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Volumn 134, Issue 2, 1996, Pages 279-293

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

Author keywords

[No Author keywords available]

Indexed keywords

MANNOSE; MEMBRANE PROTEIN;

EID: 0029953563     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.134.2.279     Document Type: Article
Times cited : (131)

References (50)
  • 1
    • 23444432144 scopus 로고
    • Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum
    • Balch, W.E., J.M. McCaffery, H. Plutner, and M.G. Farquhar. 1994. Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum. Cell. 76:841-852.
    • (1994) Cell , vol.76 , pp. 841-852
    • Balch, W.E.1    McCaffery, J.M.2    Plutner, H.3    Farquhar, M.G.4
  • 2
    • 0027500969 scopus 로고
    • SEC12 encodes a guanine nucleotide exchange factor essential for transport vesicle budding from the ER
    • Barlowe, C., and R. Schekman. 1993. SEC12 encodes a guanine nucleotide exchange factor essential for transport vesicle budding from the ER. Nature (Lond.). 365:347-349.
    • (1993) Nature (Lond.) , vol.365 , pp. 347-349
    • Barlowe, C.1    Schekman, R.2
  • 4
    • 0027968228 scopus 로고
    • Kex2-dependent invertase secretion as a tool to study the targeting of transmembrane proteins which are involved in ER→Golgi transport in yeast
    • Boehm, J., H.D. Ulrich, R. Ossig, and H.D. Schmitt. 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 (Eur. Mol. Biol. Organ.) J. 13:3696-3710.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 3696-3710
    • Boehm, J.1    Ulrich, H.D.2    Ossig, R.3    Schmitt, H.D.4
  • 5
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher, M.S., and S. Munro. 1993. Cholesterol and the Golgi apparatus. Science. (Wash. DC). 261:1280-1281.
    • (1993) Science. (Wash. DC) , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 6
    • 0000182975 scopus 로고
    • XL1-blue: A high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection
    • Bullock, W.O., J.M. Fernandez, and J.M. Short. 1987. XL1-blue: a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. Biotechniques. 5:376.
    • (1987) Biotechniques , vol.5 , pp. 376
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 7
    • 0028181745 scopus 로고
    • Coatomer interaction with dilysine endoplasmic reticulum retention motifs
    • Cosson, P., and F. Letourneur. 1994. Coatomer interaction with dilysine endoplasmic reticulum retention motifs. Science (Wash. DC). 263:1629-1631.
    • (1994) Science (Wash. DC) , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 8
    • 0025362658 scopus 로고
    • Recycling of proteins from the Golgi compartment to the ER in yeast
    • Dean, N., and H.R.B. Pelham. 1990. Recycling of proteins from the Golgi compartment to the ER in yeast. J. Cell Biol. 111:369-377.
    • (1990) J. Cell Biol. , vol.111 , pp. 369-377
    • Dean, N.1    Pelham, H.R.B.2
  • 9
    • 0025941558 scopus 로고
    • Structural and functional dissection of a membrane glycoprotein required for vesicle budding from the endoplasmic reticulum
    • d'Enfert, C., C. Barlowe, S. Nishikawa, A. Nakano, and R. Schekman. 1991. Structural and functional dissection of a membrane glycoprotein required for vesicle budding from the endoplasmic reticulum. Mol. Cell. Biol. 11: 5727-5734.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5727-5734
    • D'Enfert, C.1    Barlowe, C.2    Nishikawa, S.3    Nakano, A.4    Schekman, R.5
  • 10
    • 0028029829 scopus 로고
    • Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast
    • Gaynor, E.C., S. te Heesen, T.R. Graham, M. Aebi, and S.D. Emr. 1994. Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast. J. Cell Biol. 127:653-665.
    • (1994) J. Cell Biol. , vol.127 , pp. 653-665
    • Gaynor, E.C.1    Te Heesen, S.2    Graham, T.R.3    Aebi, M.4    Emr, S.D.5
  • 11
    • 0028885714 scopus 로고
    • SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and participates in vesicle formation
    • Gimeno, R.E., P. Espenshade, and C. Kaiser. 1995. SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and participates in vesicle formation. J. Cell Biol. 131:325-338.
