메뉴 건너뛰기




Volumn 65, Issue 18, 2008, Pages 2859-2874

Membrane traffic in the secretory pathway: Take the 'A' train: On fast tracks to the cell surface

Author keywords

Brefeldin A; Endosomes; Pre Golgi compartments; Rab1; Rafts; Secretory pathway; Yeast Ypt1

Indexed keywords

3 HYDROXY 3 METHYLGLUTARYL COENZYME A; ADAPTOR PROTEIN; ALPHA1 INTEGRIN; BREFELDIN A; CALSEQUESTRIN; CD45 ANTIGEN; CHOLESTEROL; CLASSICAL COMPLEMENT PATHWAY C3 C5 CONVERTASE; CLATHRIN; CONNEXIN 26; CONTACTIN; FLOTILLIN 1; GANGLIOSIDE GD3; GAP JUNCTION PROTEIN; GLATIRAMER; GLUCOSYLCERAMIDE; GLYCOPROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; K RAS PROTEIN; LIPID; MATRIX METALLOPROTEINASE; MEMBRANE LIPID; MEMBRANE PROTEIN; PHOSPHATIDYLETHANOLAMINE; RAB PROTEIN; SPHINGOMYELIN; SYNDECAN 1; TRANSMEMBRANE CONDUCTANCE REGULATOR; UVOMORULIN; PROTEIN SYNTHESIS INHIBITOR;

EID: 52549093192     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-8355-0     Document Type: Review
Times cited : (34)

References (200)
  • 1
    • 0034614647 scopus 로고    scopus 로고
    • The road taken: Past and future foundations of membrane traffic
    • Mellman, I. and Warren, G. (2000) The road taken: past and future foundations of membrane traffic. Cell 100, 99-112.
    • (2000) Cell , vol.100 , pp. 99-112
    • Mellman, I.1    Warren, G.2
  • 3
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • Scales, S. J., Pepperkok, R. and Kreis, T. E. (1997) Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell 90, 1137-1148.
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 4
    • 0034664730 scopus 로고    scopus 로고
    • The debate about transport in the Golgi - two sides of the same coin?
    • Pelham, H. R. and Rothman, J. E. (2000) The debate about transport in the Golgi - two sides of the same coin? Cell 102, 713-719.
    • (2000) Cell , vol.102 , pp. 713-719
    • Pelham, H.R.1    Rothman, J.E.2
  • 5
    • 0031975699 scopus 로고    scopus 로고
    • The Golgi apparatus: 100 years of progress and controversy
    • Farquhar, M. G. and Palade, G. E. (1998) The Golgi apparatus: 100 years of progress and controversy. Trends Cell Biol. 8, 2-10.
    • (1998) Trends Cell Biol , vol.8 , pp. 2-10
    • Farquhar, M.G.1    Palade, G.E.2
  • 6
    • 0035827374 scopus 로고    scopus 로고
    • What can yeast tell us about N-linked glycosylation in the Golgi apparatus?
    • Munro, S. (2001) What can yeast tell us about N-linked glycosylation in the Golgi apparatus? FEBS Lett. 498, 223-227.
    • (2001) FEBS Lett , vol.498 , pp. 223-227
    • Munro, S.1
  • 7
    • 0036704669 scopus 로고    scopus 로고
    • The Golgi apparatus: Balancing new with old
    • Storrie, B. and Nilsson, T. (2002) The Golgi apparatus: balancing new with old. Traffic 3, 521-529.
    • (2002) Traffic , vol.3 , pp. 521-529
    • Storrie, B.1    Nilsson, T.2
  • 8
    • 0026503134 scopus 로고
    • The Golgi complex: In vitro veritas?
    • 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
  • 11
    • 0031229420 scopus 로고    scopus 로고
    • Robert Feulgen Lecture 1997. Lipid microdomains and membrane trafficking in mammalian cells
    • Verkade, P. and Simons, K. (1997) Robert Feulgen Lecture 1997. Lipid microdomains and membrane trafficking in mammalian cells. Histochem. Cell Biol. 108, 211-220.
    • (1997) Histochem. Cell Biol , vol.108 , pp. 211-220
    • Verkade, P.1    Simons, K.2
  • 12
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D. A. and London, E. (1998) Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14, 111-136.
    • (1998) Annu. Rev. Cell Dev. Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 13
    • 34248195469 scopus 로고    scopus 로고
    • Lipid rafts and membrane traffic
    • Hanzal-Bayer, M. F. and Hancock, J. F. (2007) Lipid rafts and membrane traffic. FEBS Lett. 581, 2098-2104.
    • (2007) FEBS Lett , vol.581 , pp. 2098-2104
    • Hanzal-Bayer, M.F.1    Hancock, J.F.2
  • 14
  • 15
    • 0034682501 scopus 로고    scopus 로고
    • Dissecting the role of the Golgi complex and lipid rafts in biosynthetic transport of cholesterol to the cell surface
    • Heino, S., Lusa, S., Somerharju, P., Ehnholm, C., Olkkonen, V. M. and Ikonen, E. (2000) Dissecting the role of the Golgi complex and lipid rafts in biosynthetic transport of cholesterol to the cell surface. Proc. Natl. Acad. Sci. USA 97, 8375-8380.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8375-8380
    • Heino, S.1    Lusa, S.2    Somerharju, P.3    Ehnholm, C.4    Olkkonen, V.M.5    Ikonen, E.6
  • 16
    • 0037155829 scopus 로고    scopus 로고
    • Intestinal dipeptidyl peptidase IV is efficiently sorted to the apical membrane through the concerted action of N- and O-glycans as well as association with lipid microdomains
    • Alfalah, M., Jacob, R. and Naim, H. Y. (2002) Intestinal dipeptidyl peptidase IV is efficiently sorted to the apical membrane through the concerted action of N- and O-glycans as well as association with lipid microdomains. J. Biol. Chem. 277, 10683-10690.
    • (2002) J. Biol. Chem , vol.277 , pp. 10683-10690
    • Alfalah, M.1    Jacob, R.2    Naim, H.Y.3
  • 19
    • 33748325741 scopus 로고    scopus 로고
    • Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER
    • Browman, D. T., Resek, M. E., Zajchowski, L. D. and Robbins, S. M. (2006) Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER. J. Cell Sci. 119, 3149-3160.
    • (2006) J. Cell Sci , vol.119 , pp. 3149-3160
    • Browman, D.T.1    Resek, M.E.2    Zajchowski, L.D.3    Robbins, S.M.4
  • 21
    • 0033990428 scopus 로고    scopus 로고
    • Coat proteins regulating membrane traffic
    • Scales, S. J., Gomez, M. and Kreis, T. E. (2000) Coat proteins regulating membrane traffic. Int. Rev. Cytol. 195, 67-144.
    • (2000) Int. Rev. Cytol , vol.195 , pp. 67-144
    • Scales, S.J.1    Gomez, M.2    Kreis, T.E.3
  • 24
    • 20544451051 scopus 로고    scopus 로고
    • COPII and exit from the endoplasmic reticulum
    • Tang, B. L., Wang, Y., Ong, Y. S. and Hong, W. (2005) COPII and exit from the endoplasmic reticulum. Biochim. Biophys. Acta 1744, 293-303.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 293-303
    • Tang, B.L.1    Wang, Y.2    Ong, Y.S.3    Hong, W.4
  • 25
    • 0032516893 scopus 로고    scopus 로고
    • Regulation of membrane traffic in animal cells by COPI
    • Lowe, M. and Kreis, T. E. (1998) Regulation of membrane traffic in animal cells by COPI. Biochim. Biophys. Acta 1404, 53-66.
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 53-66
    • Lowe, M.1    Kreis, T.E.2
  • 26
    • 33748313351 scopus 로고    scopus 로고
    • Retrograde transport from endosomes to the trans-Golgi network
    • Bonifacino, J. S. and Rojas, R. (2006) Retrograde transport from endosomes to the trans-Golgi network. Nat. Rev. Mol. Cell Biol. 7, 568-579.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 568-579
    • Bonifacino, J.S.1    Rojas, R.2
  • 28
    • 33751168961 scopus 로고    scopus 로고
    • The formation of TGN-to-plasma-membrane transport carriers
    • Bard, F. and Malhotra, V. (2006) The formation of TGN-to-plasma-membrane transport carriers. Annu. Rev. Cell Dev. Biol. 22, 439-455.
    • (2006) Annu. Rev. Cell Dev. Biol , vol.22 , pp. 439-455
    • Bard, F.1    Malhotra, V.2
  • 29
    • 0038701886 scopus 로고    scopus 로고
    • The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes
    • Nickel, W. (2003) The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes. Eur. J. Biochem. 270, 2109-2119.
    • (2003) Eur. J. Biochem , vol.270 , pp. 2109-2119
    • Nickel, W.1
  • 30
    • 0037207470 scopus 로고    scopus 로고
    • Transport of exogenous growth factors and cytokines to the cytosol and to the nucleus
    • Olsnes, S., Klingenberg, O. and Wiedlocha, A. (2003) Transport of exogenous growth factors and cytokines to the cytosol and to the nucleus. Physiol. Rev. 83, 163-182.
    • (2003) Physiol. Rev , vol.83 , pp. 163-182
    • Olsnes, S.1    Klingenberg, O.2    Wiedlocha, A.3
  • 31
    • 33646184680 scopus 로고    scopus 로고
    • ARF proteins: Roles in membrane traffic and beyond
    • D'Souza-Schorey, C. and Chavrier, P. (2006) ARF proteins: roles in membrane traffic and beyond. Nat. Rev. Mol. Cell Biol. 7, 347-358.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 347-358
    • D'Souza-Schorey, C.1    Chavrier, P.2
  • 32
    • 0026654763 scopus 로고
    • Brefeldin A and the endocytic pathway. Possible implications for membrane traffic and sorting
    • Hunziker, W., Whitney, J. A. and Mellman, I. (1992) Brefeldin A and the endocytic pathway. Possible implications for membrane traffic and sorting. FEBS Lett. 307, 93-96.
