메뉴 건너뛰기




Volumn 139, Issue 7, 1997, Pages 1735-1745

Aggregation as a determinant of protein fate in post-Golgi compartments: Role of the luminal domain of furin in lysosomal targeting

Author keywords

[No Author keywords available]

Indexed keywords

FURIN; MEMBRANE PROTEIN; PROTEINASE;

EID: 0031426632     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.7.1735     Document Type: Article
Times cited : (63)

References (70)
  • 1
    • 0028922618 scopus 로고
    • Invariant chain cleavage and peptide loading in major histocompatibility complex class II vesicles
    • Amigorena, S., P. Webster, J. Drake, J. Newcomb, P. Cresswell, and I. Mellman. 1995. Invariant chain cleavage and peptide loading in major histocompatibility complex class II vesicles. J. Exp. Med. 181:1729-1741.
    • (1995) J. Exp. Med. , vol.181 , pp. 1729-1741
    • Amigorena, S.1    Webster, P.2    Drake, J.3    Newcomb, J.4    Cresswell, P.5    Mellman, I.6
  • 2
    • 0031001304 scopus 로고    scopus 로고
    • Activation of the furin endoprotease is a multiple-step process: Requirements for acidification and internal propeptide cleavage
    • Anderson, E.D., J.K. VanSlyke, C.D. Thulin, F. Jean, and G. Thomas. 1997. Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage. EMBO (Eur. Mol. Biol. Organ.) J. 16:1508-1518.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 1508-1518
    • Anderson, E.D.1    Vanslyke, J.K.2    Thulin, C.D.3    Jean, F.4    Thomas, G.5
  • 3
    • 0022894660 scopus 로고
    • Biosynthesis, glycosylation, movement through the Golgi system, and transport to lysosomes by an N-linked carbohydrate-independent mechanism of three lysosomal integral membrane proteins
    • Barriocanal, J.G., J.S. Bonifacino, L. Yuan, and I.V. Sandoval. 1986. Biosynthesis, glycosylation, movement through the Golgi system, and transport to lysosomes by an N-linked carbohydrate-independent mechanism of three lysosomal integral membrane proteins. J. Biol. Chem. 261:16755-16763.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16755-16763
    • Barriocanal, J.G.1    Bonifacino, J.S.2    Yuan, L.3    Sandoval, I.V.4
  • 4
    • 0027639817 scopus 로고
    • Biogenesis of constitutive secretory vesicles, secretory granules and synaptic vesicles
    • Bauerfeind, R., and W.B. Huttner. 1993. Biogenesis of constitutive secretory vesicles, secretory granules and synaptic vesicles. Curr. Opin. Cell Biol. 5: 628-635.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 628-635
    • Bauerfeind, R.1    Huttner, W.B.2
  • 5
    • 0011720253 scopus 로고
    • Role for intracellular proteases in the processing and transport of class II HLA antigens
    • Blum, J.S., and P. Cresswell. 1988. Role for intracellular proteases in the processing and transport of class II HLA antigens. Proc. Natl. Acad. Sci. USA. 85:3975-3979.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3975-3979
    • Blum, J.S.1    Cresswell, P.2
  • 7
    • 0001708541 scopus 로고
    • Degradation of proteins retained in the endoplasmic reticulum
    • A. Ciechanover, and A.L. Schwarte, editors. Wiley-Liss, Inc., New York
    • Bonifacino, J.S., and R.D. Klausner. 1994. Degradation of proteins retained in the endoplasmic reticulum. In Cellular Proteolytic Systems. A. Ciechanover, and A.L. Schwarte, editors. Wiley-Liss, Inc., New York. 137-160.
    • (1994) Cellular Proteolytic Systems , pp. 137-160
    • Bonifacino, J.S.1    Klausner, R.D.2
  • 8
    • 0024577266 scopus 로고
    • Internalization and recycling to serotonin-containing granules of the 80K integral membrane protein exposed on the surface of secreting rat basophilic leukaemia cells
    • Bonifacino, J.S., L. Yuan, and I.V. Sandoval. 1989. Internalization and recycling to serotonin-containing granules of the 80K integral membrane protein exposed on the surface of secreting rat basophilic leukaemia cells. J. Cell Sci. 92:701-712.