    • (1995) J. Cell Biol. , vol.131 , pp. 325-338
    • Gimeno, R.E.1    Espenshade, P.2    Kaiser, C.3
  • 12
    • 0028980860 scopus 로고
    • Sorting of α1,3-mannosyltransferase is mediated by a lumenal domain interaction, and a transmembrane domain signal that can confer clathrin-dependent Golgi localization to a secreted protein
    • Graham, T.R., and V.A. Krasnov. 1995. Sorting of α1,3-mannosyltransferase is mediated by a lumenal domain interaction, and a transmembrane domain signal that can confer clathrin-dependent Golgi localization to a secreted protein. Mol. Biol. Cell. 6:809-824.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 809-824
    • Graham, T.R.1    Krasnov, V.A.2
  • 13
    • 0028171094 scopus 로고
    • Clathrin-dependent localization of α1,3-mannosyltransferase to the Golgi complex of Saccharomyces cerevisiae
    • Graham, T.R., M. Seeger, G.S. Payne, V.L. MacKay, and S.D. Emr. 1994. Clathrin-dependent localization of α1,3-mannosyltransferase to the Golgi complex of Saccharomyces cerevisiae. J. Cell Biol. 127:667-678.
    • (1994) J. Cell Biol. , vol.127 , pp. 667-678
    • Graham, T.R.1    Seeger, M.2    Payne, G.S.3    MacKay, V.L.4    Emr, S.D.5
  • 15
    • 0025775723 scopus 로고
    • A recycling pathway between the endoplasmic reticulum and the Golgi apparatus for retention of unassembled MHC class I molecule
    • Hsu, V.W., L.C. Yuan, J.G. Nuchtern, J. Lippincott-Schwartz, G.J. Hammerling, and R.D. Klausner. 1991. A recycling pathway between the endoplasmic reticulum and the Golgi apparatus for retention of unassembled MHC class I molecule. Nature (Lond.). 352:441-444.
    • (1991) Nature (Lond.) , vol.352 , pp. 441-444
    • Hsu, V.W.1    Yuan, L.C.2    Nuchtern, J.G.3    Lippincott-Schwartz, J.4    Hammerling, G.J.5    Klausner, R.D.6
  • 16
    • 0029098968 scopus 로고
    • Targeting of protein ERGIG-53 to the ER/ERGIC/cis-Golgi recycling pathway
    • Itin, C., R. Schindler, and H.P. Hauri. 1995. Targeting of protein ERGIG-53 to the ER/ERGIC/cis-Golgi recycling pathway. J. Cell Biol. 131:57-67.
    • (1995) J. Cell Biol. , vol.131 , pp. 57-67
    • Itin, C.1    Schindler, R.2    Hauri, H.P.3
  • 17
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson, M.R., T. Nillson, and P.A. Peterson. 1990. Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO (Eur. Mol. Biol. Organ.) J. 9:3153-3162.
    • (1990) EMBO (Eur. Mol. Biol. Organ.) J. , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nillson, T.2    Peterson, P.A.3
  • 18
    • 0027538121 scopus 로고
    • Retrieval of transmembrane proteins to the endoplasmic reticulum
    • Jackson, M.R., T. Nillson, and P.A. Peterson. 1993. Retrieval of transmembrane proteins to the endoplasmic reticulum. J. Cell Biol. 121:317-333.
    • (1993) J. Cell Biol. , vol.121 , pp. 317-333
    • Jackson, M.R.1    Nillson, T.2    Peterson, P.A.3
  • 19
    • 0023832246 scopus 로고
    • A colony procedure for transformation of Saccharomyces cerevisiae
    • Keszenman-Pereyra, D., and K. Hieda. 1988. A colony procedure for transformation of Saccharomyces cerevisiae. Curr. Genet. 13:21-23.
    • (1988) Curr. Genet. , vol.13 , pp. 21-23
    • Keszenman-Pereyra, D.1    Hieda, K.2
  • 21
    • 0025187298 scopus 로고
    • A human homologue of the yeast HDEL receptor
    • Lewis, M.J., and H.R.B. Pelham. 1990. A human homologue of the yeast HDEL receptor. Nature (Lond.). 348:162-163.