    • (1992) FEBS Lett , vol.307 , pp. 93-96
    • Hunziker, W.1    Whitney, J.A.2    Mellman, I.3
  • 33
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R. D., Donaldson, J. G. and Lippincott-Schwartz, J. (1992) Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116, 1071-1080.
    • (1992) J. Cell Biol , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 34
    • 84954944159 scopus 로고
    • Brefeldin A, a specific inhibitor of intracellular translocation of vesicular stomatitis virus G Protein: Intracellular accumulation of high-mannose type G Protein and inhibition of its cell surface expression
    • Takatsuki, A. and Tamura, G. (1984) Brefeldin A, a specific inhibitor of intracellular translocation of vesicular stomatitis virus G Protein: Intracellular accumulation of high-mannose type G Protein and inhibition of its cell surface expression. Agric. Biol. Chem. 49, 899-902.
    • (1984) Agric. Biol. Chem , vol.49 , pp. 899-902
    • Takatsuki, A.1    Tamura, G.2
  • 35
    • 0023008846 scopus 로고
    • Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes
    • Misumi, Y., Misumi, Y., Miki, K., Takatsuki, A., Tamura, G. and Ikehara, Y. (1986) Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes. J. Biol. Chem. 261, 11398-11403.
    • (1986) J. Biol. Chem , vol.261 , pp. 11398-11403
    • Misumi, Y.1    Misumi, Y.2    Miki, K.3    Takatsuki, A.4    Tamura, G.5    Ikehara, Y.6
  • 36
    • 0026091737 scopus 로고
    • Selective inhibition of transcytosis by brefeldin A in MDCK cells
    • Hunziker, W., Whitney, J. A. and Mellman, I. (1991) Selective inhibition of transcytosis by brefeldin A in MDCK cells. Cell 67, 617-627.
    • (1991) Cell , vol.67 , pp. 617-627
    • Hunziker, W.1    Whitney, J.A.2    Mellman, I.3
  • 37
    • 0025919701 scopus 로고
    • PtK1 cells contain a nondiffusible, dominant factor that makes the Golgi apparatus resistant to brefeldin A
    • Ktistakis, N. T., Roth, M. G. and Bloom, G. S. (1991) PtK1 cells contain a nondiffusible, dominant factor that makes the Golgi apparatus resistant to brefeldin A. J. Cell Biol. 113, 1009-1023.
    • (1991) J. Cell Biol , vol.113 , pp. 1009-1023
    • Ktistakis, N.T.1    Roth, M.G.2    Bloom, G.S.3
  • 38
    • 0026353711 scopus 로고
    • Ricin transport in brefeldin A-treated cells: Correlation between Golgi structure and toxic effect
    • Sandvig, K., Prydz, K., Hansen, S. H. and van Deurs, B. (1991) Ricin transport in brefeldin A-treated cells: correlation between Golgi structure and toxic effect. J. Cell Biol. 115, 971-981.
    • (1991) J. Cell Biol , vol.115 , pp. 971-981
    • Sandvig, K.1    Prydz, K.2    Hansen, S.H.3    van Deurs, B.4
  • 39
    • 0025142335 scopus 로고
    • Cholesterol and vesicular stomatitis virus G protein take separate routes from the endoplasmic reticulum to the plasma membrane
    • Urbani, L. and Simoni, R. D. (1990) Cholesterol and vesicular stomatitis virus G protein take separate routes from the endoplasmic reticulum to the plasma membrane. J. Biol. Chem. 265, 1919-1923.
    • (1990) J. Biol. Chem , vol.265 , pp. 1919-1923
    • Urbani, L.1    Simoni, R.D.2
  • 40
    • 0021148465 scopus 로고
    • Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface
    • Saraste, J. and Kuismanen, E. (1984) Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface. Cell 38, 535-549.
    • (1984) Cell , vol.38 , pp. 535-549
    • Saraste, J.1    Kuismanen, E.2
  • 41
    • 0343986043 scopus 로고
    • Passage of an integral membrane protein, the vesicular stomatitis virus glycoprotein, through the Golgi apparatus en route to the plasmamembrane
    • Bergmann, J. E., Tokuyasu, K. T. and Singer, S. J. (1981) Passage of an integral membrane protein, the vesicular stomatitis virus glycoprotein, through the Golgi apparatus en route to the plasmamembrane. Proc. Natl. Acad. Sci. USA 78, 1746-1750.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 1746-1750
    • Bergmann, J.E.1    Tokuyasu, K.T.2    Singer, S.J.3
  • 42
    • 0022390560 scopus 로고
    • Transport of cholesterol from the endoplasmic reticulum to the plasma membrane
    • Kaplan, M. R. and Simoni, R. D. (1985) Transport of cholesterol from the endoplasmic reticulum to the plasma membrane. J. Cell Biol. 101, 446-453.
    • (1985) J. Cell Biol , vol.101 , pp. 446-453
    • Kaplan, M.R.1    Simoni, R.D.2
  • 44
    • 0037184948 scopus 로고    scopus 로고
    • The protein-tyrosine phosphatase CD45 reaches the cell surface via Golgi-dependent and -independent pathways
    • Baldwin, T. A. and Ostergaard, H. L. (2002) The protein-tyrosine phosphatase CD45 reaches the cell surface via Golgi-dependent and -independent pathways. J. Biol. Chem. 277, 50333-50340.
    • (2002) J. Biol. Chem , vol.277 , pp. 50333-50340
    • Baldwin, T.A.1    Ostergaard, H.L.2
  • 45
    • 0032919043 scopus 로고    scopus 로고
    • Chicken erythroid AE1 anion exchangers associate with the cytoskeleton during recycling to the Golgi
    • Ghosh, S., Cox, K. H. and Cox, J. V. (1999) Chicken erythroid AE1 anion exchangers associate with the cytoskeleton during recycling to the Golgi. Mol. Biol. Cell 10, 455-469.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 455-469
    • Ghosh, S.1    Cox, K.H.2    Cox, J.V.3
  • 46
  • 47
    • 0034328820 scopus 로고    scopus 로고
    • Traffic pattern of cystic fibrosis transmembrane regulator through the early exocytic pathway
    • Bannykh, S. I., Bannykh, G. I., Fish, K. N., Moyer, B. D., Riordan, J. R. and Balch, W. E. (2000) Traffic pattern of cystic fibrosis transmembrane regulator through the early exocytic pathway. Traffic 1, 852-870.
    • (2000) Traffic , vol.1 , pp. 852-870
    • Bannykh, S.I.1    Bannykh, G.I.2    Fish, K.N.3    Moyer, B.D.4    Riordan, J.R.5    Balch, W.E.6
  • 48
    • 0037192856 scopus 로고    scopus 로고
    • Non-conventional trafficking of the cystic fibrosis transmembrane conductance regulator through the early secretory pathway
    • Yoo, J. S., Moyer, B. D., Bannykh, S., Yoo, H. M., Riordan, J. R. and Balch, W. E. (2002) Non-conventional trafficking of the cystic fibrosis transmembrane conductance regulator through the early secretory pathway. J. Biol. Chem. 277, 11401-11409.
    • (2002) J. Biol. Chem , vol.277 , pp. 11401-11409
    • Yoo, J.S.1    Moyer, B.D.2    Bannykh, S.3    Yoo, H.M.4    Riordan, J.R.5    Balch, W.E.6
  • 50
    • 0019273454 scopus 로고
    • Intracellular localization of fibronectin using immunoperoxidase cytochemistry in light and electron microscopy
    • Hedman, K. (1980) Intracellular localization of fibronectin using immunoperoxidase cytochemistry in light and electron microscopy. J. Histochem. Cytochem. 28, 1233-1241.
    • (1980) J. Histochem. Cytochem , vol.28 , pp. 1233-1241
    • Hedman, K.1
  • 51
    • 0021800558 scopus 로고
    • Vesicles and cisternae in the trans Golgi apparatus of human fibroblasts are acidic compartments
    • Anderson, R. G. and Pathak, R. K. (1985) Vesicles and cisternae in the trans Golgi apparatus of human fibroblasts are acidic compartments. Cell 40, 635-643.
    • (1985) Cell , vol.40 , pp. 635-643
    • Anderson, R.G.1    Pathak, R.K.2
  • 52
    • 0020657386 scopus 로고
    • Abnormal glycosylation of human fibronectin secreted in the presence of monensin
    • Ledger, P. W., Nishimoto, S. K., Hayashi, S. and Tanzer, M. L. (1983) Abnormal glycosylation of human fibronectin secreted in the presence of monensin. J. Biol. Chem. 258, 547-554.
    • (1983) J. Biol. Chem , vol.258 , pp. 547-554
    • Ledger, P.W.1    Nishimoto, S.K.2    Hayashi, S.3    Tanzer, M.L.4
  • 53
    • 0030846017 scopus 로고    scopus 로고
    • Rotavirus is released from the apical surface of cultured human intestinal cells through non-conventional vesicular transport that bypasses the Golgi apparatus
    • Jourdan, N., Maurice, M., Delautier, D., Quero, A. M., Servin, A. L. and Trugnan, G. (1997) Rotavirus is released from the apical surface of cultured human intestinal cells through non-conventional vesicular transport that bypasses the Golgi apparatus. J. Virol. 71, 8268-8278.
    • (1997) J. Virol , vol.71 , pp. 8268-8278
    • Jourdan, N.1    Maurice, M.2    Delautier, D.3    Quero, A.M.4    Servin, A.L.5    Trugnan, G.6
  • 54
    • 33645755879 scopus 로고    scopus 로고
    • Dissecting rotavirus particle-raft interaction with small interfering RNAs: Insights into rotavirus transit through the secretory pathway
    • Cuadras, M. A., Bordier, B. B., Zambrano, J. L., Ludert, J. E. and Greenberg, H. B. (2006) Dissecting rotavirus particle-raft interaction with small interfering RNAs: insights into rotavirus transit through the secretory pathway. J. Virol. 80, 3935-3946.
