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Volumn 10, Issue 4, 1999, Pages 1043-1059

Two endoplasmic reticulum (ER) membrane proteins that facilitate ER-to- Golgi transport of glycosylphosphatidylinositol-anchored proteins

Author keywords

[No Author keywords available]

Indexed keywords

GLYPICAN; MEMBRANE PROTEIN;

EID: 0032910193     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.4.1043     Document Type: Article
Times cited : (98)

References (72)
  • 1
    • 0029157811 scopus 로고
    • The yeast proprotein convertase encoded by YAP3 is a glycophosphatidylinositol-anchored protein that localizes to the plasma membrane
    • Ash, J., Dominguez, M., Bergeron, J.J., Thomas, D.Y., and Bourbonnais, Y. (1995). The yeast proprotein convertase encoded by YAP3 is a glycophosphatidylinositol-anchored protein that localizes to the plasma membrane. J. Biol. Chem. 270, 20847-20854.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20847-20854
    • Ash, J.1    Dominguez, M.2    Bergeron, J.J.3    Thomas, D.Y.4    Bourbonnais, Y.5
  • 2
    • 0025974216 scopus 로고
    • High-efficiency transformation of yeast by electroporation
    • Becker, D.M., and Guarente, L. (1991). High-efficiency transformation of yeast by electroporation. Methods Enzymol. 194, 182-187.
    • (1991) Methods Enzymol , vol.194 , pp. 182-187
    • Becker, D.M.1    Guarente, L.2
  • 3
    • 0029910214 scopus 로고    scopus 로고
    • Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport
    • Belden, W.J., and Barlowe, C. (1996). Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport. J. Biol. Chem. 271, 26939-26946.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26939-26946
    • Belden, W.J.1    Barlowe, C.2
  • 4
    • 0029827249 scopus 로고    scopus 로고
    • Yeast Gpi8p is essential for GP1 anchor attachment onto proteins
    • Benghezal, M., Benachour, A., Rusconi, S., Aebi, M., and Conzelmann, A. (1996). Yeast Gpi8p is essential for GP1 anchor attachment onto proteins. EMBO J. 15, 6575-6583.
    • (1996) EMBO J. , vol.15 , pp. 6575-6583
    • Benghezal, M.1    Benachour, A.2    Rusconi, S.3    Aebi, M.4    Conzelmann, A.5
  • 5
    • 0029124071 scopus 로고
    • Identification of six complementation classes involved in the biosynthesis of glycosylphosphatidyl inositol anchors in Saccharomyces cerevisiae
    • Benghezal, M., Lipke, P.N., and Conzelmann, A. (1995). Identification of six complementation classes involved in the biosynthesis of glycosylphosphatidyl inositol anchors in Saccharomyces cerevisiae. J. Cell Biol. 130, 1333-1344.
    • (1995) J. Cell Biol. , vol.130 , pp. 1333-1344
    • Benghezal, M.1    Lipke, P.N.2    Conzelmann, A.3
  • 6
    • 0026667338 scopus 로고
    • Interactions between GPI-anchored proteins and membrane lipids
    • Brown, D.A. (1992). Interactions between GPI-anchored proteins and membrane lipids. Trends Cell Biol. 2, 338-343.
    • (1992) Trends Cell Biol. , vol.2 , pp. 338-343
    • Brown, D.A.1
  • 7
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D.A., and Rose, J.K. (1992). Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 8
    • 0025174038 scopus 로고
    • Myo inositol gets incorporated into numerous membrane glycoproteins of Saccharomyces cerevisiae; incorporation is dependent on phosphomannomutase (sec53)
    • Conzelmann, A., Fankhauser, C., and Desponds, C. (1990). Myo inositol gets incorporated into numerous membrane glycoproteins of Saccharomyces cerevisiae; incorporation is dependent on phosphomannomutase (sec53). EMBO J. 9, 653-661.
    • (1990) EMBO J. , vol.9 , pp. 653-661
    • Conzelmann, A.1    Fankhauser, C.2    Desponds, C.3
  • 9
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
    • Cosson, P., and Letourneur, F. (1994). Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 263, 1629-1631.
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 10
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • Crowley, K.S., Liao, S., Worrell, V.E., Reinhart, G.D., and Johnson, A.E. (1994). Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell 78, 461-471.
