
    • 0025245001 scopus 로고
    • Mannosidase II and the 135 k-Da Golgi-specifc antigen recognized by monoclonal antibody 53FC3 are the same dimeric protein
    • Baron, M. D. and Garoff, H. (1990). Mannosidase II and the 135 k-Da Golgi-specifc antigen recognized by monoclonal antibody 53FC3 are the same dimeric protein. J. Biol. Chem. 265, 19928-19931.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19928-19931
    • Baron, M.D.1    Garoff, H.2
  • 3
    • 0019174555 scopus 로고
    • Use of a novel rapid preparation of fat-cell plasma membranes employing Percoll to investigate the effects of insulin and adrenaline on membrane protein phosphorylation within intact fat cells
    • Belsham, G. J., Denton, R. M. and Tanner, M. J. (1980). Use of a novel rapid preparation of fat-cell plasma membranes employing Percoll to investigate the effects of insulin and adrenaline on membrane protein phosphorylation within intact fat cells. Biochem. J. 192, 457-467.
    • (1980) Biochem. J. , vol.192 , pp. 457-467
    • Belsham, G.J.1    Denton, R.M.2    Tanner, M.J.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
  • 5
    • 0020338604 scopus 로고
    • A monoclonal antibody against a 135-k Golgi membrane protein
    • Burke, B., Griffiths, G., Reggio, H., Louvard, D. and Warren, G. (1982) A monoclonal antibody against a 135-k Golgi membrane protein. EMBO J. 1, 1621-1628.
    • (1982) EMBO J. , vol.1 , pp. 1621-1628
    • Burke, B.1    Griffiths, G.2    Reggio, H.3    Louvard, D.4    Warren, G.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
    • 0028014372 scopus 로고
    • Vacuolar ATPase activity is required for endosomal carrier vesicle formation
    • Clague, M. J., Urbe, S., Aniento, F. and Gruenberg, J. (1994). Vacuolar ATPase activity is required for endosomal carrier vesicle formation. J. Biol. Chem. 269, 21-24.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21-24
    • Clague, M.J.1    Urbe, S.2    Aniento, F.3    Gruenberg, J.4
  • 8
    • 2842574825 scopus 로고
    • TGN38 forms a macromolecular complex with small GTP-binding proteins - Functional-studies using a cell-free assay
    • Crosby, J. R., Jones, S. M. and Howell, K. E. (1992). TGN38 forms a macromolecular complex with small GTP-binding proteins - functional-studies using a cell-free assay. Mol. Biol. Cell 3, A 308.
    • (1992) Mol. Biol. Cell , vol.3
    • Crosby, J.R.1    Jones, S.M.2    Howell, K.E.3
  • 10
    • 0030051441 scopus 로고    scopus 로고
    • The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor
    • Dittié, A. S., Hajibagheri, N. and Tooze, S. A. (1996). The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor. J. Cell Biol. 132, 523-536.
    • (1996) J. Cell Biol. , vol.132 , pp. 523-536
    • Dittié, A.S.1    Hajibagheri, N.2    Tooze, S.A.3
  • 11
    • 0028580734 scopus 로고
    • Wavelength mutations and posttranslational autoxidation of green fluorescent protein
    • Heim, R., Prasher, D. C. and Tsien, R. Y. (1994). Wavelength mutations and posttranslational autoxidation of green fluorescent protein. Proc. Nat. Acad. Sci. USA 91, 12501-12504.
    • (1994) Proc. Nat. Acad. Sci. USA , vol.91 , pp. 12501-12504
    • Heim, R.1    Prasher, D.C.2    Tsien, R.Y.3
  • 12
    • 0028232868 scopus 로고
    • Okadaic acid treatment leads to a fragmentation of the trans-Golgi network and an increase in expression of TGN38 at the cell-surface
    • Horn, M. and Banting, G. (1994). Okadaic acid treatment leads to a fragmentation of the trans-Golgi network and an increase in expression of TGN38 at the cell-surface. Biochem. J. 301, 69-73.
    • (1994) Biochem. J. , vol.301 , pp. 69-73
    • Horn, M.1    Banting, G.2
  • 13
    • 0029160620 scopus 로고
    • Visualization of protein-transport along the secretory pathway using green fluorescent protein
    • Kaether, C. and Gerdes, H. H. (1995). Visualization of protein-transport along the secretory pathway using green fluorescent protein. FEBS Lett. 369, 267-271.
    • (1995) FEBS Lett. , vol.369 , pp. 267-271
    • Kaether, C.1    Gerdes, H.H.2
  • 14
    • 0026472647 scopus 로고
    • The trans-Golgi network can be dissected structurally and functionally from the cisternae of the Golgi-complex by brefeldin-A
    • Ladinsky, M. S. and Howell, K. E. (1992). The trans-Golgi network can be dissected structurally and functionally from the cisternae of the Golgi-complex by brefeldin-A. Eur. J. Cell Biol. 59, 92-105.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 92-105
    • Ladinsky, M.S.1    Howell, K.E.2
  • 15
    • 0025940101 scopus 로고
    • Brefeldin-As effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic
    • Lippincott-Schwartz, J., Yuan, L., Tipper, C., Amherdt, M., Orci, L. and Klausner, R. D. (1991). Brefeldin-As effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic. Cell 67, 601-616.