    • (2006) J. Virol , vol.80 , pp. 3935-3946
    • Cuadras, M.A.1    Bordier, B.B.2    Zambrano, J.L.3    Ludert, J.E.4    Greenberg, H.B.5
  • 55
    • 4444258805 scopus 로고    scopus 로고
    • Different ways to reach the top of a cell. Analysis of rotavirus assembly and targeting in human intestinal cells reveals an original raft-dependent, Golgi-independent apical targeting pathway
    • Delmas, O., Gardet, A., Chwetzoff, S., Breton, M., Cohen, J., Colard, O., Sapin, C. and Trugnan, G. (2004) Different ways to reach the top of a cell. Analysis of rotavirus assembly and targeting in human intestinal cells reveals an original raft-dependent, Golgi-independent apical targeting pathway. Virology 327, 157-161.
    • (2004) Virology , vol.327 , pp. 157-161
    • Delmas, O.1    Gardet, A.2    Chwetzoff, S.3    Breton, M.4    Cohen, J.5    Colard, O.6    Sapin, C.7    Trugnan, G.8
  • 56
    • 33748114368 scopus 로고    scopus 로고
    • Rotavirus assembly: An alternative model that utilizes an atypical trafficking pathway
    • Chwetzoff, S. and Trugnan, G. (2006) Rotavirus assembly: an alternative model that utilizes an atypical trafficking pathway. Curr. Top. Microbiol. Immunol. 309, 245-261.
    • (2006) Curr. Top. Microbiol. Immunol , vol.309 , pp. 245-261
    • Chwetzoff, S.1    Trugnan, G.2
  • 57
    • 39449116332 scopus 로고    scopus 로고
    • Distinct functions for Arf nucleotide exchange factors at the Golgi complex: GBF1 and BIGs are required for assembly and maintenance of the Golgi stack and TGN, respectively
    • Manolea, F., Claude, A., Chun, J., Rosas, J. and Melancon, P. (2007) Distinct functions for Arf nucleotide exchange factors at the Golgi complex: GBF1 and BIGs are required for assembly and maintenance of the Golgi stack and TGN, respectively. Mol. Biol. Cell 19, 523-535.
    • (2007) Mol. Biol. Cell , vol.19 , pp. 523-535
    • Manolea, F.1    Claude, A.2    Chun, J.3    Rosas, J.4    Melancon, P.5
  • 58
    • 37249041571 scopus 로고    scopus 로고
    • Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking
    • Szul, T., Grabski, R., Lyons, S., Morohashi, Y., Shestopal, S., Lowe, M. and Sztul, E. (2007) Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking. J. Cell Sci. 120, 3929-3940.
    • (2007) J. Cell Sci , vol.120 , pp. 3929-3940
    • Szul, T.1    Grabski, R.2    Lyons, S.3    Morohashi, Y.4    Shestopal, S.5    Lowe, M.6    Sztul, E.7
  • 59
    • 0026934508 scopus 로고
    • Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex
    • Saraste, J. and Kuismanen, E. (1992) Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex. Semin. Cell Biol. 3, 343-355.
    • (1992) Semin. Cell Biol , vol.3 , pp. 343-355
    • Saraste, J.1    Kuismanen, E.2
  • 60
    • 33745485316 scopus 로고    scopus 로고
    • The ERGolgi intermediate compartment (ERGIC): In search of its identity and function
    • Appenzeller-Herzog, C. and Hauri, H. P. (2006) The ERGolgi intermediate compartment (ERGIC): in search of its identity and function. J. Cell Sci. 119, 2173-2183.
    • (2006) J. Cell Sci , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 61
    • 0027499531 scopus 로고
    • b-COP localizes mainly to the cis-Golgi side in exocrine pancreas
    • Oprins, A., Duden, R., Kreis, T. E., Geuze, H. J. and Slot, J. W. (1993) b-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.E.3    Geuze, H.J.4    Slot, J.W.5
  • 62
    • 0033538549 scopus 로고    scopus 로고
    • Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles
    • Martinez-Menarguez, J. A., Geuze, H. J., Slot, J. W. and Klumperman, J. (1999)Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles. Cell 98, 81-90.
    • (1999) Cell , vol.98 , pp. 81-90
    • Martinez-Menarguez, J.A.1    Geuze, H.J.2    Slot, J.W.3    Klumperman, J.4
  • 64
    • 20544471158 scopus 로고    scopus 로고
    • ER-to-Golgi transport: Form and formation of vesicular and tubular carriers
    • Watson, P. and Stephens, D. J. (2005) ER-to-Golgi transport: form and formation of vesicular and tubular carriers. Biochim. Biophys. Acta 1744, 304-315.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 304-315
    • Watson, P.1    Stephens, D.J.2
  • 65
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz, J., Donaldson, J. G., Schweizer, A., Berger, E. G., Hauri, H. P., Yuan, L. C. and Klausner, R. D. (1990) Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 60, 821-836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 66
    • 0026052099 scopus 로고
    • Distribution of the intermediate elements operating in ER to Golgi transport
    • Saraste, J. and Svensson, K. (1991) Distribution of the intermediate elements operating in ER to Golgi transport. J. Cell Sci. 100, 415-430.
    • (1991) J. Cell Sci , vol.100 , pp. 415-430
    • Saraste, J.1    Svensson, K.2
  • 67
    • 0028211035 scopus 로고
    • Brefeldin A induced dose-dependent changes to Golgi structure and function in the rat exocrine pancreas
    • Kömhoff, M., Hollinshead, M., Tooze, J. and Kern, H. F. (1994) Brefeldin A induced dose-dependent changes to Golgi structure and function in the rat exocrine pancreas. Eur. J. Cell Biol. 63, 192-207.
    • (1994) Eur. J. Cell Biol , vol.63 , pp. 192-207
    • Kömhoff, M.1    Hollinshead, M.2    Tooze, J.3    Kern, H.F.4
  • 70
    • 0031772176 scopus 로고    scopus 로고
    • Retrograde transport from the pre-Golgi intermediate compartment and the Golgi complex is affected by the vacuolar H+-ATPase inhibitor bafilomycin A1
    • Palokangas, H., Ying, M., Väänänen, K. and Saraste, J. (1998) Retrograde transport from the pre-Golgi intermediate compartment and the Golgi complex is affected by the vacuolar H+-ATPase inhibitor bafilomycin A1. Mol. Biol. Cell 9, 3561-3578.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3561-3578
    • Palokangas, H.1    Ying, M.2    Väänänen, K.3    Saraste, J.4
  • 71
    • 33745421381 scopus 로고    scopus 로고
    • Rab1 defines a novel pathway connecting the pre-Golgi intermediate compartment with the cell periphery
    • Sannerud, R., Marie, M., Nizak, C., Dale, H. A., Pernet-Gallay, K., Perez, F., Goud, B. and Saraste, J. (2006) Rab1 defines a novel pathway connecting the pre-Golgi intermediate compartment with the cell periphery. Mol. Biol. Cell 17, 1514-1526.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1514-1526
    • Sannerud, R.1    Marie, M.2    Nizak, C.3    Dale, H.A.4    Pernet-Gallay, K.5    Perez, F.6    Goud, B.7    Saraste, J.8
  • 73
    • 0037087610 scopus 로고    scopus 로고
    • Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells
    • Stephens, D. J. and Pepperkok, R. (2002) Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells. J. Cell Sci. 115, 1149-1160.
    • (2002) J. Cell Sci , vol.115 , pp. 1149-1160
    • Stephens, D.J.1    Pepperkok, R.2
  • 74
    • 0028862992 scopus 로고
    • Two redundant systems maintain levels of resident proteins within the yeast endoplasmic reticulum
    • Beh, C. T. and Rose, M. D. (1995) Two redundant systems maintain levels of resident proteins within the yeast endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 92, 9820-9823.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9820-9823
    • Beh, C.T.1    Rose, M.D.2
  • 75
    • 0031027758 scopus 로고    scopus 로고
    • COPI-independent anterograde transport: Cargo-selective ER to Golgi protein transport in yeast COPI mutants
    • Gaynor, E. C. and Emr, S. D. (1997) COPI-independent anterograde transport: cargo-selective ER to Golgi protein transport in yeast COPI mutants. J. Cell Biol. 136, 789-802.
    • (1997) J. Cell Biol , vol.136 , pp. 789-802
    • Gaynor, E.C.1    Emr, S.D.2
  • 76
    • 0025940101 scopus 로고
    • Brefeldin A's 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 A's 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
  • 77
    • 0025943380 scopus 로고
    • Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes
    • Wood, S. A., Park, J. E. and Brown, W. J. (1991) Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes. Cell 67, 591-600.
    • (1991) Cell , vol.67 , pp. 591-600
    • Wood, S.A.1    Park, J.E.2    Brown, W.J.3
  • 78
    • 0026713586 scopus 로고
    • The morphology but not the function of endosomes and lysosomes is altered by brefeldin A
    • Wood, S. A. and Brown, W. J. (1992) The morphology but not the function of endosomes and lysosomes is altered by brefeldin A. J. Cell Biol. 119, 273-285.
    • (1992) J. Cell Biol , vol.119 , pp. 273-285
    • Wood, S.A.1    Brown, W.J.2
  • 79
    • 0026776711 scopus 로고
    • Post-Golgi membrane traffic: Brefeldin A inhibits export from distal Golgi compartments to the cell surface but not recycling
    • Miller, S. G., Carnell, L. and Moore, H. H. (1992) Post-Golgi membrane traffic: brefeldin A inhibits export from distal Golgi compartments to the cell surface but not recycling. J. Cell Biol. 118, 267-283.
    • (1992) J. Cell Biol , vol.118 , pp. 267-283
    • Miller, S.G.1    Carnell, L.2    Moore, H.H.3
  • 80
    • 0031052040 scopus 로고    scopus 로고
    • TGN38 and its orthologues: Roles in post-TGN vesicle formation and maintenance of TGN morphology
    • Banting, G. and Ponnambalam, S. (1997) TGN38 and its orthologues: roles in post-TGN vesicle formation and maintenance of TGN morphology. Biochim. Biophys. Acta 1355, 209-217.
