메뉴 건너뛰기




Volumn 71, Issue 1, 1996, Pages 53-61

Modification of the cytoplasmic domain affects the subcellular localization of Golgi glycosyltransferases

Author keywords

Cytoplasmic domain; Epitope tagging; Glycosyltransferase; Golgi complex; VVS G epitope

Indexed keywords

GLYCOSYLTRANSFERASE;

EID: 0029816516     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (15)

References (37)
  • 1
    • 0028363162 scopus 로고
    • Medial Golgi retention of N-acetylglucosaminetransferase I
    • Burke, J., J. M. Pettitt, D. Humphres, P. A. Gleeson: Medial Golgi retention of N-acetylglucosaminetransferase I. J. Biol. Chem. 269, 12049-12059 (1994)
    • (1994) J. Biol. Chem. , vol.269 , pp. 12049-12059
    • Burke, J.1    Pettitt, J.M.2    Humphres, D.3    Gleeson, P.A.4
  • 2
    • 0026459645 scopus 로고
    • The transmembrane and flanking sequences of β-1,2-N-acetylglucosaminyltransferase I specify medial-Golgi localization
    • Burke, J., J. M. Pettitt, H. Schachter, M. Sarkar, P. A. Gleeson: The transmembrane and flanking sequences of β-1,2-N-acetylglucosaminyltransferase I specify medial-Golgi localization. J. Biol. Chem. 267, 24433-24440 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 24433-24440
    • Burke, J.1    Pettitt, J.M.2    Schachter, H.3    Sarkar, M.4    Gleeson, P.A.5
  • 3
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C., H. Okyama: High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7, 2745-2752 (1987).
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okyama, H.2
  • 4
    • 0026738935 scopus 로고
    • The signal anchor and stem region of the β-galactoside α-2,6-sialyltransferase may each act to localize the enzyme to the Golgi apparatus
    • Colley, K. J., E. U. Lee, J. C. Paulson: The signal anchor and stem region of the β-galactoside α-2,6-sialyltransferase may each act to localize the enzyme to the Golgi apparatus. J. Biol. Chem. 267, 7784-7793 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 7784-7793
    • Colley, K.J.1    Lee, E.U.2    Paulson, J.C.3
  • 5
    • 0025228404 scopus 로고
    • Tubulovesicular processes emerge from trans-Golgi cisternae, extend along microtubules, and interlink adjacent trans-Golgi elements into a reticulum
    • Cooper, M. S., A. H. Cornell-Bell, A. J. Chernjavsky, W. Dani, S. J. Smith: Tubulovesicular processes emerge from trans-Golgi cisternae, extend along microtubules, and interlink adjacent trans-Golgi elements into a reticulum. Cell 61, 135-145 (1990).
    • (1990) Cell , vol.61 , pp. 135-145
    • Cooper, M.S.1    Cornell-Bell, A.H.2    Chernjavsky, A.J.3    Dani, W.4    Smith, S.J.5
  • 6
    • 0027370882 scopus 로고
    • Specific sequences in the signal anchor of the β-galactoside α-2,6-sialyltransferase are not essential for Golgi localization
    • Dahdal, R. Y., K. J. Colley: Specific sequences in the signal anchor of the β-galactoside α-2,6-sialyltransferase are not essential for Golgi localization. J. Biol. Chem. 268, 26310-26319 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 26310-26319
    • Dahdal, R.Y.1    Colley, K.J.2
  • 7
    • 0026034357 scopus 로고
    • β-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to β-adaptin
    • Duden, R., G. Griffiths, R. Frank, P. Argos, T. E. Kreis: β-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to β-adaptin. Cell 64, 649-665 (1991).
    • (1991) Cell , vol.64 , pp. 649-665
    • Duden, R.1    Griffiths, G.2    Frank, R.3    Argos, P.4    Kreis, T.E.5
  • 8
    • 0022340978 scopus 로고