    • (1991) Cell , vol.67 , pp. 601-616
    • Lippincott-Schwartz, J.1    Yuan, L.2    Tipper, C.3    Amherdt, M.4    Orci, L.5    Klausner, R.D.6
  • 16
    • 0027514907 scopus 로고
    • Eukaryotic membrane traffic - Retrieval and retention mechanisms to achieve organelle residence
    • Luzio, J. P. and Banting, G. (1993). Eukaryotic membrane traffic - retrieval and retention mechanisms to achieve organelle residence. Trends Biochem. Sci. 18, 395-398.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 395-398
    • Luzio, J.P.1    Banting, G.2
  • 17
    • 0020804564 scopus 로고
    • Reduced temperature prevents transfer of a membrane glycoprotein to the cell-surface but does not prevent terminal glycosylation
    • Matlin, K. S. and Simons, K. (1983). Reduced temperature prevents transfer of a membrane glycoprotein to the cell-surface but does not prevent terminal glycosylation Cell 34, 233-243.
    • (1983) Cell , vol.34 , pp. 233-243
    • Matlin, K.S.1    Simons, K.2
  • 18
    • 0027489133 scopus 로고
    • Sorting of membrane-proteins in the secretory pathway
    • Pelham, H. R. B. and Munro, S. (1993). Sorting of membrane-proteins in the secretory pathway. Cell 75, 603-605.
    • (1993) Cell , vol.75 , pp. 603-605
    • Pelham, H.R.B.1    Munro, S.2
  • 19
    • 9044241677 scopus 로고    scopus 로고
    • Primate homologues of rat TGN38: Primary structure, expression and functional implications
    • Ponnambalam, S., Girotti, M., Yaspo, M.-L., Owen, C. W., Perry, A. C. F., Suganuma, T., et al. (1996). Primate homologues of rat TGN38: primary structure, expression and functional implications. J. Cell Sci. 109, 675-685.
    • (1996) J. Cell Sci. , vol.109 , pp. 675-685
    • Ponnambalam, S.1    Girotti, M.2    Yaspo, M.-L.3    Owen, C.W.4    Perry, A.C.F.5    Suganuma, T.6
  • 20
    • 0028905820 scopus 로고
    • Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides
    • Rabouille, C., Hui, N., Hunte, F., Kieckbusch, R., Berger, E. G., Warren, G., et al. (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.2    Hunte, F.3    Kieckbusch, R.4    Berger, E.G.5    Warren, G.6
  • 21
    • 0026570788 scopus 로고
    • Perturbation of the morphology of the trans-Golgi network following brefeldin-A treatment - Redistribution of a TGN-specific integral membrane-protein. TGN38
    • Reaves, B. and Banting, G. (1992). Perturbation of the morphology of the trans-Golgi network following brefeldin-A treatment - redistribution of a TGN-specific integral membrane-protein. TGN38. J. Cell Biol. 116, 85-94.
    • (1992) J. Cell Biol. , vol.116 , pp. 85-94
    • Reaves, B.1    Banting, G.2
  • 22
    • 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
  • 23
    • 0027968347 scopus 로고
    • Overexpression of TGN38/41 leads to mislocalisation of gamma-adaptin
    • Reaves, B. and Banting, G. (1994a). Overexpression of TGN38/41 leads to mislocalisation of gamma-adaptin. FEBS Lett. 351, 448-456.
    • (1994) FEBS Lett. , vol.351 , pp. 448-456
    • Reaves, B.1    Banting, G.2
  • 24
    • 0028305440 scopus 로고
    • Vacuolar ATPase inactivation blocks recycling to the trans-Golgi network from the plasma-membrane
    • Reaves, B. and Banting, G. (1994b). Vacuolar ATPase inactivation blocks recycling to the trans-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
  • 25
    • 0026627966 scopus 로고
    • Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells - Effects of Brefeldin-A and G-protein activators
    • Robinson, M. S. and Kreis, T. E. (1992). Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells - effects of Brefeldin-A and G-protein activators. Cell 69, 129-138.
    • (1992) Cell , vol.69 , pp. 129-138
    • Robinson, M.S.1    Kreis, T.E.2
  • 26
    • 0021148465 scopus 로고
    • Pre-Golgi and post-Golgi vesicles operate in the transport of semliki forest virus membrane-glvcoproteins to the cell-surface
    • Saraste, J. and Kuismanen, E. (1984). Pre-Golgi and post-Golgi vesicles operate in the transport of semliki forest virus membrane-glvcoproteins to the cell-surface. Cell 38, 535-549.
    • (1984) Cell , vol.38 , pp. 535-549
    • Saraste, J.1    Kuismanen, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.