    • (1997) Biochim. Biophys. Acta , vol.1355 , pp. 209-217
    • Banting, G.1    Ponnambalam, S.2
  • 84
    • 33749078313 scopus 로고    scopus 로고
    • A new paradigm for membrane-organizing and -shaping scaffolds
    • Bauer, M. and Pelkmans, L. (2006) A new paradigm for membrane-organizing and -shaping scaffolds. FEBS Lett. 580, 5559-5564.
    • (2006) FEBS Lett , vol.580 , pp. 5559-5564
    • Bauer, M.1    Pelkmans, L.2
  • 85
    • 1442284337 scopus 로고    scopus 로고
    • Caveolins and membrane cholesterol
    • Ikonen, E., Heino, S. and Lusa, S. (2004) Caveolins and membrane cholesterol. Biochem. Soc. Trans. 32, 121-123.
    • (2004) Biochem. Soc. Trans , vol.32 , pp. 121-123
    • Ikonen, E.1    Heino, S.2    Lusa, S.3
  • 87
    • 0034062812 scopus 로고    scopus 로고
    • H-ras but not K-ras traffics to the plasma membrane through the exocytic pathway
    • Apolloni, A., Prior, I. A., Lindsay, M., Parton, R. G. and Hancock, J. F. (2000) H-ras but not K-ras traffics to the plasma membrane through the exocytic pathway. Mol. Cell Biol. 20, 2475-2487.
    • (2000) Mol. Cell Biol , vol.20 , pp. 2475-2487
    • Apolloni, A.1    Prior, I.A.2    Lindsay, M.3    Parton, R.G.4    Hancock, J.F.5
  • 88
    • 33845794047 scopus 로고    scopus 로고
    • Palmitoylation: Policing protein stability and traffic
    • Linder, M. E. and Deschenes, R. J. (2007) Palmitoylation: policing protein stability and traffic. Nat. Rev. Mol. Cell Biol. 8, 74-84.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 74-84
    • Linder, M.E.1    Deschenes, R.J.2
  • 89
    • 34548490482 scopus 로고    scopus 로고
    • H-Ras does not need COPI- or COPII-dependent vesicular transport to reach the plasma membrane
    • Zheng, H., McKay, J. and Buss, J. E. (2007) H-Ras does not need COPI- or COPII-dependent vesicular transport to reach the plasma membrane. J. Biol. Chem. 282, 25760-25768.
    • (2007) J. Biol. Chem , vol.282 , pp. 25760-25768
    • Zheng, H.1    McKay, J.2    Buss, J.E.3
  • 90
    • 0035188530 scopus 로고    scopus 로고
    • Multiple pathways in trafficking and assembly of connexin 26, 32 and 43 into gap junction intercellular communication channels
    • Martin, P. E., Blundell, G., Ahmad, S., Errington, R. J. and Evans, W. H. (2001) Multiple pathways in trafficking and assembly of connexin 26, 32 and 43 into gap junction intercellular communication channels. J. Cell Sci. 114, 3845-3855.
    • (2001) J. Cell Sci , vol.114 , pp. 3845-3855
    • Martin, P.E.1    Blundell, G.2    Ahmad, S.3    Errington, R.J.4    Evans, W.H.5
  • 91
    • 0027364529 scopus 로고
    • Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin-43, occurs after exit from the ER
    • Musil, L. S. and Goodenough, D. A. (1993) Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin-43, occurs after exit from the ER. Cell 74, 1065-1077.
    • (1993) Cell , vol.74 , pp. 1065-1077
    • Musil, L.S.1    Goodenough, D.A.2
  • 92
    • 33644826498 scopus 로고    scopus 로고
    • Pathways and control of connexin oligomerization
    • Koval, M. (2006) Pathways and control of connexin oligomerization. Trends Cell Biol. 16, 159-166.
    • (2006) Trends Cell Biol , vol.16 , pp. 159-166
    • Koval, M.1
  • 93
    • 0034671351 scopus 로고    scopus 로고
    • Functional morphology of the secretory pathway organelles in yeast
    • Vorisek, J. (2000). Functional morphology of the secretory pathway organelles in yeast. Microsc. Res. Tech. 51, 530-546.
    • (2000) Microsc. Res. Tech , vol.51 , pp. 530-546
    • Vorisek, J.1
  • 95
    • 0020399748 scopus 로고
    • Effect of Brefeldin A on biosynthesis of cellular components in Candida albicans
    • Hayashi, T., Takatsuki, A. and Tamura, G. (1982) Effect of Brefeldin A on biosynthesis of cellular components in Candida albicans. Agric. Biol. Chem. 46, 2241-2248.
    • (1982) Agric. Biol. Chem , vol.46 , pp. 2241-2248
    • Hayashi, T.1    Takatsuki, A.2    Tamura, G.3
  • 96
    • 0027992519 scopus 로고
    • Brefeldin A sensitivity and resistance in Schizosaccharomyces pombe. Isolation of multiple genes conferring resistance
    • Turi, T. G., Webster, P. and Rose, J. K. (1994) Brefeldin A sensitivity and resistance in Schizosaccharomyces pombe. Isolation of multiple genes conferring resistance. J. Biol. Chem. 269, 24229-24236.
    • (1994) J. Biol. Chem , vol.269 , pp. 24229-24236
    • Turi, T.G.1    Webster, P.2    Rose, J.K.3
  • 97
    • 0032959440 scopus 로고    scopus 로고
    • Overview of N- and O-linked oligosaccharide structures found in various yeast species
    • Gemmill, T. R. and Trimble, R. B. (1999). Overview of N- and O-linked oligosaccharide structures found in various yeast species. Biochim. Biophys. Acta 1426, 227-237.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 227-237
    • Gemmill, T.R.1    Trimble, R.B.2
  • 98
    • 0030609041 scopus 로고    scopus 로고
    • Vesicular transport: How many Ypt/Rab-GTPases make a eukaryotic cell?
    • Lazar, T., Gotte, M. and Gallwitz, D. (1997) Vesicular transport: how many Ypt/Rab-GTPases make a eukaryotic cell? Trends Biochem. Sci. 22, 468-472.
    • (1997) Trends Biochem. Sci , vol.22 , pp. 468-472
    • Lazar, T.1    Gotte, M.2    Gallwitz, D.3
  • 99
    • 0035909125 scopus 로고    scopus 로고
    • Ypt/Rab GTPases: Regulators of protein trafficking
    • Segev, N. (2001) Ypt/Rab GTPases: regulators of protein trafficking. Sci STKE, RE11-25.
    • (2001) Sci STKE
    • Segev, N.1
  • 100
    • 33747066132 scopus 로고    scopus 로고
    • Rabs and their effectors: Achieving specificity in membrane traffic
    • Grosshans, B. L., Ortiz, D. and Novick, P. (2006) Rabs and their effectors: achieving specificity in membrane traffic. Proc. Natl. Acad. Sci. USA 103, 11821-11827.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11821-11827
    • Grosshans, B.L.1    Ortiz, D.2    Novick, P.3
  • 101
    • 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
  • 102
    • 0019424489 scopus 로고
    • Order of events in the yeast secretory pathway
    • Novick, P., Ferro, S. and Schekman, R. (1981) Order of events in the yeast secretory pathway. Cell 25, 461-469.
    • (1981) Cell , vol.25 , pp. 461-469
    • Novick, P.1    Ferro, S.2    Schekman, R.3
  • 104
    • 0028787438 scopus 로고
    • Parallel secretory pathways to the cell surface in yeast
    • Harsay, E. and Bretscher, A. (1995) Parallel secretory pathways to the cell surface in yeast. J. Cell Biol. 131, 297-310.
    • (1995) J. Cell Biol , vol.131 , pp. 297-310
    • Harsay, E.1    Bretscher, A.2
  • 105
    • 0037148531 scopus 로고    scopus 로고
    • A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway
    • Harsay, E. and Schekman, R. (2002) A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway. J. Cell Biol. 156, 271-285.
    • (2002) J. Cell Biol , vol.156 , pp. 271-285
    • Harsay, E.1    Schekman, R.2
  • 106
    • 0023658351 scopus 로고
    • The rate of bulk flow from the endoplasmic reticulum to the cell surface
    • Wieland, F. T., Gleason, M. L., Serafini, T. A. and Rothman, J. E. (1987) The rate of bulk flow from the endoplasmic reticulum to the cell surface. Cell 50, 289-300.
    • (1987) Cell , vol.50 , pp. 289-300
    • Wieland, F.T.1    Gleason, M.L.2    Serafini, T.A.3    Rothman, J.E.4
  • 108
    • 0025224796 scopus 로고
    • Reconstitution of steps in the constitutive secretory pathway in permeabilized cells. Secretion of glycosylated tripeptide and truncated sphingomyelin
    • Helms, J. B., Karrenbauer, A., Wirtz, K. W., Rothman, J. E. and Wieland, F. T. (1990) Reconstitution of steps in the constitutive secretory pathway in permeabilized cells. Secretion of glycosylated tripeptide and truncated sphingomyelin. J. Biol. Chem. 265, 20027-20032.
    • (1990) J. Biol. Chem , vol.265 , pp. 20027-20032
    • Helms, J.B.1    Karrenbauer, A.2    Wirtz, K.W.3    Rothman, J.E.4    Wieland, F.T.5
  • 109
    • 0028067206 scopus 로고
    • Complete Golgi passage of glycotripeptides generated in the endoplasmic reticulum of mammalian cells
    • van Leyen, K. and Wieland, F. (1994) Complete Golgi passage of glycotripeptides generated in the endoplasmic reticulum of mammalian cells. FEBS Lett. 352, 211-215.
    • (1994) FEBS Lett , vol.352 , pp. 211-215
    • van Leyen, K.1    Wieland, F.2
  • 110
    • 0022343674 scopus 로고
    • Demonstration of an extensive transtubular network continuous with the Golgi apparatus stack that may function in glycosylation
    • Roth, J., Taatjes, D. J., Lucocq, J. M., Weinstein, J. and Paulson, J. C. (1985) Demonstration of an extensive transtubular network continuous with the Golgi apparatus stack that may function in glycosylation. Cell 43, 287-295.
