메뉴 건너뛰기




Volumn 11, Issue 1, 2000, Pages 13-22

Efficient export of the vesicular stomatitis virus G protein from the endoplasmic reticulum requires a signal in the cytoplasmic tail that includes both tyrosine-based and di-acidic motifs

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; TYROSINE DERIVATIVE; VIRUS PROTEIN;

EID: 0033959784     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.1.13     Document Type: Article
Times cited : (155)

References (43)
  • 1
    • 23444432144 scopus 로고
    • Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum
    • Balch, W.E., McCaffery, J.M., Plutner, H., and Farquhar, MG. (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
  • 3
    • 0025027874 scopus 로고
    • Polymerase errors accumulating during natural evolution of the glycoprotein gene of vesicular stomatitis virus indiana serotype isolates
    • Bilsel, P.K., and Nichol, S.T. (1990). Polymerase errors accumulating during natural evolution of the glycoprotein gene of vesicular stomatitis virus indiana serotype isolates. J. Virol. 64, 4873-4883.
    • (1990) J. Virol. , vol.64 , pp. 4873-4883
    • Bilsel, P.K.1    Nichol, S.T.2
  • 4
    • 0029907407 scopus 로고    scopus 로고
    • Sequence requirements for the recognition of tyrosine-based endocytic signals by clathrin AP-2 complexes
    • Boll, W., Ohno, H., Songyang, Z., Rapoport, I., Cantley, L.C., Bonifacino, J.S., and Kirchhausen, T. (1996). Sequence requirements for the recognition of tyrosine-based endocytic signals by clathrin AP-2 complexes. EMBO J. 15, 5789-5795.
    • (1996) EMBO J. , vol.15 , pp. 5789-5795
    • Boll, W.1    Ohno, H.2    Songyang, Z.3    Rapoport, I.4    Cantley, L.C.5    Bonifacino, J.S.6    Kirchhausen, T.7
  • 5
    • 0025012782 scopus 로고
    • A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum
    • Bonifacino, J.S., Suzuki, C.K., and Klausner, R.D. (1990). A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum. Science 247, 79-82.
    • (1990) Science , vol.247 , pp. 79-82
    • Bonifacino, J.S.1    Suzuki, C.K.2    Klausner, R.D.3
  • 6
    • 0030782261 scopus 로고    scopus 로고
    • Heterogeneous distribution of the unusual phospholipid semilysobisphosphatidic acid through the Golgi complex
    • Cluett, E.B., Kuismanen, E., and Machamer, C.E. (1997). Heterogeneous distribution of the unusual phospholipid semilysobisphosphatidic acid through the Golgi complex. Mol. Biol. Cell 8, 2233-2240.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2233-2240
    • Cluett, E.B.1    Kuismanen, E.2    Machamer, C.E.3
  • 8
    • 0023788652 scopus 로고
    • Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein
    • Doms, R.W., Ruusala, A., Machamer, C., Helenius, J., Helenius, A., and Rose, J.K. (1988). Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein. J. Cell Biol. 107, 89-99.
    • (1988) J. Cell Biol. , vol.107 , pp. 89-99
    • Doms, R.W.1    Ruusala, A.2    Machamer, C.3    Helenius, J.4    Helenius, A.5    Rose, J.K.6
  • 9
    • 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
  • 10
    • 0000233999 scopus 로고
    • Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst, T.R., Niles, E.G., Studier, F.W., and Moss, B. (1986). Eukaryotic transient expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA 83, 8122-8126.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, F.W.3    Moss, B.4
  • 11
    • 0027395956 scopus 로고
    • Localization of TGN38 to the trans-Golgi network: Involvement of a cytoplasmic tyrosine-containing sequence
    • Humphrey, J.S., Peters, P.J., Yuan, L.C., and Bonifacino, J.S. (1993). Localization of TGN38 to the trans-Golgi network: involvement of a cytoplasmic tyrosine-containing sequence. J. Cell Biol. 120, 1123-1135.