    • Isolation of monoclonal-antibodies specific for human c-myc proto-onco-gene product
    • Evan, G. I., G. K. Lewis, G. Ramsay, J. M. Bishop: Isolation of monoclonal-antibodies specific for human c-myc proto-onco-gene product. Mol. Cell. Biol. 5, 3610-3616 (1985).
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 9
    • 0028132043 scopus 로고
    • Targeting of proteins to the Golgi apparatus
    • Gleeson, P. A., R. D. Teasdale, J. Burke: Targeting of proteins to the Golgi apparatus. Glycoconj. J. 11, 381-394 (1994).
    • (1994) Glycoconj. J. , vol.11 , pp. 381-394
    • Gleeson, P.A.1    Teasdale, R.D.2    Burke, J.3
  • 10
    • 0027157541 scopus 로고
    • Characterization of two cis-regulatory regions in the murine β-1,4-galactosyltransferase gene. Evidence for a negative regulatory element that controls initiation at the proximal site
    • Harduin-Lepers, A., J. H. Shaper, N. L. Shaper: Characterization of two cis-regulatory regions in the murine β-1,4-galactosyltransferase gene. Evidence for a negative regulatory element that controls initiation at the proximal site. J. Biol. Chem. 268, 14348-14359 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 14348-14359
    • Harduin-Lepers, A.1    Shaper, J.H.2    Shaper, N.L.3
  • 11
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane-spanning proteins
    • Hartmann, E., T. A. Rapoport, H. F. Lodish: Predicting the orientation of eukaryotic membrane-spanning proteins. Proc. Natl. Acad. Sci. USA 86, 5786-5790 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5786-5790
    • Hartmann, E.1    Rapoport, T.A.2    Lodish, H.F.3
  • 12
    • 0025074737 scopus 로고
    • Movement of interphase Golgi apparatus is fused mammalian cells and its relationship to cytoskeletal elements and rearrangement of nuclei
    • Ho, W. C., B. Storrie, R .Pepperkok, W. Ansorge, P. Karecla, T. E. Kreis: Movement of interphase Golgi apparatus is fused mammalian cells and its relationship to cytoskeletal elements and rearrangement of nuclei. Eur. J. Cell Biol. 52, 315-327 (1990).
    • (1990) Eur. J. Cell Biol. , vol.52 , pp. 315-327
    • Ho, W.C.1    Storrie, B.2    Pepperkok, R.3    Ansorge, W.4    Karecla, P.5    Kreis, T.E.6
  • 14
    • 0022721628 scopus 로고
    • Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to cell surface
    • Kreis, T. E.: Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to cell surface. EMBO J. 5, 931-941 (1986).
    • (1986) EMBO J. , vol.5 , pp. 931-941
    • Kreis, T.E.1
  • 15
    • 0025638959 scopus 로고
    • Cloning and expression of N-acetylglucosaminyltransferase I, the medial Golgi transferase that initiates complex N-linked carbohydrate formation
    • Kumar, R., J. Yang, R. D. Larsen, P. Stanley: Cloning and expression of N-acetylglucosaminyltransferase I, the medial Golgi transferase that initiates complex N-linked carbohydrate formation. Proc. Natl. Acad. Sci. USA 87, 9948-9952 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9948-9952
    • Kumar, R.1    Yang, J.2    Larsen, R.D.3    Stanley, P.4
  • 16
    • 0027640284 scopus 로고
    • Targeting and retention of Golgi proteins
    • Machamer, C. E.: Targeting and retention of Golgi proteins. Curr. Opin. Cell Biol. 5, 606-612 (1993).
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 606-612
    • Machamer, C.E.1
  • 17
    • 0026503134 scopus 로고
    • The Golgi complex: In vitro veritas?
    • Mellman, I., K. Simons: The Golgi complex: in vitro veritas? Cell 68, 829-840 (1992).
    • (1992) Cell , vol.68 , pp. 829-840