    • (1985) Cell , vol.43 , pp. 287-295
    • Roth, J.1    Taatjes, D.J.2    Lucocq, J.M.3    Weinstein, J.4    Paulson, J.C.5
  • 111
    • 0033611145 scopus 로고    scopus 로고
    • ER-Golgi intermediates acquire Golgi enzymes by brefeldin A-sensitive retrograde transport in vitro
    • Lin, C. C., Love, H. D., Gushue, J. N., Bergeron, J. J. and Ostermann, J. (1999) ER-Golgi intermediates acquire Golgi enzymes by brefeldin A-sensitive retrograde transport in vitro. J. Cell Biol. 147, 1457-1472.
    • (1999) J. Cell Biol , vol.147 , pp. 1457-1472
    • Lin, C.C.1    Love, H.D.2    Gushue, J.N.3    Bergeron, J.J.4    Ostermann, J.5
  • 113
    • 0036239516 scopus 로고    scopus 로고
    • Ectopic localizations of Golgi glycosyltransferases
    • Berger, E. G. (2002) Ectopic localizations of Golgi glycosyltransferases. Glycobiology 12, R29-36.
    • (2002) Glycobiology , vol.12
    • Berger, E.G.1
  • 114
    • 33845961707 scopus 로고    scopus 로고
    • Modulation of GalT1 and SialT1 sub-Golgi localization by SialT2 expression reveals an organellar level of glycolipid synthesis control
    • Uliana, A. S., Crespo, P. M., Martina, J. A., Daniotti, J. L. and Maccioni, H. J. (2006) Modulation of GalT1 and SialT1 sub-Golgi localization by SialT2 expression reveals an organellar level of glycolipid synthesis control. J. Biol. Chem. 281, 32852-32860.
    • (2006) J. Biol. Chem , vol.281 , pp. 32852-32860
    • Uliana, A.S.1    Crespo, P.M.2    Martina, J.A.3    Daniotti, J.L.4    Maccioni, H.J.5
  • 115
    • 0036441135 scopus 로고    scopus 로고
    • Membrane traffic exploited by protein toxins
    • Sandvig, K. and van Deurs, B. (2002) Membrane traffic exploited by protein toxins. Annu. Rev. Cell Dev. Biol. 18, 1-24.
    • (2002) Annu. Rev. Cell Dev. Biol , vol.18 , pp. 1-24
    • Sandvig, K.1    van Deurs, B.2
  • 116
    • 0030929658 scopus 로고    scopus 로고
    • Retrograde transport of mutant ricin to the endoplasmic reticulum with subsequent translocation to cytosol
    • Rapak, A., Falnes, P. O. and Olsnes, S. (1997) Retrograde transport of mutant ricin to the endoplasmic reticulum with subsequent translocation to cytosol. Proc. Natl. Acad. Sci. USA 94, 3783-3788.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3783-3788
    • Rapak, A.1    Falnes, P.O.2    Olsnes, S.3
  • 117
    • 0031890793 scopus 로고    scopus 로고
    • Surfing on a retrograde wave: How does Shiga toxin reach the endoplasmic reticulum?
    • Johannes, L. and Goud, B. (1998) Surfing on a retrograde wave: how does Shiga toxin reach the endoplasmic reticulum? Trends Cell Biol. 8, 158-162.
    • (1998) Trends Cell Biol , vol.8 , pp. 158-162
    • Johannes, L.1    Goud, B.2
  • 118
    • 0037012521 scopus 로고    scopus 로고
    • Retrograde transport of protein toxins under conditions of COPI dysfunction
    • Chen, A., Hu, T., Mikoryak, C. and Draper, R. K. (2002) Retrograde transport of protein toxins under conditions of COPI dysfunction. Biochim. Biophys. Acta 1589, 124-139.
    • (2002) Biochim. Biophys. Acta , vol.1589 , pp. 124-139
    • Chen, A.1    Hu, T.2    Mikoryak, C.3    Draper, R.K.4
  • 119
    • 0041326901 scopus 로고    scopus 로고
    • Evidence that the transport of ricin to the cytoplasm is independent of both Rab6A and COPI
    • Chen, A., AbuJarour, R. J. and Draper, R. K. (2003) Evidence that the transport of ricin to the cytoplasm is independent of both Rab6A and COPI. J. Cell Sci. 116, 3503-3510.
    • (2003) J. Cell Sci , vol.116 , pp. 3503-3510
    • Chen, A.1    AbuJarour, R.J.2    Draper, R.K.3
  • 120
    • 0043282584 scopus 로고    scopus 로고
    • Induction of direct endosome to endoplasmic reticulum transport in Chinese hamster ovary (CHO) cells (LdlF) with a temperature-sensitive defect in e-coatomer protein (e-COP)
    • Llorente, A., Lauvrak, S. U., van Deurs, B. and Sandvig, K. (2003) Induction of direct endosome to endoplasmic reticulum transport in Chinese hamster ovary (CHO) cells (LdlF) with a temperature-sensitive defect in e-coatomer protein (e-COP). J. Biol. Chem. 278, 35850-35855.
    • (2003) J. Biol. Chem , vol.278 , pp. 35850-35855
    • Llorente, A.1    Lauvrak, S.U.2    van Deurs, B.3    Sandvig, K.4
  • 121
    • 0041328515 scopus 로고    scopus 로고
    • Brefeldin A-regulated retrograde transport into the endoplasmic reticulum of internalized wheat germ agglutinin
    • Vetterlein, M., Niapir, M., Ellinger, A., Neumüller, J. and Pavelka, M. (2003) Brefeldin A-regulated retrograde transport into the endoplasmic reticulum of internalized wheat germ agglutinin. Histochem. Cell Biol. 120, 121-128.
    • (2003) Histochem. Cell Biol , vol.120 , pp. 121-128
    • Vetterlein, M.1    Niapir, M.2    Ellinger, A.3    Neumüller, J.4    Pavelka, M.5
  • 122
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans, L., Kartenbeck, J. and Helenius, A. (2001) Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat. Cell Biol. 3, 473-483.
    • (2001) Nat. Cell Biol , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 123
    • 0031847686 scopus 로고    scopus 로고
    • Localization of autocrine motility factor receptor to caveolae and clathrinin-dependent internalization of its ligand to smooth endoplasmic reticulum
    • Benlimame, N., Le, P. U. and Nabi, I. R. (1998) Localization of autocrine motility factor receptor to caveolae and clathrinin-dependent internalization of its ligand to smooth endoplasmic reticulum. Mol. Biol. Cell 9, 1773-1786.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1773-1786
    • Benlimame, N.1    Le, P.U.2    Nabi, I.R.3
  • 124
    • 0037444495 scopus 로고    scopus 로고
    • Distinct caveolae-mediated endocytic path-ways target the Golgi apparatus and the endoplasmic reticulum
    • Le, P. U. and Nabi, I. R. (2003) Distinct caveolae-mediated endocytic path-ways target the Golgi apparatus and the endoplasmic reticulum. J. Cell Sci. 116, 1059-1071.
    • (2003) J. Cell Sci , vol.116 , pp. 1059-1071
    • Le, P.U.1    Nabi, I.R.2
  • 125
    • 0014118370 scopus 로고
    • Intracellular transport of secretory proteins in the pancreatic exocrine cell. I. Role of the peripheral elements of the Golgi complex
    • Jamieson, J. D. and Palade, G. E. (1967) Intracellular transport of secretory proteins in the pancreatic exocrine cell. I. Role of the peripheral elements of the Golgi complex. J. Cell Biol. 34, 577-596.
    • (1967) J. Cell Biol , vol.34 , pp. 577-596
    • Jamieson, J.D.1    Palade, G.E.2
  • 126
    • 0017570023 scopus 로고
    • Dynamics of the Golgi apparatus: Membrane differentiation and membrane flow
    • Morre, D. J. and Ovtracht, L. (1977) Dynamics of the Golgi apparatus: membrane differentiation and membrane flow. Int. Rev. Cytol. Suppl., 61-188.
    • (1977) Int. Rev. Cytol. Suppl , pp. 61-188
    • Morre, D.J.1    Ovtracht, L.2
  • 127
    • 0017174781 scopus 로고
    • The endoplasmic reticulum: A cytochemist's view (a review)
    • Novikoff, A. B. (1976) The endoplasmic reticulum: a cytochemist's view (a review). Proc. Natl. Acad. Sci. USA 73, 2781-2787.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2781-2787
    • Novikoff, A.B.1
  • 128
    • 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
  • 129
    • 0020804564 scopus 로고
    • Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface, but does not prevent terminal glycosylation
    • Matlin, K. 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.1    Simons, K.2
  • 130
    • 0022187987 scopus 로고
    • Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasmamembrane
    • Griffiths, G., Pfeiffer, S., Simons, K. and Matlin, K. (1985) Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasmamembrane. J. Cell Biol. 101, 949-964.
    • (1985) J. Cell Biol , vol.101 , pp. 949-964
    • Griffiths, G.1    Pfeiffer, S.2    Simons, K.3    Matlin, K.4
  • 131
    • 0024821099 scopus 로고
    • Low temperature-induced transport blocks as tools to manipulate membrane traffic
    • Kuismanen, E. and Saraste, J. (1989) Low temperature-induced transport blocks as tools to manipulate membrane traffic. Methods Cell Biol. 32, 257-274.
    • (1989) Methods Cell Biol , vol.32 , pp. 257-274
    • Kuismanen, E.1    Saraste, J.2
  • 132
    • 0018409518 scopus 로고
    • Three-dimensional architecture of the Golgi apparatus in Sertoli cells of the rat
    • Rambourg, A., Clermont, Y. and Hermo, L. (1979) Three-dimensional architecture of the Golgi apparatus in Sertoli cells of the rat. Am. J. Anat. 154, 455-476.
    • (1979) Am. J. Anat , vol.154 , pp. 455-476
    • Rambourg, A.1    Clermont, Y.2    Hermo, L.3
  • 133
    • 0002471181 scopus 로고    scopus 로고
    • Three-dimensional structure of the Golgi apparatus in mammalian cells
    • Berger, E. G. and Roth, J, eds, pp, Birkhäuser, Basel
    • Rambourg, A. and Clermont, Y. (1997) Three-dimensional structure of the Golgi apparatus in mammalian cells. In: The Golgi Apparatus, Berger, E. G. and Roth, J. (eds), pp. 37-61, Birkhäuser , Basel.