    • (1990) Nature (Lond.) , vol.348 , pp. 162-163
    • Lewis, M.J.1    Pelham, H.R.B.2
  • 22
    • 0026604647 scopus 로고
    • Ligand induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum
    • Lewis, M.J., and H.R.B. Pelham. 1992. Ligand induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum. Cell. 68:353-364.
    • (1992) Cell , vol.68 , pp. 353-364
    • Lewis, M.J.1    Pelham, H.R.B.2
  • 23
    • 0023838784 scopus 로고
    • Transport of secretory and membrane glycoproteins from the rough endoplasmic reticulum to the Golgi. A rate-limiting step in protein maturation and secretion
    • Lodish, H.F. 1988. Transport of secretory and membrane glycoproteins from the rough endoplasmic reticulum to the Golgi. A rate-limiting step in protein maturation and secretion. J. Biol. Chem. 263:2107-2110.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2107-2110
    • Lodish, H.F.1
  • 24
    • 0027175236 scopus 로고
    • A soluble secretory protein is first concentrated in the endoplasmic reticulum before transfer to the Golgi apparatus
    • Mizuno, M., and S.J. Singer. 1993. A soluble secretory protein is first concentrated in the endoplasmic reticulum before transfer to the Golgi apparatus. Proc. Natl. Acad. Sci. USA. 90:5732-5736.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5732-5736
    • Mizuno, M.1    Singer, S.J.2
  • 25
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro, S., and H.R.B. Pelham. 1987. A C-terminal signal prevents secretion of luminal ER proteins. Cell. 48:899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.B.2
  • 26
    • 0029165107 scopus 로고
    • An investigation of the role of transmembrane domains in Golgi protein retention
    • Munro, S. 1995. An investigation of the role of transmembrane domains in Golgi protein retention. EMBO (Eur. Mol. Biol. Organ.) J. 14:4695-4704.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 4695-4704
    • Munro, S.1
  • 27
    • 0024807217 scopus 로고
    • A novel GTP-binding protein, SAR1, is involved in transport from the endoplasmic reticulum to the Golgi apparatus
    • Nakano, A., and M. Muramatsu. 1989. A novel GTP-binding protein, SAR1, is involved in transport from the endoplasmic reticulum to the Golgi apparatus. J. Cell Biol. 109:2677-2691.
    • (1989) J. Cell Biol. , vol.109 , pp. 2677-2691
    • Nakano, A.1    Muramatsu, M.2
  • 28
    • 0024075376 scopus 로고
    • A membrane glycoprotein, Sec12p, required for protein transport from the endoplasmic reticulum to the Golgi apparatus in yeast
    • Nakano, A., D. Brada, and R. Schekman. 1988. A membrane glycoprotein, Sec12p, required for protein transport from the endoplasmic reticulum to the Golgi apparatus in yeast. J. Cell Biol. 107:851-863.
    • (1988) J. Cell Biol. , vol.107 , pp. 851-863
    • Nakano, A.1    Brada, D.2    Schekman, R.3
  • 29
    • 0026749963 scopus 로고
    • OCHI encodes a novel membrane bound mannosyltransferase: Outer chain elongation of asparagine-linked oligosaccharides
    • Nakayama, K., T. Nagasu, Y. Shimma, J. Kuromitsu, and Y. Jigami. 1992. OCHI encodes a novel membrane bound mannosyltransferase: outer chain elongation of asparagine-linked oligosaccharides. EMBO (Eur. Mol. Biol. Organ.) J. 11:2511-2519.
    • (1992) EMBO (Eur. Mol. Biol. Organ.) J. , vol.11 , pp. 2511-2519
    • Nakayama, K.1    Nagasu, T.2    Shimma, Y.3    Kuromitsu, J.4    Jigami, Y.5
  • 31
    • 0025909492 scopus 로고
    • The GTP-binding Sar1 protein is localized to the early compartment of the yeast secretory pathway
    • Nishikawa, S., and A. Nakano. 1991. The GTP-binding Sar1 protein is localized to the early compartment of the yeast secretory pathway. Biochim. Biophys. Acta. 103:135-143.
