REFERENCES

1. 1. Balch W. E.

   (1989). Biochemistry of interorganelle transport. J. Biol. Chem 264, 16965–16968

   OpenUrlFREE Full Text
2. 1. Balch W. E.

   (1990). Molecular dissection of early stages of the eukaryotic secretory pathway. Curr. Opin. Cell Biol 2, 634–644

   OpenUrlCrossRefPubMed
3. 1. Banfield D. K.,
   2. Lewis M. J.,
   3. Rabouille C.,
   4. Warren G. and
   5. Pelham H. R. B.

   (1994). Localization of sed5, a putative vesicle targeting molecule, to the cis-Golgi network involves both its transmembrane domain and cytoplasmic domains. J. Cell Biol 127, 357–371

   OpenUrlAbstract/FREE Full Text
4. 1. Barlowe C.,
   2. Orci L.,
   3. Yueng T.,
   4. Hosobuchi M.,
   5. Hamamoto S.,
   6. Salama N.,
   7. Rexach M.,
   8. Ravazzola M. and
   9. Schekman R.

   (1994). COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the ER. Cell 77, 895–907

   OpenUrlCrossRefPubMedWeb of Science
5. 1. Bergman J.,
   2. Tokuyasu K. T. and
   3. Singer S. J.

   (1981). Passage of an integral membrane protein, the vesicular stomatitis virus glycoprotein, through the Golgi apparatus on route to the plasma membrane. Proc. Nat. Acad. Sci. USA 78, 1746–1750

   OpenUrlAbstract/FREE Full Text
6. 1. Bergman J. E. and
   2. Fusco P. J.

   (1991). The G protein of vesicular stomatitis virus has free access into and egress from the smooth endoplasmic reticulum of UT-1 cells. J. Cell Biol 110, 625–635

   OpenUrl
7. 1. Bonatti S.,
   2. Migliaccio G. and
   3. Simons K.

   (1989). Palmitosylation of viral membrane glycoprotein takes places after exit from the endoplasmic reticulum. J. Biol. Chem 264, 12590–12595

   OpenUrlAbstract/FREE Full Text
8. 1. Doms R. W.,
   2. Keller D. S.,
   3. Helenius A. and
   4. Balch W. E.

   (1987). Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers. J. Cell Biol 105, 1957–1969

   OpenUrlAbstract/FREE Full Text
9. 1. Doms R. W.,
   2. Lamb R. A.,
   3. Rose J. K. and
   4. Helenius A.

   (1993). Folding and assembly of viral membrane proteins. Virology 193, 545–562

   OpenUrlCrossRefPubMedWeb of Science
10. 1. Duden R.,
    2. Griffiths G.,
    3. Frank R.,
    4. Argos P. and
    5. Kreis T. E.

    (1991). -COP, a 110Kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to -adaptin. Cell 64, 649–665

    OpenUrlCrossRefPubMedWeb of Science
11. 1. Duden R.,
    2. Hosobuchi M.,
    3. Hamamoto S.,
    4. Winey M.,
    5. Byers B. and
    6. Schekman R.

    (1994). Yeast-and -coat proteins (COP). J. Biol. Chem 269, 24486–24495

    OpenUrlAbstract/FREE Full Text
12. 1. Griffiths G.,
    2. Warren G.,
    3. Stuhlfauth I. and
    4. Jockusch B. M.

    (1981). The role of clathrin-coated vesicles in acrosome formation. Eur. J. Cell Biol 26, 52–60

    OpenUrlPubMedWeb of Science
13. 1. Griffiths G.,
    2. Pfeiffer S.,
    3. Simons K. and
    4. Matlin K.

    (1985). Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane. J. Cell Biol 101, 949–964

    OpenUrlAbstract/FREE Full Text
14. 1. Griffiths G.,
    2. Fuller S.D.,
    3. Back R.,
    4. Hollinshead D.,
    5. Pfeiffer S. and
    6. Simons K.

    (1989). The dynamic nature of the Golgi complex. J. Cell Biol 108, 277–297

    OpenUrlAbstract/FREE Full Text
15. 1. Griffiths G. and
    2. Rottier P. J. M.

    (1992). Cell biology of viruses that assemble along the biosynthetic pathway. Semin. Cell Biol 3, 367–381

    OpenUrlCrossRefPubMed
16. 1. Griffiths G.,
    2. Ericsson M.,
    3. Krijnse-Locker J.,
    4. Nilsson T.,
    5. Goud B.,
    6. Söling H.-D.,
    7. Tang B. L.,
    8. Wong S. H. and
    9. Hong W.

    (1994). Localization of the Lys, Asp, Glu, Leu tetrapeptide receptor to the Golgi complex and the intermediate compartment in mammalian cells. J. Cell Biol 127, 1557–1574

    OpenUrlAbstract/FREE Full Text
17. 1. Hammond C. and
    2. Helenius A.