    • (1997) The Golgi Apparatus , pp. 37-61
    • Rambourg, A.1    Clermont, Y.2
  • 134
    • 0033594080 scopus 로고    scopus 로고
    • Golgi structure in three dimensions: Functional insights from the normal rat kidney cell
    • Ladinsky, M. S., Mastronarde, D. N., McIntosh, J. R., Howell, K. E. and Stae-helin, L. A. (1999) Golgi structure in three dimensions: functional insights from the normal rat kidney cell. J. Cell Biol. 144, 1135-1149.
    • (1999) J. Cell Biol , vol.144 , pp. 1135-1149
    • Ladinsky, M.S.1    Mastronarde, D.N.2    McIntosh, J.R.3    Howell, K.E.4    Stae-helin, L.A.5
  • 136
    • 39749142542 scopus 로고    scopus 로고
    • Retrograde traffic in the biosynthetic-secretory route
    • Pavelka, M,, Neumüller, J. and Ellinger A. (2008) Retrograde traffic in the biosynthetic-secretory route. Histochem. Cell Biol. 129, 277-288.
    • (2008) Histochem. Cell Biol , vol.129 , pp. 277-288
    • Pavelka, M.1    Neumüller, J.2    Ellinger, A.3
  • 138
    • 2442640305 scopus 로고    scopus 로고
    • Predicting function from structure: 3-D structure studies of the mammalian Golgi complex
    • Mogelsvang, S., Marsh, B. J., Ladinsky, M. S. and Howell, K. E. (2004) Predicting function from structure: 3-D structure studies of the mammalian Golgi complex. Traffic 5, 338-345.
    • (2004) Traffic , vol.5 , pp. 338-345
    • Mogelsvang, S.1    Marsh, B.J.2    Ladinsky, M.S.3    Howell, K.E.4
  • 139
    • 0036678493 scopus 로고    scopus 로고
    • Structure of the Golgi and distribution of reporter molecules at 20 degrees C reveals the complexity of the exit compartments
    • Ladinsky, M. S., Wu, C., McIntosh, S., McIntosh, J. R. and Howell, K. E. (2002) Structure of the Golgi and distribution of reporter molecules at 20 degrees C reveals the complexity of the exit compartments. Mol. Biol. Cell 13, 2810-2825.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2810-2825
    • Ladinsky, M.S.1    Wu, C.2    McIntosh, S.3    McIntosh, J.R.4    Howell, K.E.5
  • 140
    • 33745755614 scopus 로고    scopus 로고
    • Inter-organelle membrane contact sites: Through a glass, darkly
    • Levine, T. and Loewen, C. (2006). Inter-organelle membrane contact sites: through a glass, darkly. Curr. Opin. Cell Biol. 18, 371-378.
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 371-378
    • Levine, T.1    Loewen, C.2
  • 142
    • 33744728346 scopus 로고    scopus 로고
    • Oxysterol-binding protein and VAMP-associated membrane protein are required for sterol-dependent activation of the ceramide transport protein
    • Perry, R. J. and Ridgway, N. D. (2006) Oxysterol-binding protein and VAMP-associated membrane protein are required for sterol-dependent activation of the ceramide transport protein. Mol. Biol. Cell 17, 2604-2616.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2604-2616
    • Perry, R.J.1    Ridgway, N.D.2
  • 143
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • Muniz, M., Morsomme, P. and Riezman, H. (2001) Protein sorting upon exit from the endoplasmic reticulum. Cell 104, 313-320.
    • (2001) Cell , vol.104 , pp. 313-320
    • Muniz, M.1    Morsomme, P.2    Riezman, H.3
  • 144
    • 20544431747 scopus 로고    scopus 로고
    • Protein sorting in the Golgi complex: Shifting paradigms
    • Rodriguez-Boulan, E. and Musch, A. (2005) Protein sorting in the Golgi complex: shifting paradigms. Biochim. Biophys. Acta 1744, 455-464.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 455-464
    • Rodriguez-Boulan, E.1    Musch, A.2
  • 145
    • 33749422547 scopus 로고    scopus 로고
    • Polarized biosynthetic traffic in renal epithelial cells: Sorting, sorting, everywhere
    • Ellis, M. A., Potter, B. A., Cresawn, K. O. and Weisz, O. A. (2006) Polarized biosynthetic traffic in renal epithelial cells: sorting, sorting, everywhere. Am. J. Physiol. Renal Physiol. 291, F707-713.
    • (2006) Am. J. Physiol. Renal Physiol , vol.291
    • Ellis, M.A.1    Potter, B.A.2    Cresawn, K.O.3    Weisz, O.A.4
  • 146
    • 38849131487 scopus 로고    scopus 로고
    • How many ways through the Golgi maze?
    • Prydz, K., Dick, G. and Tveit, H. (2008) How many ways through the Golgi maze? Traffic 9, 299-304.
    • (2008) Traffic , vol.9 , pp. 299-304
    • Prydz, K.1    Dick, G.2    Tveit, H.3
  • 147
    • 0028969528 scopus 로고
    • Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface
    • Futter, C. E., Connolly, C. N., Cutler, D. F. and Hopkins, C. R. (1995) Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface. J. Biol. Chem. 270, 10999-11003.
    • (1995) J. Biol. Chem , vol.270 , pp. 10999-11003
    • Futter, C.E.1    Connolly, C.N.2    Cutler, D.F.3    Hopkins, C.R.4
  • 148
    • 8444221583 scopus 로고    scopus 로고
    • Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells
    • Ang, A. L., Taguchi, T., Francis, S., Folsch, H., Murrells, L. J., Pypaert, M., Warren, G. and Mellman, I. (2004) Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells. J. Cell Biol. 167, 531-543.
    • (2004) J. Cell Biol , vol.167 , pp. 531-543
    • Ang, A.L.1    Taguchi, T.2    Francis, S.3    Folsch, H.4    Murrells, L.J.5    Pypaert, M.6    Warren, G.7    Mellman, I.8
  • 149
    • 16344363943 scopus 로고    scopus 로고
    • Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin
    • Lock, J. G. and Stow, J. L. (2005) Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin. Mol. Biol. Cell 16, 1744-1755.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1744-1755
    • Lock, J.G.1    Stow, J.L.2
  • 152
    • 12444283809 scopus 로고    scopus 로고
    • Structure and dynamics of the Golgi complex at 15 degrees C: Low temperature induces the formation of Golgi-derived tubules
    • Martinez-Alonso, E., Egea, G., Ballesta, J. and Martinez-Menarguez, J. A. (2005) Structure and dynamics of the Golgi complex at 15 degrees C: Low temperature induces the formation of Golgi-derived tubules. Traffic 6, 32-44.
    • (2005) Traffic , vol.6 , pp. 32-44
    • Martinez-Alonso, E.1    Egea, G.2    Ballesta, J.3    Martinez-Menarguez, J.A.4
  • 153
    • 0015096084 scopus 로고
    • Synthesis, intracellular transport, and discharge of secretory proteins in stimulated pancreatic exocrine cells
    • Jamieson, J. D. and Palade, G. E. (1971) Synthesis, intracellular transport, and discharge of secretory proteins in stimulated pancreatic exocrine cells. J. Cell Biol. 50, 135-158.
    • (1971) J. Cell Biol , vol.50 , pp. 135-158
    • Jamieson, J.D.1    Palade, G.E.2
  • 154
    • 0017814833 scopus 로고
    • Recovery of surface membrane in anterior pituitary cells. Variations in traffic detected with anionic and cationic ferritin
    • Farquhar, M. G. (1978) Recovery of surface membrane in anterior pituitary cells. Variations in traffic detected with anionic and cationic ferritin. J. Cell Biol. 77, R35-42.
    • (1978) J. Cell Biol , vol.77
    • Farquhar, M.G.1
  • 155
    • 0019769965 scopus 로고    scopus 로고
    • Farquhar, M. G. and Palade, G. E. (1981) The Golgi apparatus (complex)-(1954-1981)-from artifact to center stage. J. Cell Biol. 91, 77 s-103 s.
    • Farquhar, M. G. and Palade, G. E. (1981) The Golgi apparatus (complex)-(1954-1981)-from artifact to center stage. J. Cell Biol. 91, 77 s-103 s.
  • 156
    • 0034766485 scopus 로고    scopus 로고
    • The ER to Golgi interface is the major concentration site of secretory proteins in the exocrine pancreatic cell
    • Oprins, A., Rabouille, C., Posthuma, G., Klumperman, J., Geuze, H. J. and Slot, J. W. (2001) The ER to Golgi interface is the major concentration site of secretory proteins in the exocrine pancreatic cell. Traffic 2, 831-838.
    • (2001) Traffic , vol.2 , pp. 831-838
    • Oprins, A.1    Rabouille, C.2    Posthuma, G.3    Klumperman, J.4    Geuze, H.J.5    Slot, J.W.6
  • 158
    • 0021246906 scopus 로고
    • The mannose-6-phosphate receptor for lysosomal enzymes is concentrated in cis-Golgi cisternae
    • Brown, W. J. and Farquhar, M. G. (1984) The mannose-6-phosphate receptor for lysosomal enzymes is concentrated in cis-Golgi cisternae. Cell 36, 295-307.
    • (1984) Cell , vol.36 , pp. 295-307
    • Brown, W.J.1    Farquhar, M.G.2
  • 160
    • 0023496264 scopus 로고
    • The distribution of 215-kilodalton mannose 6-phosphate receptors within cis (heavy) and trans (light) Golgi subfractions varies in different cell types
    • Brown, W. J. and Farquhar, M. G. (1987) The distribution of 215-kilodalton mannose 6-phosphate receptors within cis (heavy) and trans (light) Golgi subfractions varies in different cell types. Proc. Natl. Acad. Sci. USA 84, 9001-9005.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 9001-9005
    • Brown, W.J.1    Farquhar, M.G.2
  • 161
    • 0013882085 scopus 로고
    • Origin of granules in polymorphonuclear leukocytes. Two types derived from opposite faces of the Golgi complex in developing granulocytes
    • Bainton, D. F. and Farquhar, M. G. (1966) Origin of granules in polymorphonuclear leukocytes. Two types derived from opposite faces of the Golgi complex in developing granulocytes. J. Cell Biol. 28, 277-301.
