Sec12p requires Rer1p for sorting to coatomer (COPI)-coated vesicles and retrieval to the ER

Journal of Cell Science

Volumn 110, Issue 8, 1997, Pages 991-1003

  Boehm, Johannes ^a   Letourneur, François ^b   Ballensiefen, Wolfgang ^a   Ossipov, Dmitri ^a   Démollière, Corinne ^c   Schmitt, Hans Dieter ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b INSTITUT DE BIOLOGIE ET CHIMIE DES PROTÉINES   (France)

^c NONE

Author keywords

Coatomer; Endoplasmic reticulum; Recycling RER1 SEC12

Indexed keywords

FUNGAL PROTEIN; HYBRID PROTEIN; MEMBRANE PROTEIN; MUTANT PROTEIN;

ARTICLE; ENDOPLASMIC RETICULUM; FUNGAL GENETICS; FUNGUS MUTANT; GENE MUTATION; GOLGI COMPLEX; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE;

COATOMER PROTEIN; CYTOPLASMIC GRANULES; ENDOPLASMIC RETICULUM; FUNGAL PROTEINS; MEMBRANE GLYCOPROTEINS; MEMBRANE PROTEINS; MUTATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 0030955820     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (58)

1. 2+-ATPase homolog. PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol. Biol. Cell 3, 633-654.
2. Barlowe, C., Orci, L., Yeung, T., Hosobuchi, M., Hamamoto, S., Salama, N., Rexach, M. F., Ravazzola, M., Amherdt, M. and Schekman, R. (1994). COPII - a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77, 895-907.
3. Bednarek, S. Y., Ravazzola, M., Hosobuchi, M., Amherdt, M., Perrelet, A., Schekman, R. and Orci, L. (1995). COPI-coated and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast. Cell 83, 1183-1196.
4. Boehm, J., Ulrich, H. D., Ossig, R. and Schmitt, H. D. (1994). Kex2-dependent invertase secretion as a tool to study the targeting of transmembrane proteins which are involved in ER→Golgi transport in yeast. EMBO J. 13, 3696-3710.
5. Chapman, R. E. and Munro, S. (1994). The functioning of the yeast Golgi apparatus requires an ER protein encoded by ANP1, a member of a new family of genes affecting the secretory pathway. EMBO J. 13, 4896-4907.
6. Cosson, P. and Letourneur, F. (1994). Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 263, 1629-1631.
7. Cosson, P., Démollière, C., Hennecke, S., Duden, R. and Letourneur, F. (1996). δ-COP and ζ-COP, two coatomer subunits homologous to clathrin-associated proteins, are involved in ER retrieval. EMBO J. 15, 1792-1798.
8. Cosson, P., Schröder-Köhne, S., Sweet, D., Démollière, C., Hennecke, S., Frigerio, G. and Letourneur, F. (1997). The Sec20/Tip20p complex is involved in ER retrieval of dilysine-tagged proteins. Eur. J. Cell Biol. (in press).
9. d'Enfert, C., Barlowe, C., Nishikawa, S., Nakano, A. and Schekman, R. (1991). Structural and functional dissection of a membrane glycoprotein required for vesicle budding from the endoplasmic reticulum. Mol. Cell. Biol. 11, 5727-5734.
10. Dascher, C., Ossig, R., Gallwitz, D. and Schmitt, H. D. (1991). Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the ras-superfamily. Mol. Cell. Biol. 11, 872-885.
11. Duden, R., Hosobuchi, M., Hamamoto, S., Winey, M., Byers, B. and Schekman, R. (1994). Yeast β- and β′-coat proteins (COP). Two coatomer subunits essential for endoplasmic reticulum-to-Golgi protein traffic. J. Biol. Chem. 269, 24486-24495.
12. Espenshade, P., Gimeno, R. E., Holzmacher, E., Teung, P. and Kaiser, C. A. (1995). Yeast SEC16 gene encodes a multidomain vesicle protein that interacts with Sec23p. J. Cell Biol. 131, 311-324.
13. Fiedler, K., Veit, M., Stamnes, M. A. and Rothman, J. E. (1996). Bimodal interaction of coatomer with the p24 family of putative caro receptors. Science 273, 1396-1399.
14. Franzusoff, A. and Schekman, R. (1989). Functional compartments of the yeast Golgi apparatus are defined by the sec7 mutation. EMBO J. 8, 2695-2702.