    • (1989) J. Cell Sci. , vol.92 , pp. 701-712
    • Bonifacino, J.S.1    Yuan, L.2    Sandoval, I.V.3
  • 11
    • 0027498027 scopus 로고
    • Multiple GTP-binding proteins participate in clathrin-coated vesicle-mediated endocytosis
    • Carter, L.L., T.E. Redelmeier, L.A. Woollenweber, and S.L. Schmid. 1993. Multiple GTP-binding proteins participate in clathrin-coated vesicle-mediated endocytosis. J. Cell Biol. 120:37-45.
    • (1993) J. Cell Biol. , vol.120 , pp. 37-45
    • Carter, L.L.1    Redelmeier, T.E.2    Woollenweber, L.A.3    Schmid, S.L.4
  • 12
    • 0028283375 scopus 로고
    • Retrieval of TGN proteins from the cell surface requires endosomal acidification
    • Chapman, R.E., and S. Munro. 1994. Retrieval of TGN proteins from the cell surface requires endosomal acidification. EMBO (Eur. Mol. Biol. Organ.) J. 13:2305-2312.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 2305-2312
    • Chapman, R.E.1    Munro, S.2
  • 13
    • 0024260833 scopus 로고
    • Selective degradation of T cell antigen receptor chains retained in a pre-Golgi compartment
    • Chen, C., J.S. Bonifacino, L.C. Yuan, and R.D. Klausner. 1988. Selective degradation of T cell antigen receptor chains retained in a pre-Golgi compartment. J. Cell Biol. 107:2149-2161.
    • (1988) J. Cell Biol. , vol.107 , pp. 2149-2161
    • Chen, C.1    Bonifacino, J.S.2    Yuan, L.C.3    Klausner, R.D.4
  • 14
    • 0030043593 scopus 로고    scopus 로고
    • Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH
    • Colomer, V., G.A. Kicska, and M.J. Rindler. 1996. Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH. J. Biol. Cliem. 271:48-55.
    • (1996) J. Biol. Cliem. , vol.271 , pp. 48-55
    • Colomer, V.1    Kicska, G.A.2    Rindler, M.J.3
  • 16
    • 0030896993 scopus 로고    scopus 로고
    • Endocytic trafficking of megalin/RAP complexes: Dissociation of the complexes in late endosomes
    • Czekay, R.P., R.A. Orlando, L. Woodward, M. Lundstrom, and M.G. Farquhar. 1997. Endocytic trafficking of megalin/RAP complexes: dissociation of the complexes in late endosomes. Mol. Biol. Cell. 8:517-532.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 517-532
    • Czekay, R.P.1    Orlando, R.A.2    Woodward, L.3    Lundstrom, M.4    Farquhar, M.G.5
  • 17
    • 0027455464 scopus 로고
    • Posttranslational folding of vesicular stomatitis virus G protein in the ER: Involvement of noncovalent and covalent complexes
    • de Silva, A., I. Braakman, and A. Helenius. 1993. Posttranslational folding of vesicular stomatitis virus G protein in the ER: Involvement of noncovalent and covalent complexes. J. Cell Biol. 120:647-655.