    • (1966) J. Cell Biol , vol.28 , pp. 277-301
    • Bainton, D.F.1    Farquhar, M.G.2
  • 162
    • 0030014148 scopus 로고    scopus 로고
    • Moving membrane up to the front of migrating cells
    • Bretscher, M. S. (1996) Moving membrane up to the front of migrating cells. Cell 85, 465-467.
    • (1996) Cell , vol.85 , pp. 465-467
    • Bretscher, M.S.1
  • 163
    • 0032789927 scopus 로고    scopus 로고
    • The polarization of the motile cell
    • Nabi, I. R. (1999) The polarization of the motile cell. J. Cell Sci. 112, 1803-1811.
    • (1999) J. Cell Sci , vol.112 , pp. 1803-1811
    • Nabi, I.R.1
  • 164
    • 33748466150 scopus 로고    scopus 로고
    • Endocytic recycling pathways: Emerging regulators of cell migration
    • Jones, M. C., Caswell, P. T. and Norman, J. C. (2006) Endocytic recycling pathways: emerging regulators of cell migration. Curr. Opin. Cell Biol. 18, 549-557.
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 549-557
    • Jones, M.C.1    Caswell, P.T.2    Norman, J.C.3
  • 165
    • 34247282758 scopus 로고    scopus 로고
    • Functional symmetry of endomembranes
    • Saraste, J. and Goud, B. (2007) Functional symmetry of endomembranes. Mol. Biol. Cell 18, 1430-1436.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1430-1436
    • Saraste, J.1    Goud, B.2
  • 166
    • 0028286028 scopus 로고
    • Disruption of the Golgi apparatus by brefeldin A blocks cell polarization and inhibits directed cell migration
    • Bershadsky, A. D. and Futerman, A. H. (1994) Disruption of the Golgi apparatus by brefeldin A blocks cell polarization and inhibits directed cell migration. Proc. Natl. Acad. Sci. USA 91, 5686-5689.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5686-5689
    • Bershadsky, A.D.1    Futerman, A.H.2
  • 167
    • 0029096817 scopus 로고
    • Lonely MHC molecules seeking immunogenic peptides for meaningful relationships
    • Mellman, I., Pierre, P. and Amigorena, S. (1995) Lonely MHC molecules seeking immunogenic peptides for meaningful relationships. Curr. Opin. Cell Biol. 7, 564-572.
    • (1995) Curr. Opin. Cell Biol , vol.7 , pp. 564-572
    • Mellman, I.1    Pierre, P.2    Amigorena, S.3
  • 168
    • 1842292202 scopus 로고    scopus 로고
    • Immunocytochemical analysis of Uukuniemi virus budding compartments: Role of the intermediate compartment and the Golgi stack in virus maturation
    • Jäntti, J., Hilden, P., Rönka, H., Mäkiranta, V., Keränen, S. and Kuismanen, E. (1997) Immunocytochemical analysis of Uukuniemi virus budding compartments: role of the intermediate compartment and the Golgi stack in virus maturation. J. Virol. 71, 1162-1172.
    • (1997) J. Virol , vol.71 , pp. 1162-1172
    • Jäntti, J.1    Hilden, P.2    Rönka, H.3    Mäkiranta, V.4    Keränen, S.5    Kuismanen, E.6
  • 169
    • 0032845105 scopus 로고    scopus 로고
    • Structural maturation of the transmissible gastroenteritis coronavirus
    • Salanueva, I. J., Carrascosa, J. L. and Risco, C. (1999) Structural maturation of the transmissible gastroenteritis coronavirus. J. Virol. 73, 7952-7964.
    • (1999) J. Virol , vol.73 , pp. 7952-7964
    • Salanueva, I.J.1    Carrascosa, J.L.2    Risco, C.3
  • 170
    • 0036145462 scopus 로고    scopus 로고
    • Assembly of vaccinia virus revisited: De novo membrane synthesis or acquisition from the host?
    • Sodeik, B. and Krijnse-Locker, J. (2002) Assembly of vaccinia virus revisited: de novo membrane synthesis or acquisition from the host? Trends Microbiol. 10, 15-24.
    • (2002) Trends Microbiol , vol.10 , pp. 15-24
    • Sodeik, B.1    Krijnse-Locker, J.2
  • 172
    • 35548989199 scopus 로고    scopus 로고
    • Poliovirus infection blocks ERGIC-to-Golgi trafficking and induces microtubule-dependent disruption of the Golgi complex
    • Beske, O., Reichelt, M., Taylor, M. P., Kirkegaard, K. and Andino, R. (2007) Poliovirus infection blocks ERGIC-to-Golgi trafficking and induces microtubule-dependent disruption of the Golgi complex. J. Cell Sci. 120, 3207-3218.
    • (2007) J. Cell Sci , vol.120 , pp. 3207-3218
    • Beske, O.1    Reichelt, M.2    Taylor, M.P.3    Kirkegaard, K.4    Andino, R.5
  • 173
    • 11144295188 scopus 로고    scopus 로고
    • Cell biology of the plant Golgi apparatus
    • Hawes, C. (2005) Cell biology of the plant Golgi apparatus. New Phytol. 165, 29-44.
    • (2005) New Phytol , vol.165 , pp. 29-44
    • Hawes, C.1
  • 174
    • 0033130151 scopus 로고    scopus 로고
    • Export of Plasmodium proteins via a novel secretory pathway
    • Wiser, M. F., Lanners, H. N. and Bafford, R. A. (1999) Export of Plasmodium proteins via a novel secretory pathway. Parasitol. Today 15, 194-198.
    • (1999) Parasitol. Today , vol.15 , pp. 194-198
    • Wiser, M.F.1    Lanners, H.N.2    Bafford, R.A.3
  • 175
    • 0344740599 scopus 로고    scopus 로고
    • BFA-sensitive and insensitive exocytic pathways in Entamoeba histolytica trophozoites: Their relationship to pathogenesis
    • Manning-Cela, R., Marquez, C., Franco, E., Talamas-Rohana, P. and Meza, I. (2003) BFA-sensitive and insensitive exocytic pathways in Entamoeba histolytica trophozoites: their relationship to pathogenesis. Cell. Microbiol. 5, 921-932.
    • (2003) Cell. Microbiol , vol.5 , pp. 921-932
    • Manning-Cela, R.1    Marquez, C.2    Franco, E.3    Talamas-Rohana, P.4    Meza, I.5
  • 176
    • 0037884975 scopus 로고    scopus 로고
    • The secretory apparatus of an ancient eukaryote: Protein sorting to separate export pathways occurs before formation of transient Golgi-like compartments
    • Marti, M., Li, Y., Schraner, E. M., Wild, P., Kohler, P. and Hehl, A. B. (2003) The secretory apparatus of an ancient eukaryote: protein sorting to separate export pathways occurs before formation of transient Golgi-like compartments. Mol. Biol. Cell 14, 1433-1447.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1433-1447
    • Marti, M.1    Li, Y.2    Schraner, E.M.3    Wild, P.4    Kohler, P.5    Hehl, A.B.6
  • 177
    • 0029879919 scopus 로고    scopus 로고
    • Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells
    • Yoshimori, T., Keller, P., Roth, M. G. and Simons, K. (1996) Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells. J. Cell Biol. 133, 247-256.
    • (1996) J. Cell Biol , vol.133 , pp. 247-256
    • Yoshimori, T.1    Keller, P.2    Roth, M.G.3    Simons, K.4
  • 178
    • 0032963006 scopus 로고    scopus 로고
    • Dendritic and postsynaptic protein synthetic machinery
    • Gardiol, A., Racca, C. and Triller, A. (1999) Dendritic and postsynaptic protein synthetic machinery. J. Neurosci. 19, 168-179.
    • (1999) J. Neurosci , vol.19 , pp. 168-179
    • Gardiol, A.1    Racca, C.2    Triller, A.3
  • 179
    • 0035814906 scopus 로고    scopus 로고
    • Evidence for a satellite secretory pathway in neuronal dendritic spines
    • Pierce, J. P., Mayer, T. and McCarthy, J. B. (2001) Evidence for a satellite secretory pathway in neuronal dendritic spines. Curr. Biol. 11, 351-355.
    • (2001) Curr. Biol , vol.11 , pp. 351-355
    • Pierce, J.P.1    Mayer, T.2    McCarthy, J.B.3
  • 180
    • 34548291030 scopus 로고    scopus 로고
    • Secrets of the secretory pathway in dendrite growth
    • Ehlers, M. D. (2007) Secrets of the secretory pathway in dendrite growth. Neuron 55, 686-689.
    • (2007) Neuron , vol.55 , pp. 686-689
    • Ehlers, M.D.1
  • 181
    • 34547937104 scopus 로고    scopus 로고
    • Growing dendrites and axons differ in their reliance on the secretory pathway
    • Ye, B., Zhang, Y., Song, W., Younger, S. H., Jan, L. Y. and Jan, Y. N. (2007) Growing dendrites and axons differ in their reliance on the secretory pathway. Cell 130, 717-729.
    • (2007) Cell , vol.130 , pp. 717-729
    • Ye, B.1    Zhang, Y.2    Song, W.3    Younger, S.H.4    Jan, L.Y.5    Jan, Y.N.6
  • 182
    • 33746778834 scopus 로고    scopus 로고
    • Rough sheets and smooth tubules
    • Shibata, Y., Voeltz, G. K. and Rapoport, T. A. (2006) Rough sheets and smooth tubules. Cell 126, 435-439.
    • (2006) Cell , vol.126 , pp. 435-439
    • Shibata, Y.1    Voeltz, G.K.2    Rapoport, T.A.3
  • 183
    • 0025917178 scopus 로고
    • Brefeldin A does not inhibit the movement of phosphatidylethanolamine from its sites for synthesis to the cell surface
    • Vance, J. E., Aasman, E. J. and Szarka, R. (1991) Brefeldin A does not inhibit the movement of phosphatidylethanolamine from its sites for synthesis to the cell surface. J. Biol. Chem. 266, 8241-8247.