    • (1993) J. Cell Biol. , vol.120 , pp. 1123-1135
    • Humphrey, J.S.1    Peters, P.J.2    Yuan, L.C.3    Bonifacino, J.S.4
  • 12
    • 0031450221 scopus 로고    scopus 로고
    • The recycling of ERGIC-53 in the early secretory pathway. ERGIC-53 carries a cytosolic endoplasmic reticulum-exit determinant interacting with COPII
    • Kappeler, F., Klopfenstein, D.R., Foguet, M., Paccaud, J.P., and Hauri, H.P. (1997). The recycling of ERGIC-53 in the early secretory pathway. ERGIC-53 carries a cytosolic endoplasmic reticulum-exit determinant interacting with COPII. J. Biol. Chem. 272, 31801-31808.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31801-31808
    • Kappeler, F.1    Klopfenstein, D.R.2    Foguet, M.3    Paccaud, J.P.4    Hauri, H.P.5
  • 13
    • 0030794182 scopus 로고    scopus 로고
    • Linking cargo to vesicle formation: Receptor tail interactions with coat proteins
    • Kirchhausen, T., Bonifacino, J.S., and Riezman, H. (1997). Linking cargo to vesicle formation: receptor tail interactions with coat proteins. Curr. Opin. Cell Biol. 9, 488-495.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 488-495
    • Kirchhausen, T.1    Bonifacino, J.S.2    Riezman, H.3
  • 14
    • 0016904277 scopus 로고
    • Comparative aspects of glycoprotein structure
    • Kornfeld, R., and Kornfeld, S. (1976). Comparative aspects of glycoprotein structure. Annu. Rev. Biochem. 45, 217-237.
    • (1976) Annu. Rev. Biochem. , vol.45 , pp. 217-237
    • Kornfeld, R.1    Kornfeld, S.2
  • 15
    • 0022721628 scopus 로고
    • Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface
    • 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.
    • (1986) EMBO J. , vol.5 , pp. 931-941
    • Kreis, T.E.1
  • 16
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., Roberts, J.D., and Zakour, R.A. (1987). Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154, 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0019959320 scopus 로고
    • The interaction of antibody with the major surface glycoprotein of vesicular stomatitis virus
    • Lefrancois, L., and Lyles, D.S. (1982). The interaction of antibody with the major surface glycoprotein of vesicular stomatitis virus. Virology 121, 168-174.
    • (1982) Virology , vol.121 , pp. 168-174
    • Lefrancois, L.1    Lyles, D.S.2
  • 19
    • 0026772733 scopus 로고
    • A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains
    • Letourneur, F., and Klausner, R.D. (1992). A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains. Cell 69, 1143-1157.
    • (1992) Cell , vol.69 , pp. 1143-1157
    • Letourneur, F.1    Klausner, R.D.2
  • 20
    • 0022236656 scopus 로고
    • A single N-linked oligosaccharide at either of two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface
    • Machamer, C.E., Florkiewicz, R.Z., and Rose, J.K. (1985). A single N-linked oligosaccharide at either of two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface. Mol. Cell. Biol. 5, 3074-3083.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3074-3083
    • Machamer, C.E.1    Florkiewicz, R.Z.2    Rose, J.K.3
  • 21
    • 0027227549 scopus 로고
    • Retention of a cis Golgi protein requires polar residues on one face of a predicted alpha-helix in the transmembrane domain
    • Machamer, C.E., Grim, M.G., Esquela, A., Chung, S.W., Rolls, M., Ryan, K., and Swift, A.M. (1993). Retention of a cis Golgi protein requires polar residues on one face of a predicted alpha-helix in the transmembrane domain. Mol. Biol. Cell 4, 695-704.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 695-704
    • Machamer, C.E.1    Grim, M.G.2    Esquela, A.3    Chung, S.W.4    Rolls, M.5    Ryan, K.6    Swift, A.M.7
  • 22
    • 0033606772 scopus 로고    scopus 로고
    • Chimeric forms of furin and TGN38 are transported with the plasma membrane in the trans-Golgi network via distinct endosomal pathways
    • Mallet, W.G., and Maxfield, F.R. (1999). Chimeric forms of furin and TGN38 are transported with the plasma membrane in the trans-Golgi network via distinct endosomal pathways. J. Cell Biol. 146, 345-359.