    • (1993) J. Cell Biol. , vol.120 , pp. 647-655
    • De Silva, A.1    Braakman, I.2    Helenius, A.3
  • 18
    • 0027253219 scopus 로고
    • Uncleaved signals for glycosylphosphatidylinositol anchoring cause retention of precursor proteins in the endoplasmic reticulum
    • Delahunty, M.D., F.J. Stafford, L.C. Yuan, D. Shaz, and J.S. Bonifacino. 1993. Uncleaved signals for glycosylphosphatidylinositol anchoring cause retention of precursor proteins in the endoplasmic reticulum. J. Biol. Chem. 268: 12017-12027.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12017-12027
    • Delahunty, M.D.1    Stafford, F.J.2    Yuan, L.C.3    Shaz, D.4    Bonifacino, J.S.5
  • 19
    • 0030792177 scopus 로고    scopus 로고
    • Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation
    • Dittié, A.S., L. Thomas, G. Thomas, and S.A. Tooze. 1997. Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation. EMBO (Eur. Mol. Biol. Organ.) J. 16:4859-1870.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 4859-11870
    • Dittié, A.S.1    Thomas, L.2    Thomas, G.3    Tooze, S.A.4
  • 20
    • 0026623115 scopus 로고
    • ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein β-COP to Golgi membranes
    • Donaldson, J.G., D. Cassel, R.A. Kahn, and R.D. Klausner. 1992. ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein β-COP to Golgi membranes. Proc. Natl. Acad. Sci. USA. 89:6408-6412.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6408-6412
    • Donaldson, J.G.1    Cassel, D.2    Kahn, R.A.3    Klausner, R.D.4
  • 21
    • 0028290272 scopus 로고
    • Aluminum fluoride acts on the reversibility of ARF1-dependent coat protein binding to Golgi membranes
    • Finazzi, D., D. Cassel, J.G. Donaldson, and R.D. Klausner. 1994. Aluminum fluoride acts on the reversibility of ARF1-dependent coat protein binding to Golgi membranes. J. Biol. Chem. 269:13325-13330.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13325-13330
    • Finazzi, D.1    Cassel, D.2    Donaldson, J.G.3    Klausner, R.D.4
  • 22
    • 0027730475 scopus 로고
    • Regulated secretory proteins in the exocrine pancreas aggregate under conditions that mimic the trans-Golgi network
    • Freedman, S., and G.A. Scheele. 1993. Regulated secretory proteins in the exocrine pancreas aggregate under conditions that mimic the trans-Golgi network. Biochem. Biophvs. Res. Commun. 197:992-999.
    • (1993) Biochem. Biophvs. Res. Commun. , vol.197 , pp. 992-999
    • Freedman, S.1    Scheele, G.A.2
  • 23
    • 0027303736 scopus 로고
    • Peptide binding inhibits protein aggregation of invariant-chain free class II dimers and promotes expression of occupied molecules
    • Germain, R.N., and A.G. Rinker, Jr. 1993. Peptide binding inhibits protein aggregation of invariant-chain free class II dimers and promotes expression of occupied molecules. Nature. 363:725-728.
    • (1993) Nature , vol.363 , pp. 725-728
    • Germain, R.N.1    Rinker Jr., A.G.2
  • 24
    • 0023580391 scopus 로고
    • Kinetics of intracellular transport and sorting of lysosomal membrane and plasma membrane proteins
    • Green, S.A., K.P. Zimmer, G. Griffiths, and I. Mellman. 1987. Kinetics of intracellular transport and sorting of lysosomal membrane and plasma membrane proteins. J. Cell Biol. 105:1227-1240.
    • (1987) J. Cell Biol. , vol.105 , pp. 1227-1240
    • Green, S.A.1    Zimmer, K.P.2    Griffiths, G.3    Mellman, I.4
  • 25
    • 0022187987 scopus 로고
    • Exit of newly synthesized membrane proteins from the trans cisternae of the Golgi complex to the plasma membrane
    • Griffiths, G., S. Pfeiffer, K. Simons, and K. Matlin. 1985. Exit of newly synthesized membrane proteins from the trans cisternae of the Golgi complex to the plasma membrane. J. Cell Biol. 101:949-964.