15. Gaynor, E. C., Heesen, S. T., Graham, T. R., Aebi, M. and Emr, S. D. (1994). Signal-mediated retrieval of a membrane-protein from the Golgi to the ER in yeast. J. Cell Biol. 127, 653-665.
16. Graham, T. R. and Emr, S. D. (1991). Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant. J. Cell Biol. 114, 207-218.
17. Hardwick, K. G., Lewis, M. J., Semenza, J., Dean, N. and Pelham, H. R. B. (1990). ERD1, a yeast gene required for the retention of luminal endoplasmic reticulum proteins, affects glycoprotein processing in the Golgi apparatus. EMBO J. 9, 623-630.
18. Harris, S. L. and Waters, M. G. (1996). Localization of a yeast early Golgi mannosyltransferase, Och1p, involves retrograde transport. J. Cell Biol. 132, 985-998.
19. Haubruck, H., Disela, C., Wagner, P. and Gallwitz, D. (1987). The ras-related ypt protein is an ubiquitous eukaryotic protein: isolation and sequence analysis of mouse cDNA clones highly homologous to the yeast YPT1 gene. EMBO J. 6, 4049-4053.
20. Helenius, A. (1994). How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 5, 253-265.
21. Hirschberg, C. B. and Snider, M. D. (1987). Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus. Annu. Rev. Biochem. 56, 63-87.
22. Jackson, M. R., Nilsson, T. and Peterson, P. A. (1990). Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J. 9, 3153-3162.
23. Jackson, M. R., Nilsson, T. and Peterson, P. A. (1993). Retrieval of transmembrane proteins to the endoplasmic reticulum. J. Cell Biol. 121, 317-333.
24. Klionsky, D. J., Herman, P. K. and Emr, S. D. (1990). The fungal vacuole: composition, function, and biogenesis. Microbiol. Rev. 54, 266-292.
25. Kuehn, M. J., Schekman, R. and Ljungdahl, P. O. (1996). Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro. J. Cell Biol. 135, 585-595.
26. Kurjan, J. and Herskowitz, I. (1982). Structure of a yeast pheromone gene (MFα): a putative α-factor precursor contains four tandem copies of mature α-factor. Cell 30, 933-943.
27. Lehle, L., Eiden, A., Lehnert, K., Haselbeck, A. and Kopetzki, E. (1995). Glycoprotein biosynthesis in Saccharomyces cerevisiae: ngd29, an N-glycosylation mutant allelic to och1 having a defect in the initiation of outer chain formation. FEBS Lett. 370, 41-45.
28. Letourneur, F., Gaynor, E. C., Hennecke, S., Démollière, C., Duden, R., Emr, S. D., Riezman, H. and Cosson, P. (1994). Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum. Cell 79, 1199-1207.
29. Lewis, M. J. and Pelham, H. R. B. (1990). A human homologue of the yeast HDEL receptor. Nature 348, 162-163.
30. Lewis, M. J., Sweet, D. J. and Pelham, H. R. (1992). The ERD2 gene determines the specificity of the luminal ER protein retention system. Cell 61, 1359-1363.
31. Lewis, M. J. and Pelham, H. R. B. (1996). SNARE-mediated retrograde traffic from the Golgi-complex to the endoplasmic reticulum. Cell 85, 205-215.
32. Nakanishi-Shindo, Y., Nakayama, K. I., Tanaka, A., Toda, Y. and Jigami, Y. (1993). Structure of the N-linked oligosaccharides that show the complete loss of α-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae. J. Biol. Chem. 268, 26338-26345.
33. Nilsson, T., Jackson, M. and Peterson, P. A. (1989). Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmatic reticulum. Cell 58, 707-718.
34. Nishikawa, S.-I. and Nakano, A. (1993). Identification of a novel gene required for membrane protein retention in the early secretory pathway. Proc. Nat. Acad. Sci. USA 90, 8179-8183
35. Nothwehr, S. F., Conibear, E. and Stevens, T. H. (1995). Golgi and vacuolar membrane-proteins reach the vacuole in vps1 mutant yeast-cells via the plasma-membrane. J. Cell Biol. 129, 35-46.
36. Novick, P., Ferro, S. and Schekman, R. (1981). Order of events in the yeast secretory pathway. Cell 25, 461-469.
