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Volumn 132, Issue 4, 1996, Pages 499-509

ER membrane protein complex required for nuclear fusion

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 0030051440     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.132.4.499     Document Type: Article
Times cited : (77)

References (44)
  • 1
    • 0029084786 scopus 로고
    • The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events
    • Acharya, U., R Jacobs, J.-M. Peters, N. Watson, M.G. Farquar, and V. Malhotra. 1995. The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events. Cell. 82:895-904
    • (1995) Cell. , vol.82 , pp. 895-904
    • Acharya, U.1    Jacobs, R.2    Peters, J.-M.3    Watson, N.4    Farquar, M.G.5    Malhotra, V.6
  • 2
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel, C.P., T.G. Wolfsberg, C.W. Turck, D.G Myles, P. Primakoff, and J M White. 1992 A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion Nature (Lond.). 356:248-252.
    • (1992) Nature (Lond.) , vol.356 , pp. 248-252
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 3
    • 0027759380 scopus 로고
    • A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome
    • Brodsky, J.L., and R. Schekman. 1993. A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J. Cell Biol. 123:1355-1363.
    • (1993) J. Cell Biol. , vol.123 , pp. 1355-1363
    • Brodsky, J.L.1    Schekman, R.2
  • 5
    • 0001301433 scopus 로고
    • A mutant of Saccharomyces cerevisiae defective for nuclear fusion
    • Conde, J., and G.R. Fink. 1976. A mutant of Saccharomyces cerevisiae defective for nuclear fusion. Proc Natl Acad. Sci USA. 73:3651-3655.
    • (1976) Proc Natl Acad. Sci USA , vol.73 , pp. 3651-3655
    • Conde, J.1    Fink, G.R.2
  • 6
    • 0028353336 scopus 로고
    • DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70
    • Cyr, D M , T. Langer, and M.G. Douglas. 1994 DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci. 19:176-181.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 176-181
    • Cyr, D.M.1    Langer, T.2    Douglas, M.G.3
  • 7
    • 0023567026 scopus 로고
    • A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum
    • Deshaies, R.J , and R. Schekman. 1987. A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum. J. Cell Biol 105.633-645.
    • (1987) J. Cell Biol , vol.105 , pp. 633-645
    • Deshaies, R.J.1    Schekman, R.2
  • 8
    • 0024828302 scopus 로고
    • SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum
    • Deshaies, R.J., and R. Schekman 1989. SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum. J. Cell Biol 109:2653-2664.
    • (1989) J. Cell Biol , vol.109 , pp. 2653-2664
    • Deshaies, R.J.1    Schekman, R.2
  • 9
    • 0025970051 scopus 로고
    • Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex
    • Deshaies, R.J., S.L. Sanders, D.A. Feldheim, and R. Schekman. 1991. Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex. Nature (Lond.) 349 806-808.
    • (1991) Nature (Lond.) , vol.349 , pp. 806-808
    • Deshaies, R.J.1    Sanders, S.L.2    Feldheim, D.A.3    Schekman, R.4
  • 10
    • 0028022701 scopus 로고
    • Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex
    • Feldheim, D., and R. Schekman. 1994. Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex. J. Cell Biol. 126:935-943.
    • (1994) J. Cell Biol. , vol.126 , pp. 935-943
    • Feldheim, D.1    Schekman, R.2
  • 11
    • 0026690820 scopus 로고
    • Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation
    • Feldheim, D., J Rothblatt, and R. Schekman. 1992. Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation. Mol. Cell. Biol. 12:3288-3296
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3288-3296
    • Feldheim, D.1    Rothblatt, J.2    Schekman, R.3
  • 12
    • 0027507707 scopus 로고
    • Structural and functional characterization of Sec66p, a new subunit of the polypeptide translocation apparatus in the yeast endoplasmic reticulum
    • Feldheim, D., K. Yoshimura, A Admon, and R Schekman 1993. Structural and functional characterization of Sec66p, a new subunit of the polypeptide translocation apparatus in the yeast endoplasmic reticulum. Mol. Biol. Cell. 4:931-939.
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 931-939
    • Feldheim, D.1    Yoshimura, K.2    Admon, A.3    Schekman, R.4
  • 13
  • 14
    • 0026531641 scopus 로고
    • Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae
    • Green, N., H. Fang, and P. Walter. 1992. Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae. J. Cell Biol. 116:597-604.
    • (1992) J. Cell Biol. , vol.116 , pp. 597-604
    • Green, N.1    Fang, H.2    Walter, P.3
  • 15
    • 84920293356 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 16
    • 0025949923 scopus 로고
    • The signal recognition particle in S. cerevisiae
    • Hann, B.C , and P Walter. 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
  • 17
    • 0023794908 scopus 로고
    • Diverse effects of β-tubulin mutations of microtubule formation and function
    • Huffaker, T.C., J.H. Thomas, and D. Botstein. 1988 Diverse effects of β-tubulin mutations of microtubule formation and function. J Cell Biol. 106:1997-2010.