    • (1985) J. Cell Biol. , vol.101 , pp. 949-964
    • Griffiths, G.1    Pfeiffer, S.2    Simons, K.3    Matlin, K.4
  • 26
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C., and A. Helenius. 1995. Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7:523-529.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 27
    • 0025635768 scopus 로고
    • Structure and expression of mouse furin, a yeast Kex2-rclated protease: Lack of processing of coexpressed prorenin in GH4C1 cells
    • Hatsuzawa, K., M. Hosaka, T. Nakagawa, M. Nagase, A. Shoda, K. Murakami, and K. Nakayama. 1990. Structure and expression of mouse furin, a yeast Kex2-rclated protease: lack of processing of coexpressed prorenin in GH4C1 cells. J. Biol. Chem. 265:22075-22078.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22075-22078
    • Hatsuzawa, K.1    Hosaka, M.2    Nakagawa, T.3    Nagase, M.4    Shoda, A.5    Murakami, K.6    Nakayama, K.7
  • 28
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi, R., B. Krummel, and R.K. Saiki. 1988. A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res. 16:7351-7367.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 30
    • 0027395956 scopus 로고
    • Localization of TGN38 to the trans-Golgi network: Involvement of a cytoplasmic tyrosine-containing sequence
    • Humphrey, J.S., P.J. Peters, L.C. Yuan, and J.S. Bonifacino. 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
  • 31
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley, S.M., and A. Helenius. 1989. Protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 5:277-307.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 32
    • 0028866530 scopus 로고
    • Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase II site in its cytoplasmic tail
    • Jones, B.J., L. Thomas, S.S. Molloy, C.D. Thulin, M.D. Fry, K.A. Walsh, and G. Thomas. 1995. Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase II site in its cytoplasmic tail. EMBO (Eur. Mol. Biol. Organ.) J. 14:5869-5883.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 5869-5883
    • Jones, B.J.1    Thomas, L.2    Molloy, S.S.3    Thulin, C.D.4    Fry, M.D.5    Walsh, K.A.6    Thomas, G.7
  • 33
    • 0028871001 scopus 로고
    • Endoproteolytic cleavage of HIV-1 gp160 envelope precursor occurs after exit from the transGolgi network (TGN)
    • Kantanen, M.L., P. Leinikki, and E. Kuismanen. 1995. Endoproteolytic cleavage of HIV-1 gp160 envelope precursor occurs after exit from the transGolgi network (TGN). Arch. Virol. 140:1441-1449.
    • (1995) Arch. Virol. , vol.140 , pp. 1441-1449
    • Kantanen, M.L.1    Leinikki, P.2    Kuismanen, E.3
  • 34
    • 0030910371 scopus 로고    scopus 로고
    • Proprotein-processing endoprotease furin controls the growth and differentiation of gastric mucous cells
    • Konda, Y., H. Yokota, T. Kayo, T. Horiuchi, N. Sugiyama, S. Tanaka, K. Takata, and T. Takeuchi. 1997. Proprotein-processing endoprotease furin controls the growth and differentiation of gastric mucous cells. J. Clin. Invest. 99:1842-1851.
    • (1997) J. Clin. Invest. , vol.99 , pp. 1842-1851
    • Konda, Y.1    Yokota, H.2    Kayo, T.3    Horiuchi, T.4    Sugiyama, N.5    Tanaka, S.6    Takata, K.7    Takeuchi, T.8
  • 35
    • 0026721473 scopus 로고
    • Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage
    • Leduc, R., S.S. Molloy, B.A. Thorne, and G. Thomas. 1992. Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage. J. Biol. Chem. 267:14304-14308.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14304-14308
    • Leduc, R.1    Molloy, S.S.2    Thorne, B.A.3    Thomas, G.4
  • 37
    • 0026772733 scopus 로고
    • A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targetine and endocytosis of CD3 chains
    • Letourneur, F., and R.D. Klausner. 1992. A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targetine and endocytosis of CD3 chains. Cell. 69:1143-1157.
    • (1992) Cell , vol.69 , pp. 1143-1157
    • Letourneur, F.1    Klausner, R.D.2
  • 39
    • 0028820625 scopus 로고
    • A lysosomal targeting signal in the cytoplasmic tail of the β chain directs HLA-DM to MHC class II compartments
    • Marks, M.S., P.A. Roche, E. van Donselaar, L. Woodruff, P.J. Peters, and J.S. Bonifacino. 1995. A lysosomal targeting signal in the cytoplasmic tail of the β 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
  • 40
    • 0030003317 scopus 로고    scopus 로고
    • Protein targeting by tyrosine- and di-leucine-based signals: Evidence for distinct saturable components
    • Marks, M.S., L. Woodruff, H. Ohno, and J.S. Bonifacino. 1996. Protein targeting by tyrosine- and di-leucine-based signals: Evidence for distinct saturable components. J. Cell Biol. 135:341-354
    • (1996) J. Cell Biol. , vol.135 , pp. 341-354
    • Marks, M.S.1    Woodruff, L.2    Ohno, H.3    Bonifacino, J.S.4
  • 41
    • 0031106781 scopus 로고    scopus 로고
    • Protein sorting by tyrosine-based signals: Adapting to the Ys and wherefores
    • Marks, M.S., H. Ohno, T. Kirchhausen, and J.S. Bonifacino. 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.S.4
  • 42
    • 73049130725 scopus 로고
    • A method for determining the sedimentation behavior of enzymes: Application to protein mixtures
    • Martin, R.G., and B.N. Ames. 1961. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J. Biol. Chem. 236:1372-1379.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1372-1379
    • Martin, R.G.1    Ames, B.N.2
  • 43
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman, I. 1996. Endocytosis and molecular sorting. Annn. Rev. Cell Dev. Biol. 12:575-625.