    • (1999) J. Cell Biol. , vol.146 , pp. 345-359
    • Mallet, W.G.1    Maxfield, F.R.2
  • 23
    • 0031106781 scopus 로고    scopus 로고
    • Protein sorting by tyrosine-based signals: Adapting to the Ys and wherefores
    • Marks, M.S., Ohno, H., Kirchhausen, T., and Bonifacino, J. (1997). Protein sorting by tyrosine-based signals: adapting to the Ys and wherefores. Trends Cell Biol. 7, 124-128.
    • (1997) Trends Cell Biol. , vol.7 , pp. 124-128
    • Marks, M.S.1    Ohno, H.2    Kirchhausen, T.3    Bonifacino, J.4
  • 24
    • 0028820625 scopus 로고
    • A lysosomal targeting signal in the cytoplasmic tail of the beta chain directs HLA-DM to MHC class II compartments
    • Marks, M.S., Roche, P.A., van Donselaar, E., Woodruff, L., Peters, P.J., and Bonifacino, J.S. (1995). A lysosomal targeting signal in the cytoplasmic tail of the beta chain directs HLA-DM to MHC class II compartments. J. Cell Biol. 131, 351-369.
    • (1995) J. Cell Biol. , vol.131 , pp. 351-369
    • Marks, M.S.1    Roche, P.A.2    Van Donselaar, E.3    Woodruff, L.4    Peters, P.J.5    Bonifacino, J.S.6
  • 25
    • 0027175236 scopus 로고
    • A soluble secretory protein is first concentrated in the endoplasmic reticulum before transfer to the Golgi apparatus
    • Mizuno, M., and Singer, S.J. (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
  • 26
    • 0024557256 scopus 로고
    • Glycoprotein evolution of vesicular stomatitis New Jersey
    • Nichol, S.T., Rowe, J.E., and Fitch, W.M. (1989). Glycoprotein evolution of vesicular stomatitis New Jersey. Virology 168, 281-291.
    • (1989) Virology , vol.168 , pp. 281-291
    • Nichol, S.T.1    Rowe, J.E.2    Fitch, W.M.3
  • 27
    • 0030812940 scopus 로고    scopus 로고
    • A di-acidic signal required for selective export from the endoplasmic reticulum
    • Nishimura, N., and Balch, W.E. (1997). A di-acidic signal required for selective export from the endoplasmic reticulum. Science 277, 556-558.
    • (1997) Science , vol.277 , pp. 556-558
    • Nishimura, N.1    Balch, W.E.2
  • 28
    • 0033018150 scopus 로고    scopus 로고
    • A di-acidic (DXE) code directs concentration of cargo during export from the endoplasmic reticulum
    • Nishimura, N., Bannykh, S., Slabough, S., Matteson, J., Altschuler, Y., Hahn, K., and Balch, W.E. (1999). A di-acidic (DXE) code directs concentration of cargo during export from the endoplasmic reticulum. J. Biol. Chem. 274, 15937-15946.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15937-15946
    • Nishimura, N.1    Bannykh, S.2    Slabough, S.3    Matteson, J.4    Altschuler, Y.5    Hahn, K.6    Balch, W.E.7
  • 29
    • 0032476017 scopus 로고    scopus 로고
    • The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals
    • Ohno, H., Aguilar, R.C., Yeh, D., Taura, D., Saito, T., and Bonifacino, J.S. (1998). The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals. J. Biol. Chem. 273, 25915-25921.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25915-25921
    • Ohno, H.1    Aguilar, R.C.2    Yeh, D.3    Taura, D.4    Saito, T.5    Bonifacino, J.S.6
  • 30
    • 0029826535 scopus 로고    scopus 로고
    • Structural determinants of interaction of tyrosine-based sorting signals with the adaptor medium chains
    • Ohno, H., Fournier, M.-C., Poy, G., and Bonifacino, J.S. (1996). Structural determinants of interaction of tyrosine-based sorting signals with the adaptor medium chains. J. Biol. Chem. 271, 29009-29015.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29009-29015
    • Ohno, H.1    Fournier, M.-C.2    Poy, G.3    Bonifacino, J.S.4
  • 32
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • Owen, D.J., and Evans, P.R. (1998). A structural explanation for the recognition of tyrosine-based endocytotic signals. Science 282, 1327-1332.