    • (1991) Biochim. Biophys. Acta , vol.103 , pp. 135-143
    • Nishikawa, S.1    Nakano, A.2
  • 32
    • 0027198483 scopus 로고
    • Identification of a gene required for membrane protein retention in the early secretory pathway
    • Nishikawa, S., and A. Nakano. 1993. Identification of a gene required for membrane protein retention in the early secretory pathway. Proc. Natl. Acad. Sci. USA. 90:8179-8183.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8179-8183
    • Nishikawa, S.1    Nakano, A.2
  • 33
    • 0025346974 scopus 로고
    • Biogenesis of vacuolar membrane glycoproteins of yeast Saccharomyces cerevisiae
    • Nishikawa, S., N. Umemoto, Y. Ohsumi, A. Nakano, and Y. Anraku. 1990. Biogenesis of vacuolar membrane glycoproteins of yeast Saccharomyces cerevisiae. J. Biol. Chem. 265:7440-7448.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7440-7448
    • Nishikawa, S.1    Umemoto, N.2    Ohsumi, Y.3    Nakano, A.4    Anraku, Y.5
  • 34
    • 0028073895 scopus 로고
    • Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces relocalization of binding protein (BiP) within the ER to form the BiP bodies
    • Nishikawa, S., A. Hirata, and A. Nakano. 1994. Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces relocalization of binding protein (BiP) within the ER to form the BiP bodies. Mol. Biol. Cell. 5:1129-1143.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1129-1143
    • Nishikawa, S.1    Hirata, A.2    Nakano, A.3
  • 35
    • 0028089202 scopus 로고
    • Inhibition of GTP hydrolysis by Sarlp causes accumulation of vesicles that are a functional intermediate of the ER-to-Golgi transport in yeast
    • Oka, T., and A. Nakano. 1994. Inhibition of GTP hydrolysis by Sarlp causes accumulation of vesicles that are a functional intermediate of the ER-to-Golgi transport in yeast. J. Cell Biol. 124:425-434.
    • (1994) J. Cell Biol. , vol.124 , pp. 425-434
    • Oka, T.1    Nakano, A.2
  • 36
    • 0023988955 scopus 로고
    • Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment
    • Pelham, H.R.B. 1988. Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment. EMBO (Eur. Mol. Biol. Organ.) J. 7:913-918.
    • (1988) EMBO (Eur. Mol. Biol. Organ.) J. , vol.7 , pp. 913-918
    • Pelham, H.R.B.1
  • 38
    • 0026687986 scopus 로고
    • RHO gene products, putative small GTP-binding proteins, are important for activation of the CALI/CDC43 gene product, a protein geranylgeranyltransferase in Saccharomyces cerevisiae
    • Qadota, H., I. Ishii, A. Fujiyama, Y. Ohya, and Y. Anraku. 1992. RHO gene products, putative small GTP-binding proteins, are important for activation of the CALI/CDC43 gene product, a protein geranylgeranyltransferase in Saccharomyces cerevisiae. Yeast. 8:735-741.
    • (1992) Yeast , vol.8 , pp. 735-741
    • Qadota, H.1    Ishii, I.2    Fujiyama, A.3    Ohya, Y.4    Anraku, Y.5
  • 39
    • 0025775567 scopus 로고
    • Distinct biochemical requirements for the budding, targeting, and fusion of ER-derived transport vesicles
    • Rexach, M.F., and R. Schekman. 1991. Distinct biochemical requirements for the budding, targeting, and fusion of ER-derived transport vesicles. J. Cell Biol. 114:219-229.
    • (1991) J. Cell Biol. , vol.114 , pp. 219-229
    • Rexach, M.F.1    Schekman, R.2
  • 40
    • 0024653797 scopus 로고
    • Structure, biosynthesis, and localization of dipeptidyl aminopeptidase B, an integral membrane glycoprotein of the yeast vacuole
    • Roberts, C.J., G. Pohling, J.H. Royhman, and T.H. Stevens. 1989. Structure, biosynthesis, and localization of dipeptidyl aminopeptidase B, an integral membrane glycoprotein of the yeast vacuole. J. Cell Biol. 108:1363-1373.