    • (1996) Annn. Rev. Cell Dev. Biol. , vol.12 , pp. 575-625
    • Mellman, I.1
  • 44
    • 0028107656 scopus 로고
    • Intracellular trafficking and activation of the furin proprotein convertase: Localization to the TGN and recycling from the cell surface
    • Molloy, S.S., L. Thomas, J.K. VanSlyke, P.E. Stenberg, and G. Thomas. 1994. Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface. EMBO (Eur. mol. Biol. Organ.) J. 13:18-33.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 18-33
    • Molloy, S.S.1    Thomas, L.2    VanSlyke, J.K.3    Stenberg, P.E.4    Thomas, G.5
  • 45
    • 0027296764 scopus 로고
    • Identification of an isoform with an extremely large Cys-rich region of PC6, a Kex2-like processing endoprotease
    • Nakagawa, T., K. Murakami, and K. Nakayama. 1993. Identification of an isoform with an extremely large Cys-rich region of PC6, a Kex2-like processing endoprotease. FEBS (Fed. Eur. Biochem. Soc.) Lett. 327:165-171.
    • (1993) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.327 , pp. 165-171
    • Nakagawa, T.1    Murakami, K.2    Nakayama, K.3
  • 46
    • 0027379586 scopus 로고
    • Intermediates in degradation of the erythropoietin receptor accumulate and are degraded in lysosomes
    • Neumann, D., L. Wikström, S.S. Watowich, and H.F. Lodish. 1993. Intermediates in degradation of the erythropoietin receptor accumulate and are degraded in lysosomes. J. Biol. Chem. 268:13639-13649.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13639-13649
    • Neumann, D.1    Wikström, L.2    Watowich, S.S.3    Lodish, H.F.4
  • 48
    • 0029826535 scopus 로고    scopus 로고
    • Structural determinants of interaction of tyrosine-based sorting signals with the adaptor medium chains
    • Ohno, H., M.C. Fournier, G. Poy, and J.S. Bonifacino. 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
  • 49
    • 0026754578 scopus 로고
    • Regulation of PACE propeptide-processing activity: Requirement for a post-endoplasmic reticulum compartment and autoproteolytic activation
    • Rehemtulla, A., A.J. Dorner, and R.J. Kaufman. 1992. Regulation of PACE propeptide-processing activity: requirement for a post-endoplasmic reticulum compartment and autoproteolytic activation. Proc. Natl. Acad. Sci. USA. 89:8235-8239.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8235-8239
    • Rehemtulla, A.1    Dorner, A.J.2    Kaufman, R.J.3
  • 50
    • 0028981715 scopus 로고
    • A determinant in the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor prevents trafficking to lysosomes
    • Rohrer, J., A. Shweizer, K.F. Johnson, and S. Kornfeld. 1995. A determinant in the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor prevents trafficking to lysosomes. J. Cell Biol. 130:1297-1306.
    • (1995) J. Cell Biol. , vol.130 , pp. 1297-1306
    • Rohrer, J.1    Shweizer, A.2    Johnson, K.F.3    Kornfeld, S.4
  • 51
    • 0024149621 scopus 로고
    • Regulation of protein export from the endoplasmic reticulum
    • Rose, J.K., and R.W. Doms. 1988. Regulation of protein export from the endoplasmic reticulum. Annu. Rev. Cell Biol. 4:257-288.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 257-288
    • Rose, J.K.1    Doms, R.W.2
  • 52
    • 0021866937 scopus 로고
    • A monoclonal antibody 7G7/B6, binds to an epitope on the human interleukin-2 (IL-2) receptor that is distinct from that recognized by IL-2 or anti-Tac
    • Rubin, L.A., C.C. Kurman, W.E. Biddison, N.D. Goldman, and D.L. Nelson. 1985. A monoclonal antibody 7G7/B6, binds to an epitope on the human interleukin-2 (IL-2) receptor that is distinct from that recognized by IL-2 or anti-Tac. Hybridoma. 4:91-102.