    • (1988) J Cell Biol. , vol.106 , pp. 1997-2010
    • Huffaker, T.C.1    Thomas, J.H.2    Botstein, D.3
  • 18
    • 0027964421 scopus 로고
    • Nuclear congression and membrane fusion: Two distinct events in the yeast karyogamy pathway
    • Kurihara, L.J., C.T. Beh, M. Latterich, R. Schekman, and M D. Rose 1994. Nuclear congression and membrane fusion: two distinct events in the yeast karyogamy pathway. J. Cell Biol. 126:911-923
    • (1994) J. Cell Biol. , vol.126 , pp. 911-923
    • Kurihara, L.J.1    Beh, C.T.2    Latterich, M.3    Schekman, R.4    Rose, M.D.5
  • 19
    • 0027425837 scopus 로고
    • Suppression of a sec63 mutation identifies a novel component of the yeast endoplasmic reticulum translocation apparatus
    • Kurihara, T., and P. Silver. 1993. Suppression of a sec63 mutation identifies a novel component of the yeast endoplasmic reticulum translocation apparatus. Mol. Cell Biol. 4:919-930.
    • (1993) Mol. Cell Biol. , vol.4 , pp. 919-930
    • Kurihara, T.1    Silver, P.2
  • 20
    • 0028365624 scopus 로고
    • The karyogamy gene KAR2 and novel proteins are required for ER-membrane fusion
    • Latterich, M , and R. Schekman. 1994. The karyogamy gene KAR2 and novel proteins are required for ER-membrane fusion. Cell. 78:87-98.
    • (1994) Cell. , vol.78 , pp. 87-98
    • Latterich, M.1    Schekman, R.2
  • 21
    • 0029122698 scopus 로고
    • Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes
    • Latterich, M., K.-U Fröhlich, and R. Schekman. 1995 Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes. Cell. 82.885-893.
    • (1995) Cell. , vol.82 , pp. 885-893
    • Latterich, M.1    Fröhlich, K.-U.2    Schekman, R.3
  • 22
    • 0027230956 scopus 로고
    • Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae
    • Nelson, M.K., T Kurihara, and P.A. Silver. 1993. Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae. Genetics 134:159-173.
    • (1993) Genetics , vol.134 , pp. 159-173
    • Nelson, M.K.1    Kurihara, T.2    Silver, P.A.3
  • 23
    • 0024395160 scopus 로고
    • S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP
    • Normington, K., K Kohno, Y. Kozutsumi, M.J. Gething, and J. Sambrook. 1989. S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell. 57:1223-12236.
    • (1989) Cell. , vol.57 , pp. 1223-12236
    • Normington, K.1    Kohno, K.2    Kozutsumi, Y.3    Gething, M.J.4    Sambrook, J.5
  • 24
    • 0026057813 scopus 로고
    • Determinants for glycophospholipid anchoring of the Saccharomyces cerevisiae GAS1 protein to the plasma membrane
    • Nuoffer, C., P. Jeno, A. Conzelmann, and H. Riezman 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    Jeno, P.2    Conzelmann, A.3    Riezman, H.4
  • 25
    • 0028158129 scopus 로고
    • Localization of the Kar3 kinesin heavy chain-related protein requires the Cik1 interacting protein
    • Page, B.D., L.L. Satterwhite, M.D. Rose, and M. Snyder. 1994. Localization of the Kar3 kinesin heavy chain-related protein requires the Cik1 interacting protein. J. Cell Biol. 124:507-519.
    • (1994) J. Cell Biol. , vol.124 , pp. 507-519
    • Page, B.D.1    Satterwhite, L.L.2    Rose, M.D.3    Snyder, M.4
  • 26
    • 0028997459 scopus 로고
    • Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
    • Panzner, S., L. Dreier, E. Hartmann, S. Kostka, and T.A. Rapoport. 1995. Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p Cell. 81:561-570.
    • (1995) Cell. , vol.81 , pp. 561-570
    • Panzner, S.1    Dreier, L.2    Hartmann, E.3    Kostka, S.4    Rapoport, T.A.5
  • 27
    • 0020000913 scopus 로고
    • Genes involved in the control of nuclear fusion during the sexual cycle of Saccharomyces cerevisiae
    • Polama, J . and J. Conde 1982. Genes involved in the control of nuclear fusion during the sexual cycle of Saccharomyces cerevisiae. Mol. & Gen. Genet. 186.253-258.
    • (1982) Mol. & Gen. Genet. , vol.186 , pp. 253-258
    • Polama, J.1    Conde, J.2
  • 29
    • 0026335172 scopus 로고
    • Structure of the yeast endoplasmic reticulum, localization of ER proteins using immunofluorescence and immunoelectron microscopy
    • Preuss, D , J Mulholland, C.A. Kaiser, P. Orlean, C. Albright, M.D Rose, P.W. Robbins, and D. Botstein 1991. Structure of the yeast endoplasmic reticulum, localization of ER proteins using immunofluorescence and immunoelectron microscopy. Yeast 7.891-911.