    • (1994) Cell , vol.78 , pp. 461-471
    • Crowley, K.S.1    Liao, S.2    Worrell, V.E.3    Reinhart, G.D.4    Johnson, A.E.5
  • 11
    • 0016739154 scopus 로고
    • Inositol-requiring mutants of Saccharomyces cerevisiae
    • Culbertson, M.R., and Henry, S.A. (1975). Inositol-requiring mutants of Saccharomyces cerevisiae. Genetics 80, 23-40.
    • (1975) Genetics , vol.80 , pp. 23-40
    • Culbertson, M.R.1    Henry, S.A.2
  • 12
  • 13
    • 0342995731 scopus 로고    scopus 로고
    • The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process
    • Do, H., Fakone, D., Lin, J., Andrews, D.W., and Johnson, A.E. (1996). The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process. Cell 85, 369-378.
    • (1996) Cell , vol.85 , pp. 369-378
    • Do, H.1    Fakone, D.2    Lin, J.3    Andrews, D.W.4    Johnson, A.E.5
  • 14
    • 0030069907 scopus 로고    scopus 로고
    • GPI anchor attachment is required for Gas1p transport from the endoplasmic reticulum in COP II vesicles
    • Doering, T.L., and Schekman, R. (1996). GPI anchor attachment is required for Gas1p transport from the endoplasmic reticulum in COP II vesicles. EMBO J. 15, 182-191.
    • (1996) EMBO J. , vol.15 , pp. 182-191
    • Doering, T.L.1    Schekman, R.2
  • 15
    • 0027294030 scopus 로고
    • The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors
    • Englund, P.T. (1993). The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors. Annu. Rev. Biochem. 62, 121-138.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 121-138
    • Englund, P.T.1
  • 16
    • 0026065711 scopus 로고
    • Purification, biosynthesis and cellular localization of a major 125-kDA glycophosphatidylinositol-anchored membrane glycoprotein of Saccharomyces cerevisiae
    • Fankhauser, C., and Conzelmann, A. (1991). Purification, biosynthesis and cellular localization of a major 125-kDa glycophosphatidylinositol-anchored membrane glycoprotein of Saccharomyces cerevisiae. Eur. J. Biochem. 195, 439-448.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 439-448
    • Fankhauser, C.1    Conzelmann, A.2
  • 17
    • 0029796074 scopus 로고    scopus 로고
    • Bimodal interaction of coatomer with the p24 family of putative cargo receptors
    • Fiedler, K., Veit, M., Stamnes, M.A., and Rothman, J.E. (1996). Bimodal interaction of coatomer with the p24 family of putative cargo receptors. Science 273, 1396-1399.
    • (1996) Science , vol.273 , pp. 1396-1399
    • Fiedler, K.1    Veit, M.2    Stamnes, M.A.3    Rothman, J.E.4
  • 18
    • 0024004720 scopus 로고
    • Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method
    • Field, J., Nikawa, J., Broek, D., MacDonald, B., Rodgers, L., Wilson, I.A., Lerner, R.A., and Wigler, M. (1988). Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method. J. Mol. Biol. 8, 2159-2165.
    • (1988) J. Mol. Biol. , vol.8 , pp. 2159-2165
    • Field, J.1    Nikawa, J.2    Broek, D.3    MacDonald, B.4    Rodgers, L.5    Wilson, I.A.6    Lerner, R.A.7    Wigler, M.8
  • 19
    • 0029142888 scopus 로고
    • Inhibition of sphingolipid synthesis: Effects on glycosphingolipid-GPI-anchored protein microdomains
    • Futerman, A.H. (1995). Inhibition of sphingolipid synthesis: effects on glycosphingolipid-GPI-anchored protein microdomains. Trends Cell Biol. 5, 377-378.
    • (1995) Trends Cell Biol. , vol.5 , pp. 377-378
    • Futerman, A.H.1
  • 20
    • 0026504192 scopus 로고
    • A protein of the endoplasmic reticulum involved early in polypeptide translocation
    • Görlich, D., Hartmann, E., Prehn, S., and Rapoport, T.A. (1992). A protein of the endoplasmic reticulum involved early in polypeptide translocation. Nature 357, 47-52.
    • (1992) Nature , vol.357 , pp. 47-52
    • Görlich, D.1    Hartmann, E.2    Prehn, S.3    Rapoport, T.A.4
  • 21
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • Görlich, D., and Rapoport, T.A. (1993). Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75, 615-630.