    (1994). Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves recycling between the ER, intermediate compartment, and the Golgi apparatus. J. Cell Biol 126, 41–52

    OpenUrlAbstract/FREE Full Text
18. 1. Hobman T. C.,
    2. Woodward L. and
    3. Farquhar M. G.

    (1992). The rubella virus E1 glycoprotein is arrested in a novel post-ER, pre-Golgi compartment. J. Cell Biol 118, 795–811

    OpenUrlAbstract/FREE Full Text
19. 1. Hosobuchi M.,
    2. Kreis T. and
    3. Schekman R.

    (1992). SEC21 is a gene required for ER to Golgi protein transport that encodes a subunit of a yeast coatomer. Nature 360, 603–605

    OpenUrlCrossRefPubMedWeb of Science
20. 1. Klumperman J.,
    2. Hille A.,
    3. Veenendaal T.,
    4. Oorshot V.,
    5. Stoorvogel W.,
    6. von Figura K. and
    7. Geuze H.

    (1993). Differences in the endosomal distributions of the two mannose 6-phosphate receptors. J. Cell Biol 121, 997–1010

    OpenUrlAbstract/FREE Full Text
21. 1. Kreis T. E.

    (1986). Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface. EMBO J 5, 931–941

    OpenUrlPubMedWeb of Science
22. 1. Kreis T. E. and
    2. Lodish H. F.

    (1986). Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface. Cell 46, 929–937

    OpenUrlCrossRefPubMedWeb of Science
23. 1. Krijnse Locker J.,
    2. Ericsson M.,
    3. Rottier P. J. M. and
    4. Griffiths G.

    (1994). Characterization of the budding compartment of mouse hepatitis virus. J. Cell Biol 124, 55–70

    OpenUrlAbstract/FREE Full Text
24. 1. Letourneur F.,
    2. Gaynor E. C.,
    3. Hennecke S.,
    4. Demolliere C.,
    5. Duden R.,
    6. Emr S. D.,
    7. Riezman H. and
    8. Cosson P.

    (1994). Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum. Cell 79, 1199–1207

    OpenUrlCrossRefPubMedWeb of Science
25. 1. Lotti L. V.,
    2. Torrisi M.-R.,
    3. Pascale M. C. and
    4. Bonatti S.

    (1992). Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex. J. Cell Biol 118, 43–50

    OpenUrlAbstract/FREE Full Text
26. 1. Matlin K. S. and
    2. 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

    OpenUrlCrossRefPubMedWeb of Science
27. 1. Oprins A.,
    2. Duden R.,
    3. Kreis T. E.,
    4. Geuze H. J. and
    5. Slot J. W.

    (1993). -COP localizes mainly to the cis-Golgi side in exocrine pancreas. J. Cell Biol 121, 49–59

    OpenUrlAbstract/FREE Full Text
28. 1. Orci L.,
    2. Ravazzola M.,
    3. Amherdt M.,
    4. Louvard D. and
    5. Perrelet A.

    (1985). Clathrin-immunoreactive sites in the Golgi apparatus are concentrated at the trans pole in polypeptide hormone-secreting cells. Proc. Nat. Acad. Sci. USA 82, 5385–5389

    OpenUrlAbstract/FREE Full Text
29. 1. Orci L.,
    2. Palmer D. J.,
    3. Ravazzola M.,
    4. Perrelet A.,
    5. Amherdt M. and
    6. Rothman J. E.

    (1993). Budding from Golgi membranes requires the coatomer complex of non-clathrin coat proteins. Nature 362, 648–652

    OpenUrlCrossRefPubMedWeb of Science
30. 1. Palade G. E.

    (1975). Intracellular aspects of the process of protein synthesis. Science 189, 347–358

    OpenUrlFREE Full Text
31. 1. Pepperkok R.,
    2. Scheel J.,
    3. Horstmann H.,
    4. Hauri H. P.,
    5. Griffiths G. and
    6. Kreis T. E.

    (1993). -COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell 74, 71–82

    OpenUrlCrossRefPubMedWeb of Science
32. 1. Peter F.,
    2. Plutner H.,
    3. Zhu H.,
    4. Kreis T. E. and
    5. Balch W. E.

    (1993). -COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro. J. Cell Biol 122, 1155–1167

    OpenUrlAbstract/FREE Full Text
33. 1. Pind S. N.,
    2. Nuoffer C.,
    3. McCaffery J. M.,
    4. Plutner H.,
    5. Davidson H. W.,
    6. Farquhar M. G. and
    7. Balch W. E.

    (1994). Rab1 and Ca2+are required for the fusion of carrier vesicles mediating endoplasmic reticulum to Golgi transport. J. Cell Biol 125, 239–252

    OpenUrlAbstract/FREE Full Text
34. 1. Pryer N. K.,
    2. Wuestehube L. J. and
    3. Schekman R.