    • (1991) Yeast , vol.7 , pp. 891-911
    • Preuss, D.1    Mulholland, J.2    Kaiser, C.A.3    Orlean, P.4    Albright, C.5    Rose, M.D.6    Robbins, P.W.7    Botstein, D.8
  • 30
    • 0029089959 scopus 로고
    • An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments
    • Rabouille, C., T.P. Levine, J.-M. Peters, and G. Warren. 1995. An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments. Cell. 82:905-914.
    • (1995) Cell. , vol.82 , pp. 905-914
    • Rabouille, C.1    Levine, T.P.2    Peters, J.-M.3    Warren, G.4
  • 31
    • 0021044363 scopus 로고
    • Structure and function of the yeast URA3 gene. Differentially regulated expression of hybrid beta-galactosidase from overlapping coding sequences in yeast
    • Rose, M., and D. Botstein. 1983. Structure and function of the yeast URA3 gene. Differentially regulated expression of hybrid beta-galactosidase from overlapping coding sequences in yeast. J. Mol. Biol. 170:883-904.
    • (1983) J. Mol. Biol. , vol.170 , pp. 883-904
    • Rose, M.1    Botstein, D.2
  • 32
    • 0025938605 scopus 로고
    • Nuclear fusion in yeast
    • Rose, M.D. 1991. Nuclear fusion in yeast. Annu. Rev. Microbiol. 45:539-567.
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 539-567
    • Rose, M.D.1
  • 33
    • 0024338964 scopus 로고
    • KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene
    • Rose, M.D., L.M. Misra, and J.P. Vogel. 1989. KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell. 57:1211-1221.
    • (1989) Cell. , vol.57 , pp. 1211-1221
    • Rose, M.D.1    Misra, L.M.2    Vogel, J.P.3
  • 34
    • 0006514917 scopus 로고
    • Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast
    • Rothblatt, J.A., R.J. Deshaies, S.L. Sanders, G. Daum, and R. Schekman. 1989. Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast J. Cell Biol 72:61-68.
    • (1989) J. Cell Biol , vol.72 , pp. 61-68
    • Rothblatt, J.A.1    Deshaies, R.J.2    Sanders, S.L.3    Daum, G.4    Schekman, R.5
  • 35
    • 0024787847 scopus 로고
    • A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein
    • Sadler, I., A. Chiang, T. Kurihara, J. Rothblatt, J. Way, and P. Silver. 1989. A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein. J Cell Biol. 109:2665-2675.
    • (1989) J Cell Biol. , vol.109 , pp. 2665-2675
    • Sadler, I.1    Chiang, A.2    Kurihara, T.3    Rothblatt, J.4    Way, J.5    Silver, P.6
  • 37
    • 0027136175 scopus 로고
    • Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum
    • Scidmore, M.A., H.H. Okamura, and M.D. Rose. 1993. Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum. Mol Biol Cell. 4:1145-1159.
    • (1993) Mol Biol Cell. , vol.4 , pp. 1145-1159
    • Scidmore, M.A.1    Okamura, H.H.2    Rose, M.D.3
  • 39
    • 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 P. Heiter. 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    Heiter, P.2
  • 40
    • 0022493616 scopus 로고
    • Gene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y
    • Stevens, T.H , J.H. Rothman, G S Payne, and R Schekman. 1986. Gene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y. J Cell Biol 102:1551-1557.
    • (1986) J Cell Biol , vol.102 , pp. 1551-1557
    • Stevens, T.H.1    Rothman, J.H.2    Payne, G.S.3    Schekman, R.4
  • 41
    • 0027175035 scopus 로고
    • Calcium mobilization is required for nuclear vesicle fusion in vitro: Implications for membrane traffic and IP3 receptor function
    • Sullivan, K.M , W.B. Busa, and K.L. Wilson. 1993. Calcium mobilization is required for nuclear vesicle fusion in vitro: implications for membrane traffic and IP3 receptor function. Cell 73:1411-1422.
    • (1993) Cell , vol.73 , pp. 1411-1422
    • Sullivan, K.M.1    Busa, W.B.2    Wilson, K.L.3
  • 42
    • 0023376280 scopus 로고
    • Two genes required for cell fusion during yeast conjugation: Evidence for a pheromone-induced surface protein
    • Trueheart, J , J D. Boeke, and G.R. Fink 1987. Two genes required for cell fusion during yeast conjugation: evidence for a pheromone-induced surface protein. Mol. Cell. Biol 7:2316-2328.
    • (1987) Mol. Cell. Biol , vol.7 , pp. 2316-2328
    • Trueheart, J.1    Boeke, J.D.2    Fink, G.R.3
  • 43
    • 0025339295 scopus 로고
    • Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast
    • Vogel, J P., L.M. Misra, and M.D. Rose. 1990. Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast. J. Cell Biol. 110:1885-1895.
    • (1990) J. Cell Biol. , vol.110 , pp. 1885-1895
    • Vogel, J.P.1    Misra, L.M.2    Rose, M.D.3
  • 44
    • 0026492542 scopus 로고
    • Membrane fusion
    • White, J M. 1992. Membrane fusion. Science (Wash. DC). 258:917-924.
    • (1992) Science (Wash. DC) , vol.258 , pp. 917-924
    • White, J.M.1


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