    • (1993) Cell , vol.75 , pp. 615-630
    • Görlich, D.1    Rapoport, T.A.2
  • 22
    • 0028940341 scopus 로고
    • Yeast Gaa1p is required for attachment of a completed GPI anchor onto proteins
    • Hamburger, D., Egerton, M., and Riezman, H. (1995). Yeast Gaa1p is required for attachment of a completed GPI anchor onto proteins. J. Cell Biol. 129, 629-639.
    • (1995) J. Cell Biol. , vol.129 , pp. 629-639
    • Hamburger, D.1    Egerton, M.2    Riezman, H.3
  • 23
    • 0025949923 scopus 로고
    • The signal recognition particle in S. cerevisiae
    • Hann, B.C., and Walter, P. (1991). The signal recognition particle in S. cerevisiae. Cell 67, 131-144.
    • (1991) Cell , vol.67 , pp. 131-144
    • Hann, B.C.1    Walter, P.2
  • 24
    • 0032489505 scopus 로고    scopus 로고
    • TRAM regulates the exposure of nascent secretory proteins to the cytosol during translocation into the endoplasmic reticulum
    • Hegde, R.S., and Lingappa, V.R. (1998). TRAM regulates the exposure of nascent secretory proteins to the cytosol during translocation into the endoplasmic reticulum. Cell 92, 621-631.
    • (1998) Cell , vol.92 , pp. 621-631
    • Hegde, R.S.1    Lingappa, V.R.2
  • 25
    • 0027454264 scopus 로고
    • Site-specific photocross-linking reveals that Sec61p and TRAM contact different regions of a membrane-inserted signal sequence
    • High, S., et al. (1993). Site-specific photocross-linking reveals that Sec61p and TRAM contact different regions of a membrane-inserted signal sequence. J. Biol. Chem. 268, 26745-26751.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26745-26751
    • High, S.1
  • 26
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning proteins segments
    • Hofmann, K., and Stoffel, W. (1993). TMbase - a database of membrane spanning proteins segments. Biol. Chem. 347, 166.
    • (1993) Biol. Chem. , vol.347 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 27
    • 0028142838 scopus 로고
    • Ceramide synthesis enhances transport of GPI-anchored proteins to the Golgi apparatus in yeast
    • Horvath, A., Sütterlin, C., Manning-Krieg, U., Movva, N.R., and Riezman, H. (1994). Ceramide synthesis enhances transport of GPI-anchored proteins to the Golgi apparatus in yeast. EMBO J. 13, 3687-3695.
    • (1994) EMBO J. , vol.13 , pp. 3687-3695
    • Horvath, A.1    Sütterlin, C.2    Manning-Krieg, U.3    Movva, N.R.4    Riezman, H.5
  • 28
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K., and Kimura, A. (1983). Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 353, 163-168.
    • (1983) J. Bacteriol. , vol.353 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 29
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • 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.
    • (1990) EMBO J. , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 30
    • 0029096050 scopus 로고
    • A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane
    • Jungnickel, B., and Rapoport, T.A. (1995). A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane. Cell 82, 261-270.
    • (1995) Cell , vol.82 , pp. 261-270
    • Jungnickel, B.1    Rapoport, T.A.2
  • 31
    • 0025277750 scopus 로고
    • Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway
    • Kaiser, C.A., and Schekman, R. (1990). Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway. Cell 61, 723-733.
    • (1990) Cell , vol.61 , pp. 723-733
    • Kaiser, C.A.1    Schekman, R.2
  • 32
    • 0024447838 scopus 로고
    • Membrane protein sorting: Biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase
    • Klionski, D.J., and Emr, S.D. (1989). Membrane protein sorting: biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase. EMBO J. 8, 2241-2250.
    • (1989) EMBO J. , vol.8 , pp. 2241-2250
    • Klionski, D.J.1    Emr, S.D.2
  • 33
    • 0027981822 scopus 로고
    • Review: Cell wall assembly in yeast
    • Klis, F.M. (1994). Review: cell wall assembly in yeast. Yeast 10, 851-869.