    • (1985) Hybridoma , vol.4 , pp. 91-102
    • Rubin, L.A.1    Kurman, C.C.2    Biddison, W.E.3    Goldman, N.D.4    Nelson, D.L.5
  • 53
    • 0029011658 scopus 로고
    • Communication of post-Golgi elements with early endocytic pathway: Regulation of endoproteolytic cleavage of Semliki Forest virus p62 precursor
    • Sariola, M., J. Saraste, and E. Kuismanen. 1995. Communication of post-Golgi elements with early endocytic pathway: regulation of endoproteolytic cleavage of Semliki Forest virus p62 precursor. J. Cell Sci. 108:2465-2475.
    • (1995) J. Cell Sci. , vol.108 , pp. 2465-2475
    • Sariola, M.1    Saraste, J.2    Kuismanen, E.3
  • 54
    • 0029071584 scopus 로고
    • Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin
    • Schäfer, W., A. Stroh, S. Berghöfer, J. Seiler, M. Vey, M.L. Kruse, H.F. Kern, H.D. Klenk, and W. Garten. 1995. Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin. EMBO (Eur. Mol. Biol. Organ.) J. 14:2424-2435.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 2424-2435
    • Schäfer, W.1    Stroh, A.2    Berghöfer, S.3    Seiler, J.4    Vey, M.5    Kruse, M.L.6    Kern, H.F.7    Klenk, H.D.8    Garten, W.9
  • 55
    • 0023637186 scopus 로고
    • An LFA-3 cDNA encodes a phospholipid-linked membrane protein homologous to its receptor CD2
    • Seed, B. 1987. An LFA-3 cDNA encodes a phospholipid-linked membrane protein homologous to its receptor CD2. Nature. 329:840-842.
    • (1987) Nature , vol.329 , pp. 840-842
    • Seed, B.1
  • 57
    • 0028238359 scopus 로고
    • Calcium- and pH-dependent aggregation and membrane association of the precursor of the prohormone convertase PC2
    • Shennan, K.I., N.A. Taylor, and K. Docherty. 1994. Calcium- and pH-dependent aggregation and membrane association of the precursor of the prohormone convertase PC2. J. Biol. Chem. 269:18646-18650.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18646-18650
    • Shennan, K.I.1    Taylor, N.A.2    Docherty, K.3
  • 58
    • 0029050635 scopus 로고
    • Processing of procarboxypeptidase E into carboxypeptidase E occurs in secretory vesicles
    • Song, L., and L. Fricker. 1995a. Processing of procarboxypeptidase E into carboxypeptidase E occurs in secretory vesicles. J. Neurochem. 65:444-453.
    • (1995) J. Neurochem. , vol.65 , pp. 444-453
    • Song, L.1    Fricker, L.2
  • 59
    • 0028912393 scopus 로고
    • Calcium- and pH -dependent aggregation of carboxypeptidase E
    • Song, L., and L.D. Fricker. 1995b. Calcium- and pH -dependent aggregation of carboxypeptidase E. J. Biol. Chem. 270:7963-7967.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7963-7967
    • Song, L.1    Fricker, L.D.2
  • 60
    • 0028875689 scopus 로고
    • Localization of furin to the trans-Golgi network and recycling from the cell surface involves Ser and Tyr residues within the cytoplasmic domain
    • Takahashi, S., T. Nakagawa, T. Banno, T. Watanabe, K. Murakami, and K. Nakayama. 1995. Localization of furin to the trans-Golgi network and recycling from the cell surface involves Ser and Tyr residues within the cytoplasmic domain. J. Biol. Chem. 270:28397-28401.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28397-28401
    • Takahashi, S.1    Nakagawa, T.2    Banno, T.3    Watanabe, T.4    Murakami, K.5    Nakayama, K.6
  • 61
    • 0023850352 scopus 로고
    • SR alpha promoter: An efficient and versatile mammalian cDNA expression system composed of the simian virus 40 early promoter and the R-U5 segment of human T-cell leukemia virus type 1 long terminal repeat
    • Takebe, Y., M. Seiki, J. Fujisawa, P. Hoy, K. Yokota, K. Arai, M. Yoshida, and N. Arai. 1988, SR alpha promoter: an efficient and versatile mammalian cDNA expression system composed of the simian virus 40 early promoter and the R-U5 segment of human T-cell leukemia virus type 1 long terminal repeat. Mol. Cell Biol. 8:466-472.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 466-472
    • Takebe, Y.1    Seiki, M.2    Fujisawa, J.3    Hoy, P.4    Yokota, K.5    Arai, K.6    Yoshida, M.7    Arai, N.8
  • 62
    • 0022468419 scopus 로고
    • Transport of macrophage Fc receptors and Fc receptor-bound ligands to lysosomes
    • Ukkonen, P., V. Lewis, M. Marsh, A. Helenius, and I. Mellman. 1986. Transport of macrophage Fc receptors and Fc receptor-bound ligands to lysosomes. J. Exp. Med. 163:952-971.