37. Ossig, R., Dascher, C., Trepte, H. H., Schmitt, H. D. and Gallwitz, D. (1991). The yeast SLY gene-products, suppressors of detects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport. Mol. Cell. Biol. 11, 2980-2993.
38. Palade, G. (1975). Intracellular aspects of the process of protein secretion. Science 189, 347-358.
39. Pelham, H. R. B. (1988). Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment. EMBO J. 7, 913-918.
40. Pelham, H. R. B. (1994). About turn for the COPs. Cell 79, 1125-1127.
41. Pelham, H. R. B., Hardwick, K. G. and Lewis, M. J. (1988). Sorting of soluble ER proteins in yeast. EMBO J. 7, 1757-1762.
42. Pepperkok, R., Scheel, J., Horstmann, H., Hauri, H. P., Griffiths, G. and Kreis, T. E. (1993). β-COP is essential for biosynthetic membrane-transport from the endoplasmic reticulum to the Golgi-complex in-vivo. Cell 74, 71-82.
43. Preuss, D., Mulholland, J., Franzusoff, A., Segev, N. and Botstein, D. (1992). Characterization of the Saccharomyces Golgi complex through the cell-cycle by immunoelectron microscopy. Mol. Biol. Cell 3, 789-803.
44. Redding, K., Holcomb, C. and Fuller, R. S. (1991). Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae. J. Cell Biol. 113, 527-538.
45. Rexach, M. F., Latterich, M. and Schekman, R. W. (1994). Characteristics of endoplasmic reticulum-derived transport vesicles. J. Cell Biol. 126, 1133-1148.
46. Rose, M. D., Mirsa, L. M. and Vogel, J. P. (1989). KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57, 1211-1221.
47. Rothman, J. E. and Orci, L. (1992). Molecular dissection of the secretory pathway. Nature 355, 409-415.
48. Sato, K., Nishikawa, S. and Nakano, A. (1995). Membrane-protein retrieval from the Golgi-apparatus to the endoplasmic-reticulum (ER) -characterization of the RER1 gene-product as a component involved in ER localization of Sec12p. Mol. Biol. Cell 6, 1459-1477.
49. Sato, M., Sato, K. and Nakano, A. (1996). Endoplasmic reticulum localization of Sec12p is achieved by two mechanisms: Rer1p-dependent retrieval that requires the transmembrane domain and Rer1p-independent retention that involves the cytoplasmic domain. J. Cell Biol. 134, 279-293.
50. Schimmöller, F., Singer-Krüger, B., Schröder, S., Krüger, U., Barlowe, C. and Riezman, H. (1995). The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. EMBO J. 14, 1329-1339.
51. Sherman, F., Fink, G. R. and Hicks, J. B. (1986). Methods in Yeast Genetics. Cold Spring Harbour Laboratory Press, Cold Spring Harbour, NY.
52. Schröder, S., Schimmöller, F., Singer-Krüger, B. and Riezman, H. (1995). The Golgi-localization of yeast Emp47p depends on its di-lysine motif but is not affected by the retI-1 mutation in α-COP. J. Cell Biol. 131, 895-912.
53. Schutze, M. P., Peterson, P. A. and Jackson, M. R. (1994). An N-terminal double-arginine motif maintains type-II membrane-proteins in the endoplasmic reticulum. EMBO J. 13, 1696-1705.
54. Semenza, J. C., Hardwick, K. G., Dean, N. and Pelham, H. R. B. (1990). ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell 61, 1349-1357.
55. Sikorski, R. S. and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
56. Søgaard, M., Tani, K., Ye, R. R., Geromanos, S., Tempst, P., Kirchhausen, T., Rothman, J. E. and Söllner, T. (1994). A rab protein is required for the assembly of snare complexes in the docking of transport vesicles. Cell 78, 937-948.
57. te Heesen, S., Knauer, R., Lehle, L. and Aebi, M. (1993). Yeast Wbp1p and Swp1p form a protein complex essential for oligosaccharyl transferase activity. EMBO J. 12, 279-284.
58. Townsley, F. M. and Pelham, H. R. B. (1994). The KKXX signal mediates retrieval of membrane-proteins from the Golgi to the ER in yeast. Eur. J. Cell Biol. 64, 211-216.