    • (1989) J. Cell Biol. , vol.108 , pp. 1363-1373
    • Roberts, C.J.1    Pohling, G.2    Royhman, J.H.3    Stevens, T.H.4
  • 41
    • 0026727566 scopus 로고
    • Membrane protein sorting in the yeast secretory pathway: Evidence that the vacuole may be the default compartment
    • Roberts, C.J., F.N. Stevens, and T.H. Stevens. 1992. Membrane protein sorting in the yeast secretory pathway: evidence that the vacuole may be the default compartment. J. Cell Biol. 119:69-83.
    • (1992) J. Cell Biol. , vol.119 , pp. 69-83
    • Roberts, C.J.1    Stevens, F.N.2    Stevens, T.H.3
  • 43
    • 0028857987 scopus 로고
    • Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): Characterization of the RERI gene products as a component involved in ER localization of Sec12p
    • Sato, K., S. Nishikawa, and A. Nakano. 1995. Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RERI gene products as a component involved in ER localization of Sec12p. Mol. Biol. Cell. 6:1459-1477.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1459-1477
    • Sato, K.1    Nishikawa, S.2    Nakano, A.3
  • 44
  • 45
    • 0025362445 scopus 로고
    • ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway
    • Semenza, J.C., K.G. Hardwick, N. Dean, and H.R.B. Pelham. 1990. ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell. 61:1349-1357.
    • (1990) Cell , vol.61 , pp. 1349-1357
    • Semenza, J.C.1    Hardwick, K.G.2    Dean, N.3    Pelham, H.R.B.4
  • 46
    • 0026542540 scopus 로고
    • The Saccharomyces cerevisiae SEC20 gene encodes a membrane glycoprotein which is sorted by the HDEL retrieval system
    • Sweet, D.J., and H.R.B. Pelham. 1992. The Saccharomyces cerevisiae SEC20 gene encodes a membrane glycoprotein which is sorted by the HDEL retrieval system. EMBO (Eur. Mol. Biol. Organ.) J. 11:423-432.
    • (1992) EMBO (Eur. Mol. Biol. Organ.) J. , vol.11 , pp. 423-432
    • Sweet, D.J.1    Pelham, H.R.B.2
  • 47
    • 0025940737 scopus 로고
    • A Golgi retention signal in a membrane-spanning domain of coronavirus E1 protein
    • Swift, A.M., and C.E. Machamer. 1991. A Golgi retention signal in a membrane-spanning domain of coronavirus E1 protein. J. Cell Biol. 115:19-30.
    • (1991) J. Cell Biol. , vol.115 , pp. 19-30
    • Swift, A.M.1    Machamer, C.E.2
  • 48
    • 0028885696 scopus 로고
    • 2-terminal transmembrane domains of cytochrome P450 contain independent signals for retention in the endoplasmic reticulum
    • 2-terminal transmembrane domains of cytochrome P450 contain independent signals for retention in the endoplasmic reticulum. J. Biol. Chem. 270:24327-24333.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24327-24333
    • Szczesna-Skorupa, E.1    Ahn, K.2    Chen, C.3    Balraj, D.4    Kemper, B.5
  • 49
    • 0027248612 scopus 로고
    • Oligomerization of a membrane protein correlates with its retention in the Golgi complex
    • Weisz, O.A., A.M. Swift, and C.E. Machamer. 1993. Oligomerization of a membrane protein correlates with its retention in the Golgi complex. J. Cell Biol. 122:1185-1196.
    • (1993) J. Cell Biol. , vol.122 , pp. 1185-1196
    • Weisz, O.A.1    Swift, A.M.2    Machamer, C.E.3
  • 50
    • 0025483121 scopus 로고
    • Chromosome III of Saccharomyces cerevisiae: An ordered clone bank, a detailed restriction map and analysis of transcripts suggest the presence of 160 genes
    • Yoshikawa, A., and K. Isono. 1990. Chromosome III of Saccharomyces cerevisiae: an ordered clone bank, a detailed restriction map and analysis of transcripts suggest the presence of 160 genes. Yeast. 6:383-401.
    • (1990) Yeast , vol.6 , pp. 383-401
    • Yoshikawa, A.1    Isono, K.2


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