    • (1994) Yeast , vol.10 , pp. 851-869
    • Klis, F.M.1
  • 34
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R.F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 35
    • 0025778531 scopus 로고
    • Expression of growth/differentiation factor 1 in the nervous system: Conservation of a bicistronic structure
    • Lee, S.J. (1991). Expression of growth/differentiation factor 1 in the nervous system: conservation of a bicistronic structure. Proc. Natl. Acad. Sci. USA 88, 4250-4254.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4250-4254
    • Lee, S.J.1
  • 36
    • 0028361106 scopus 로고
    • A conditionally lethal yeast mutant blocked at the first step in glycosylphosphatidylinositol anchor synthesis
    • Leidich, S.D., Drapp, D.A., and Orlean, P. (1994). A conditionally lethal yeast mutant blocked at the first step in glycosylphosphatidylinositol anchor synthesis. J. Biol. Chem. 269, 10193-10196.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10193-10196
    • Leidich, S.D.1    Drapp, D.A.2    Orlean, P.3
  • 37
    • 0028998118 scopus 로고
    • Temperature-sensitive yeast GPI anchoring mutants gpi2 and gpi3 are defective in the synthesis of N-acetylglucosaminyl phosphatidylinositol. Cloning of the GPI2 gene
    • Leidich, S.D., Kostova, Z., Latek, R.R., Costello, L.C., Drapp, D.A., Gray, W., Fassler, J.S., and Orlean, P. (1995). Temperature-sensitive yeast GPI anchoring mutants gpi2 and gpi3 are defective in the synthesis of N-acetylglucosaminyl phosphatidylinositol. Cloning of the GPI2 gene. J. Biol. Chem. 270, 13029-13035.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13029-13035
    • Leidich, S.D.1    Kostova, Z.2    Latek, R.R.3    Costello, L.C.4    Drapp, D.A.5    Gray, W.6    Fassler, J.S.7    Orlean, P.8
  • 39
    • 0026511056 scopus 로고
    • Mutants in the S. cerevisiae PKC1 gene display a cell cycle-specific osmotic stability defect
    • Levin, D.E., and Bartlett-Heubusch, E. (1992). Mutants in the S. cerevisiae PKC1 gene display a cell cycle-specific osmotic stability defect. J. Cell Biol. 116, 1221-1229.
    • (1992) J. Cell Biol. , vol.116 , pp. 1221-1229
    • Levin, D.E.1    Bartlett-Heubusch, E.2
  • 40
    • 0029932226 scopus 로고    scopus 로고
    • SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum
    • Lewis, M.J., and Pelham, H.R. (1996). SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum. Cell 85, 205-215.
    • (1996) Cell , vol.85 , pp. 205-215
    • Lewis, M.J.1    Pelham, H.R.2
  • 41
    • 0028909365 scopus 로고
    • Glycosyl phosphatidylinositol-dependent cross-linking of α-agglutinin and β 1,6-glucan in the Saccharomyces cerevisiae cell wall
    • Lu, C.F., Montijn, R.C., Brown, J.L., Klis, F., Kurjan, J., Bussey, H., and Lipke, P.N. (1995). Glycosyl phosphatidylinositol-dependent cross-linking of α-agglutinin and β 1,6-glucan in the Saccharomyces cerevisiae cell wall. J. Cell Biol. 128, 333-340.
    • (1995) J. Cell Biol. , vol.128 , pp. 333-340
    • Lu, C.F.1    Montijn, R.C.2    Brown, J.L.3    Klis, F.4    Kurjan, J.5    Bussey, H.6    Lipke, P.N.7
  • 42
    • 0027936633 scopus 로고
    • Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane
    • Mothes, W., Prehn, S., and Rapoport, T.A. (1994). Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane. EMBO J. 13, 3973-3982.
    • (1994) EMBO J. , vol.13 , pp. 3973-3982
    • Mothes, W.1    Prehn, S.2    Rapoport, T.A.3
  • 43
    • 0029952547 scopus 로고    scopus 로고
    • Signal sequences specify the targeting route to the endoplasmic reticulum membrane
    • Ng, D.T.W., Brown, J.D., and Walter, P. (1996). Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J. Cell Biol. 134, 269-278.
    • (1996) J. Cell Biol. , vol.134 , pp. 269-278
    • Ng, D.T.W.1    Brown, J.D.2    Walter, P.3
  • 44
    • 12444276104 scopus 로고
    • Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1
    • Nomura, N., Nagase, T., Miyajima, N., Sazuka, T., Tanaka, A., Sato, S., Seki, N., Kawarabayasi, Y., Ishikawa, K., and Tabata, S. (1994). Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1, 223-229.