    • (1991) J. Biol. Chem , vol.266 , pp. 8241-8247
    • Vance, J.E.1    Aasman, E.J.2    Szarka, R.3
  • 184
    • 0027508117 scopus 로고
    • Sphingomyelin transport to the cell surface occurs independently of protein secretion in rat hepatocytes
    • Shiao, Y. J. and Vance, J. E. (1993) Sphingomyelin transport to the cell surface occurs independently of protein secretion in rat hepatocytes. J. Biol. Chem. 268, 26085-26092.
    • (1993) J. Biol. Chem , vol.268 , pp. 26085-26092
    • Shiao, Y.J.1    Vance, J.E.2
  • 186
    • 9144274481 scopus 로고    scopus 로고
    • Ganglioside GD3 traffics from the trans-Golgi network to plasma membrane by a Rab11-independent and brefeldin A-insensitive exocytic pathway
    • Crespo, P. M., Iglesias-Bartolome, R. and Daniotti, J. L. (2004) Ganglioside GD3 traffics from the trans-Golgi network to plasma membrane by a Rab11-independent and brefeldin A-insensitive exocytic pathway. J. Biol. Chem 279, 47610-47618.
    • (2004) J. Biol. Chem , vol.279 , pp. 47610-47618
    • Crespo, P.M.1    Iglesias-Bartolome, R.2    Daniotti, J.L.3
  • 187
    • 27644547807 scopus 로고    scopus 로고
    • Mechanisms of Cx43 and Cx26 transport to the plasma membrane and gap junction regeneration
    • Thomas, T., Jordan, K., Simek, J., Shao, Q., Jedeszko, C., Walton, P. and Laird, D. W. (2005) Mechanisms of Cx43 and Cx26 transport to the plasma membrane and gap junction regeneration. J. Cell Sci. 118, 4451-4462.
    • (2005) J. Cell Sci , vol.118 , pp. 4451-4462
    • Thomas, T.1    Jordan, K.2    Simek, J.3    Shao, Q.4    Jedeszko, C.5    Walton, P.6    Laird, D.W.7
  • 188
    • 0026703819 scopus 로고
    • Selective inhibition of protein targeting to the apical domain of MDCK cells by brefeldin A
    • Low, S. H., Tang, B. L., Wong, S. H. and Hong, W. (1992) Selective inhibition of protein targeting to the apical domain of MDCK cells by brefeldin A. J. Cell Biol. 118, 51-62.
    • (1992) J. Cell Biol , vol.118 , pp. 51-62
    • Low, S.H.1    Tang, B.L.2    Wong, S.H.3    Hong, W.4
  • 189
    • 0344081339 scopus 로고    scopus 로고
    • The paranodal complex of F3/contactin and caspr/paranodin traffics to the cell surface via a non-conventional pathway
    • Bonnon, C., Goutebroze, L., Denisenko-Nehrbass, N., Girault, J. A. and Faivre-Sarrailh, C. (2003) The paranodal complex of F3/contactin and caspr/paranodin traffics to the cell surface via a non-conventional pathway. J. Biol. Chem. 278, 48339-48347.
    • (2003) J. Biol. Chem , vol.278 , pp. 48339-48347
    • Bonnon, C.1    Goutebroze, L.2    Denisenko-Nehrbass, N.3    Girault, J.A.4    Faivre-Sarrailh, C.5
  • 190
    • 0028575371 scopus 로고
    • Analysis of transport and targeting of syndecan-1: Effect of cytoplasmic tail deletions
    • Miettinen, H. M., Edwards, S. N. and Jalkanen, M. (1994) Analysis of transport and targeting of syndecan-1: effect of cytoplasmic tail deletions. Mol. Biol. Cell 5, 1325-1339.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1325-1339
    • Miettinen, H.M.1    Edwards, S.N.2    Jalkanen, M.3
  • 191
    • 4344672352 scopus 로고    scopus 로고
    • Prointegrin maturation follows rapid trafficking and processing of MT1-MMP in furin-negative colon carcinoma LoVo cells
    • Deryugina, E. I., Ratnikov, B. I., Yu, Q., Baciu, P. C., Rozanov, D. V. and Strongin, A. Y. (2004) Prointegrin maturation follows rapid trafficking and processing of MT1-MMP in furin-negative colon carcinoma LoVo cells. Traffic 5, 627-641.
    • (2004) Traffic , vol.5 , pp. 627-641
    • Deryugina, E.I.1    Ratnikov, B.I.2    Yu, Q.3    Baciu, P.C.4    Rozanov, D.V.5    Strongin, A.Y.6
  • 192
    • 2942617262 scopus 로고    scopus 로고
    • Exocytic pathway-independent plasmamembrane targeting of heterotrimeric G proteins
    • Takida, S. and Wedegaertner, P. B. (2004) Exocytic pathway-independent plasmamembrane targeting of heterotrimeric G proteins. FEBS Lett. 567, 209-213.
    • (2004) FEBS Lett , vol.567 , pp. 209-213
    • Takida, S.1    Wedegaertner, P.B.2
  • 193
    • 0037304607 scopus 로고    scopus 로고
    • The exocytotic trafficking of TC10 occurs through both classical and non-classical secretory transport pathways in 3T3L1 adipocytes
    • Watson, R. T., Furukawa, M., Chiang, S. H., Boeglin, D., Kanzaki, M., Saltiel, A. R. and Pessin, J. E. (2003) The exocytotic trafficking of TC10 occurs through both classical and non-classical secretory transport pathways in 3T3L1 adipocytes. Mol. Cell Biol. 23, 961-974.
    • (2003) Mol. Cell Biol , vol.23 , pp. 961-974
    • Watson, R.T.1    Furukawa, M.2    Chiang, S.H.3    Boeglin, D.4    Kanzaki, M.5    Saltiel, A.R.6    Pessin, J.E.7
  • 194
    • 0037073697 scopus 로고    scopus 로고
    • Flotillin-1/reggie-2 traffics to surface raft domains via a novel Golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation
    • Morrow, I. C., Rea, S., Martin, S., Prior, I. A., Prohaska, R., Hancock, J. F., James, D. E. and Parton, R. G. (2002) Flotillin-1/reggie-2 traffics to surface raft domains via a novel Golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation. J. Biol. Chem. 277, 48834-48841.
    • (2002) J. Biol. Chem , vol.277 , pp. 48834-48841
    • Morrow, I.C.1    Rea, S.2    Martin, S.3    Prior, I.A.4    Prohaska, R.5    Hancock, J.F.6    James, D.E.7    Parton, R.G.8
  • 195
    • 37549067350 scopus 로고    scopus 로고
    • Low temperature induces the delivery of mature and immature CFTR to the plasma membrane
    • Rennolds, J., Boyaka, P. N., Bellis, S. L. and Cormet-Boyaka, E. (2008) Low temperature induces the delivery of mature and immature CFTR to the plasma membrane. Biochem. Biophys. Res. Commun. 366, 1025-1029.
    • (2008) Biochem. Biophys. Res. Commun , vol.366 , pp. 1025-1029
    • Rennolds, J.1    Boyaka, P.N.2    Bellis, S.L.3    Cormet-Boyaka, E.4
  • 196
    • 2342620103 scopus 로고    scopus 로고
    • Vesicle budding from endoplasmic reticulum is involved in calsequestrin routing to sarcoplasmic reticulum of skeletal muscles
    • Nori, A., Bortoloso, E., Frasson, F., Valle, G. and Volpe, P. (2004) Vesicle budding from endoplasmic reticulum is involved in calsequestrin routing to sarcoplasmic reticulum of skeletal muscles. Biochem. J. 379, 505-512.
    • (2004) Biochem. J , vol.379 , pp. 505-512
    • Nori, A.1    Bortoloso, E.2    Frasson, F.3    Valle, G.4    Volpe, P.5
  • 197
    • 0028210170 scopus 로고
    • Synthesis of surface sphingomyelin in the plasma membrane recycling pathway of BHK cells
    • Kallen, K.-J., Allan, D., Whatmore, J. and Quinn, P. (1994) Synthesis of surface sphingomyelin in the plasma membrane recycling pathway of BHK cells. Biochim. Biophys. Acta 1191, 52-58.
    • (1994) Biochim. Biophys. Acta , vol.1191 , pp. 52-58
    • Kallen, K.-J.1    Allan, D.2    Whatmore, J.3    Quinn, P.4
  • 198
    • 0027154604 scopus 로고
    • Epithelial sphingolipid sorting is insensitive to reorganization of the Golgi by nocodazole, but is abolished by monensin in MDCK cells and brefeldin A in Caco-2 cells
    • van Meer, G. and 't Hof, W. (1993) Epithelial sphingolipid sorting is insensitive to reorganization of the Golgi by nocodazole, but is abolished by monensin in MDCK cells and brefeldin A in Caco-2 cells. J. Cell Sci. 104, 833-842.
    • (1993) J. Cell Sci , vol.104 , pp. 833-842
    • van Meer, G.1    't Hof, W.2
  • 199
    • 0028984235 scopus 로고
    • Immunocytochemical localization of b-COP to the ER-Golgi boundary and the TGN
    • Griffiths, G., Pepperkok, R., Krijnse Locker, J. and Kreis, T. E. (1995) Immunocytochemical localization of b-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    Krijnse Locker, J.3    Kreis, T.E.4
  • 200
    • 38849095347 scopus 로고    scopus 로고
    • dGRASP-mediated non-canonical integrin secretion is required for Drosophila epithelial remodeling
    • Schotman, H., Karhinen, L. and Rabouille, C. (2008) dGRASP-mediated non-canonical integrin secretion is required for Drosophila epithelial remodeling. Dev. Cell 14, 171-182.
    • (2008) Dev. Cell , vol.14 , pp. 171-182
    • Schotman, H.1    Karhinen, L.2    Rabouille, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.