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 33
    • 0023077578 scopus 로고
    • Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi complex
    • Pfeffer, S.R., and Rothman, J.E. (1987). Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi complex. Annu. Rev. Biochem. 56, 829-852.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 829-852
    • Pfeffer, S.R.1    Rothman, J.E.2
  • 34
    • 0022535303 scopus 로고
    • Cytoplasmic domain of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane
    • Puddington, L., Machamer, C.E., and Rose, J.K. (1986). Cytoplasmic domain of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane. J. Cell Biol. 102, 2147-2157.
    • (1986) J. Cell Biol. , vol.102 , pp. 2147-2157
    • Puddington, L.1    Machamer, C.E.2    Rose, J.K.3
  • 36
    • 0020826782 scopus 로고
    • Altered cytoplasmic domains affect intracellular transport of the vesicular stomatitis virus glycoprotein
    • Rose, J.K., and Bergmann, J.E. (1983). Altered cytoplasmic domains affect intracellular transport of the vesicular stomatitis virus glycoprotein. Cell 34, 513-524.
    • (1983) Cell , vol.34 , pp. 513-524
    • Rose, J.K.1    Bergmann, J.E.2
  • 37
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B., and Sander, C. (1993). Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 38
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B., and Sander, C. (1994). Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19, 55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 39
    • 0023371134 scopus 로고
    • Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane
    • Scullion, B.F., Hou, Y., Puddington, L., Rose, J.K., and Jacobson, K. (1987). Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane. J. Cell Biol. 105, 69-75.
    • (1987) J. Cell Biol. , vol.105 , pp. 69-75
    • Scullion, B.F.1    Hou, Y.2    Puddington, L.3    Rose, J.K.4    Jacobson, K.5
  • 40
    • 0025940737 scopus 로고
    • A Golgi retention signal in a membrane-spanning domain of coronavirus E1 protein
    • Swift, A.M., and Machamer, C.E. (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
  • 41
    • 0027407766 scopus 로고
    • Vesicular stomatitis virus glycoprotein contains a dominant cytoplasmic basolateral sorting signal critically dependent upon a tyrosine
    • Thomas, D.C., Brewer, C.B., and Roth, M.G. (1993). Vesicular stomatitis virus glycoprotein contains a dominant cytoplasmic basolateral sorting signal critically dependent upon a tyrosine. J. Biol. Chem. 268, 3313-3320.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3313-3320
    • Thomas, D.C.1    Brewer, C.B.2    Roth, M.G.3
  • 42
    • 0028217859 scopus 로고
    • The basolateral targeting signal in the cytoplasmic domain of glycoprotein G from vesicular stomatitis virus resembles a variety of intracellular targeting motifs related by primary sequence but having diverse targeting activities
    • Thomas, D.C., and Roth, M.G. (1994). The basolateral targeting signal in the cytoplasmic domain of glycoprotein G from vesicular stomatitis virus resembles a variety of intracellular targeting motifs related by primary sequence but having diverse targeting activities. J. Biol. Chem. 269, 15732-15739.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15732-15739
    • Thomas, D.C.1    Roth, M.G.2
  • 43
    • 0024347709 scopus 로고
    • Glycoprotein cytoplasmic domain sequences required for rescue of a vesicular stomatitis virus glycoprotein mutant
    • Whitt, M.A., Chong, L., and Rose, J.K. (1989). Glycoprotein cytoplasmic domain sequences required for rescue of a vesicular stomatitis virus glycoprotein mutant. J. Virol. 63, 3569-3578.
    • (1989) J. Virol. , vol.63 , pp. 3569-3578
    • Whitt, M.A.1    Chong, L.2    Rose, J.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.