    • (1986) J. Exp. Med. , vol.163 , pp. 952-971
    • Ukkonen, P.1    Lewis, V.2    Marsh, M.3    Helenius, A.4    Mellman, I.5
  • 64
    • 0028605962 scopus 로고
    • Maturation of the trans-Golgi network protease furin: Compartmentalization of propeptide removal, substrate cleavage, and COOH-termmal truncation
    • Vey, M., W. Schäfer, S. Berghofer, H.D. Klenk, and W. Garten. 1994. Maturation of the trans-Golgi network protease furin: Compartmentalization of propeptide removal, substrate cleavage, and COOH-termmal truncation. J. Cell Biol. 127:1829-1842.
    • (1994) J. Cell Biol. , vol.127 , pp. 1829-1842
    • Vey, M.1    Schäfer, W.2    Berghofer, S.3    Klenk, H.D.4    Garten, W.5
  • 65
    • 0028839910 scopus 로고
    • An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface
    • Voorhees, P., E. Deignan, E. van Donselaar, J. Humphrey, M.S. Marks, P.J. Peters and J. S. Bonifacino. 1995. An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface. EMBO (Eur. Mol. Biol. Organ.) J. 14:4961-4975.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 4961-4975
    • Voorhees, P.1    Deignan, E.2    Van Donselaar, E.3    Humphrey, J.4    Marks, M.S.5    Peters, P.J.6    Bonifacino, J.S.7
  • 66
    • 0022508408 scopus 로고
    • Exposure of K562 cells to anti-receptor monoclonal antibody OKT9 results in rapid redistribution and enhanced degradation of the transferrin receptor
    • Weissman, A.M., Klausner, K. Rao, and J. B. Harford. 1986 Exposure of K562 cells to anti-receptor monoclonal antibody OKT9 results in rapid redistribution and enhanced degradation of the transferrin receptor. J. Cell Biol. 102:951-958.
    • (1986) J. Cell Biol. , vol.102 , pp. 951-958
    • Weissman, A.M.1    Klausner2    Rao, K.3    Harford, J.B.4
  • 67
    • 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
  • 69
    • 0025606360 scopus 로고
    • Expression of a human proprotein processing enzyme: Correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site
    • Wise, R.J., P. J. Barr, P.A. Wong, M.C. Kiefer, A.J. Brake, and R.J. Kaufman. 1990. Expression of a human proprotein processing enzyme: correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site. Proc. Natl. Acad. Sci. USA. 87:9378-9382.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9378-9382
    • Wise, R.J.1    Barr, P.J.2    Wong, P.A.3    Kiefer, M.C.4    Brake, A.J.5    Kaufman, R.J.6
  • 70
    • 0023375833 scopus 로고
    • Two integral membrane proteins located in the cis-middle and trans-part of the Golgi system acquire sialylated N-linked carbohydrates and display diferent turnovers and sensitivity to cAMP-dependcnt phosphorylation
    • Yuan, L., J.G. Barriocanal, J.S. Bonifacino, and I.V. Sandoval. 1987. Two integral membrane proteins located in the cis-middle and trans-part of the Golgi system acquire sialylated N-linked carbohydrates and display diferent turnovers and sensitivity to cAMP-dependcnt phosphorylation. J. Cell Biol. 105: 215-227.
    • (1987) J. Cell Biol. , vol.105 , pp. 215-227
    • Yuan, L.1    Barriocanal, J.G.2    Bonifacino, J.S.3    Sandoval, I.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.