    • (1994) DNA Res , vol.1 , pp. 223-229
    • Nomura, N.1    Nagase, T.2    Miyajima, N.3    Sazuka, T.4    Tanaka, A.5    Sato, S.6    Seki, N.7    Kawarabayasi, Y.8    Ishikawa, K.9    Tabata, S.10
  • 45
    • 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
  • 46
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for posttranslational events in the yeast secretory pathway
    • Novick, P., Field, C., and Schekman, R. (1980). Identification of 23 complementation groups required for posttranslational events in the yeast secretory pathway. Cell 21, 205-215.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 47
    • 0027270310 scopus 로고
    • Analysis of the sequence requirements for glycosylphosphatidylinositol anchoring of Saccharomyces cerevisiae Gas1 protein
    • Nuoffer, C., Horvath, A., and Riezman, H. (1993). Analysis of the sequence requirements for glycosylphosphatidylinositol anchoring of Saccharomyces cerevisiae Gas1 protein. J. Biol. Chem. 268, 10558-10563.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10558-10563
    • Nuoffer, C.1    Horvath, A.2    Riezman, H.3
  • 48
    • 0026057813 scopus 로고
    • Determinants for glycophospholipid anchoring of the Saccharomyces cerevisiae GAS1 protein to the plasma membrane
    • Nuoffer, C., Jenö, P., Conzelmann, A., and Riezman, H. (1991). Determinants for glycophospholipid anchoring of the Saccharomyces cerevisiae GAS1 protein to the plasma membrane. Mol. Cell. Biol. 11, 27-37.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 27-37
    • Nuoffer, C.1    Jenö, P.2    Conzelmann, A.3    Riezman, H.4
  • 49
    • 0028279520 scopus 로고
    • Prediction of transmembrane segments in proteins utilizing multiple sequence alignments
    • Persson, B., and Argos, P. (1994). Prediction of transmembrane segments in proteins utilizing multiple sequence alignments. J. Mol. Biol. 237, 182-192.
    • (1994) J. Mol. Biol. , vol.237 , pp. 182-192
    • Persson, B.1    Argos, P.2
  • 51
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport, T.A., Jungnickel, B., and Kutay, U. (1996). Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65, 271-303.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 52
    • 0028824577 scopus 로고
    • Yeast Kre1p is a cell surface O-glycoprotein
    • Roemer, T., and Bussey, H. (1995). Yeast Kre1p is a cell surface O-glycoprotein. Mol. Gen. Genet. 249, 209-216.
    • (1995) Mol. Gen. Genet. , vol.249 , pp. 209-216
    • Roemer, T.1    Bussey, H.2
  • 54
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., and Orci, L. (1996). Coat proteins and vesicle budding. Science 271, 1526-1533.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 55
    • 0028964475 scopus 로고
    • The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi
    • 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.
    • (1995) EMBO J. , vol.14 , pp. 1329-1339
    • Schimmöller, F.1    Singer-Krüger, B.2    Schröder, S.3    Krüger, U.4    Barlowe, C.5    Riezman, H.6
  • 56
    • 0029025250 scopus 로고
    • The yeast SPT14 gene is homologous to the human PIG-A gene and is required for GPI anchor synthesis
    • Schönbächler, M., Horvath, A., Fassler, J., and Riezman, H. (1995). The yeast SPT14 gene is homologous to the human PIG-A gene and is required for GPI anchor synthesis. EMBO J. 14, 1637-1645.
    • (1995) EMBO J. , vol.14 , pp. 1637-1645
    • Schönbächler, M.1    Horvath, A.2    Fassler, J.3    Riezman, H.4
  • 57
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. (1991). Getting started with yeast. Methods Enzymol. 194, 3-21.
    • (1991) Methods Enzymol , vol.194 , pp. 3-21
    • Sherman, F.1
  • 58
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • 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.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 59
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon, S.M., and Blobel, G. (1991). A protein-conducting channel in the endoplasmic reticulum. Cell 65, 371-380.
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 60
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons, K., and van Meer, G. (1988). Lipid sorting in epithelial cells. Biochemistry 27, 6197-6202.