    (1992). Vesicle-mediated protein sorting. Annu. Rev. Biochem 61, 471–516

    OpenUrlCrossRefPubMedWeb of Science
35. 1. Rabouille C.,
    2. Hui N.,
    3. Hunte F.,
    4. Kieckbusch R.,
    5. Berger E. G.,
    6. Warren G. and
    7. Nilsson T.

    (1995). Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J. Cell Sci 108, 1617–1627

    OpenUrlAbstract/FREE Full Text
36. 1. Roth J.,
    2. Taatjes D. J.,
    3. Lucocq J. M.,
    4. Weinstein J. and
    5. Paulson J. C.

    (1985). Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation. Cell 34, 287–295

    OpenUrl
37. 1. Rothman J. E. and
    2. Orci L.

    (1992). Molecular dissection of the secretory pathway. Nature 355, 409–415

    OpenUrlCrossRefPubMed
38. 1. Saraste J. and
    2. 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

    OpenUrlCrossRefPubMedWeb of Science
39. 1. Saraste J.,
    2. Palade G. E. and
    3. Farquhar M. G.

    (1987). Antibodies to rat pancreas Golgi subfractions: identification of a 58-kD cis-Golgi protein. J. Cell Biol 105, 2021–2029

    OpenUrlAbstract/FREE Full Text
40. 1. Saraste J. and
    2. Svensson K.

    (1991). Distribution of the intermediate elements operating in ER to Golgi transport. J. Cell Sci 100, 415–430

    OpenUrlAbstract/FREE Full Text
41. 1. Saraste J.,
    2. Lahtinen U. and
    3. Goud B.

    (1995). Localization of the small GTP-binding protein rab1p to early compartments of the secretory pathway. J. Cell Sci 108, 1541–1552

    OpenUrlAbstract/FREE Full Text
42. 1. Schekman R. W.

    (1992). Genetic and biochemical analysis of vesicular traffic in yeast. Curr. Opin. Cell Biol 4, 587–592

    OpenUrlCrossRefPubMed
43. 1. Sodeik B.,
    2. Doms R. W.,
    3. Ericsson M.,
    4. Hiller G.,
    5. Machamer C. E.,
    6. van ‘t Hof W.,
    7. van Meer G.,
    8. Moss B. and
    9. Griffiths G.

    (1993). Assembly of vaccinia virus: role of the intermediate compartment between the endoplasmic reticulum and the Golgi stacks. J. Cell Biol 121, 521–541

    OpenUrlAbstract/FREE Full Text
44. 1. Schweizer A.,
    2. Fransen J. A. M.,
    3. Baechi T.,
    4. Ginsel L. and
    5. Hauri H. P.

    (1988). Identification, by monoclonal antibody, of a 53-kD proteinassociated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J. Cell Biol 107, 1643–1653

    OpenUrlAbstract/FREE Full Text
45. 1. Schweizer A.,
    2. Fransen J. A. M.,
    3. Matter K.,
    4. Kreis T. E.,
    5. Ginsel L. and
    6. Hauri H.-P.

    (1990). Identification of an intermediate compartment involved in protein transport from the endoplasmic reticulum to the Golgi apparatus. Eur. J. Cell Biol 53, 185–196

    OpenUrlPubMedWeb of Science
46. 1. Shaywitz D. A.,
    2. Orci L.,
    3. Ravazzola M.,
    4. Swaroop A. and
    5. Kaiser C. A.

    (1995). Human SEC13Rp functions in yeast and is located on transport vesicles budding from the endoplasmic reticulum. J. Cell Biol 128, 769–777

    OpenUrlAbstract/FREE Full Text
47. 1. Slot J. W.,
    2. Geuze H. J.,
    3. Gigengack S.,
    4. Lienhard G. E. and
    5. James D. E.

    (1991). Immuno-localization of the insulin regulatable glucose transporter in brown adipose tissue of the rat. J. Cell Biol 113, 123–135

    OpenUrlAbstract/FREE Full Text
48. 1. Tooze S. A.,
    2. Tooze J. and
    3. Warren G.

    (1988). Site of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59. J. Cell Biol 106, 1475–1487

    OpenUrlAbstract/FREE Full Text
49. 1. Warren G.

    (1987). Signals and salvage sequences. Nature 327, 17–18

    OpenUrlCrossRefPubMed
50. 1. Waters G. M.,
    2. Serafini T. and
    3. Rothman J. E.

    (1991). ‘Coatomer’: a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. Nature 349, 248–251

    OpenUrlCrossRefPubMed
51. 1. Weis K.,
    2. Griffiths G. and
    3. Lamond A. I.

    (1994). The endoplasmic reticulum calcium-binding protein of 55 kDa is a novel EF-hand protein retained in the endoplasmic reticulum by a carboxyl-terminal His-Asp-Glu-Leu motif. J. Biol. Chem 269, 19142–19150

    OpenUrlAbstract/FREE Full Text