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 61
    • 0031038655 scopus 로고    scopus 로고
    • Suppressor gene analysis reveals an essential role for sphingolipids in transport of glycosylphosphatidylinositol-anchored proteins in Saccharomyces cerevisiae
    • Skrzypek, M., Lester, R.L., and Dickson, R.C. (1997). Suppressor gene analysis reveals an essential role for sphingolipids in transport of glycosylphosphatidylinositol-anchored proteins in Saccharomyces cerevisiae. J. Bacteriol. 179, 1513-1520.
    • (1997) J. Bacteriol. , vol.179 , pp. 1513-1520
    • Skrzypek, M.1    Lester, R.L.2    Dickson, R.C.3
  • 63
    • 0020181690 scopus 로고
    • Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole
    • Stevens, T., Esmon, B., and Schekman, R. (1982). Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole. Cell 30, 439-448.
    • (1982) Cell , vol.30 , pp. 439-448
    • Stevens, T.1    Esmon, B.2    Schekman, R.3
  • 64
    • 0025201631 scopus 로고
    • The ADE2 gene from Saccharomyces cerevisiae: Sequence and new vectors
    • Stotz, A., and Linder, P. (1990). The ADE2 gene from Saccharomyces cerevisiae: sequence and new vectors. Gene 95, 91-98.
    • (1990) Gene , vol.95 , pp. 91-98
    • Stotz, A.1    Linder, P.2
  • 65
    • 0030665269 scopus 로고    scopus 로고
    • Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast
    • Sütterlin, C., Doering, T.L., Schimmöller, F., Schröder, S., and Riezman, H. (1997). Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast. J. Cell Sci. 110, 2703-2714.
    • (1997) J. Cell Sci. , vol.110 , pp. 2703-2714
    • Sütterlin, C.1    Doering, T.L.2    Schimmöller, F.3    Schröder, S.4    Riezman, H.5
  • 67
    • 0029951178 scopus 로고    scopus 로고
    • Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane
    • Voigt, S., Jungnickel, B., Hartmann, E., and Rapoport, T.A. (1996). Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane. J. Cell Biol. 134, 25-35.
    • (1996) J. Cell Biol. , vol.134 , pp. 25-35
    • Voigt, S.1    Jungnickel, B.2    Hartmann, E.3    Rapoport, T.A.4
  • 68
    • 0026716643 scopus 로고
    • Membrane protein structure prediction, hydrophobicity analysis and the positive-inside rule
    • von Heijne, G. (1992). Membrane protein structure prediction, hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225, 487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 69
    • 0031003650 scopus 로고    scopus 로고
    • Restrictive glycosylphosphatidylinositol anchor synthesis in cwh6/gpi3 yeast cells causes aberrant biogenesis of cell wall proteins
    • Vossen, J.H., Müller, W.H., Lipke, P.N., and Klis, F.M. (1997). Restrictive glycosylphosphatidylinositol anchor synthesis in cwh6/gpi3 yeast cells causes aberrant biogenesis of cell wall proteins. J. Bacteriol. 179, 2202-2209.
    • (1997) J. Bacteriol. , vol.179 , pp. 2202-2209
    • Vossen, J.H.1    Müller, W.H.2    Lipke, P.N.3    Klis, F.M.4
  • 70
    • 0028915532 scopus 로고
    • Identification of SPT14/CWH6 as the yeast homologue of hPIG-A, a gene involved in the biosynthesis of GPI anchors
    • Vossen, J.H., Ram, A.F., and Klis, F.M. (1995). Identification of SPT14/CWH6 as the yeast homologue of hPIG-A, a gene involved in the biosynthesis of GPI anchors. Biochim. Biophys. Acta 1243, 549-551.
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 549-551
    • Vossen, J.H.1    Ram, A.F.2    Klis, F.M.3
  • 71
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter, P., and Johnson, A.E. (1994). Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10, 87-119.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 72
    • 0027499606 scopus 로고
    • Cell surface anchorage and ligand-binding domains of the Saccharomyces cerevisiae cell adhesion protein α-agglutinin, a member of the Ig superfamily
    • Wojciechowicz, D., Lu, C.F., Kurjan, J., and Lipke, P.N. (1993). Cell surface anchorage and ligand-binding domains of the Saccharomyces cerevisiae cell adhesion protein α-agglutinin, a member of the Ig superfamily. Mol. Cell. Biol. 13, 2554-2563.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2554-2563
    • Wojciechowicz, D.1    Lu, C.F.2    Kurjan, J.3    Lipke, P.N.4


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