    • Mellman, I.1    Simons, K.2
  • 18
    • 0025990802 scopus 로고
    • Sequences within and adjacent to the transmembrane segment of β-galactoside α-2,6-sialyltransferase are sufficient for Golgi retention
    • Munro, S.: Sequences within and adjacent to the transmembrane segment of β-galactoside α-2,6-sialyltransferase are sufficient for Golgi retention. EMBO J. 10, 3577-3588 (1991).
    • (1991) EMBO J. , vol.10 , pp. 3577-3588
    • Munro, S.1
  • 19
    • 0025015646 scopus 로고
    • Fine-tuning the topology of a polytopic membrane protein: Role of positively and negatively charged amino acids
    • Nilsson, I. M., G. von Heijne: Fine-tuning the topology of a polytopic membrane protein: role of positively and negatively charged amino acids. Cell 62, 1135-1141 (1990).
    • (1990) Cell , vol.62 , pp. 1135-1141
    • Nilsson, I.M.1    Von Heijne, G.2
  • 20
    • 0026072695 scopus 로고
    • The membrane spanning domain of β-1,4-galactosyltransferase specifies trans Golgi localization
    • Nilsson, T., J. M. Lucocq, D. Mackay, G. Warren: The membrane spanning domain of β-1,4-galactosyltransferase specifies trans Golgi localization. EMBO J. 10, 3567-3575 (1991).
    • (1991) EMBO J. , vol.10 , pp. 3567-3575
    • Nilsson, T.1    Lucocq, J.M.2    Mackay, D.3    Warren, G.4
  • 21
    • 0027318045 scopus 로고
    • Kin recognition: A model for retention of Golgi enzymes
    • Nilsson, T., P. Slusarewicz, M. H. Hoe, G. Warren: Kin recognition: a model for retention of Golgi enzymes. FEBS Lett. 330, 1-4 (1993).
    • (1993) FEBS Lett. , vol.330 , pp. 1-4
    • Nilsson, T.1    Slusarewicz, P.2    Hoe, M.H.3    Warren, G.4
  • 22
    • 0027472941 scopus 로고
    • Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeIa cells
    • Nilsson, T., M. Pypaet, M. H. Hoc, P. Slusarewicz, E. G. Berger, G. Warren: Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeIa cells. J. Cell Biol. 120, 5-13 (1993).
    • (1993) J. Cell Biol. , vol.120 , pp. 5-13
    • Nilsson, T.1    Pypaet, M.2    Hoc, M.H.3    Slusarewicz, P.4    Berger, E.G.5    Warren, G.6
  • 24
    • 0024431691 scopus 로고
    • Glycosyltransferase. Structure, localization, and control of cell type-specific glycosylation
    • Paulson, J. C., K. J. Colley: Glycosyltransferase. Structure, localization, and control of cell type-specific glycosylation. J. Biol. Chem. 264, 17615-17618 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 17615-17618
    • Paulson, J.C.1    Colley, K.J.2
  • 25
    • 0027220591 scopus 로고
    • β-COP is essential for biosynthetic membrane transport from endoplasmic reticulum to Golgi complex in vivo
    • Pepperkok, R., J. Scheel, H. Horstmann, H. P. Hauri, G. Griffiths, T. E. Kreis: β-COP is essential for biosynthetic membrane transport from endoplasmic reticulum to Golgi complex in vivo. Cell 74, 71-82 (1993).
    • (1993) Cell , vol.74 , pp. 71-82
    • Pepperkok, R.1    Scheel, J.2    Horstmann, H.3    Hauri, H.P.4    Griffiths, G.5    Kreis, T.E.6
  • 26
    • 0028283041 scopus 로고
    • Molecular characterization of two functional domains of CLIP-170 in vivo
    • Pierre, P., R. Pepperkok, T. E. Kreis: Molecular characterization of two functional domains of CLIP-170 in vivo. J. Cell Sci. 107, 1909-1920 (1994).
    • (1994) J. Cell Sci. , vol.107 , pp. 1909-1920
    • Pierre, P.1    Pepperkok, R.2    Kreis, T.E.3
  • 27
    • 0028905820 scopus 로고
    • Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides
    • Rabouille, C., N. Hui, F. Hunte, R. Kieckbusch, E. G. Berger, G. Warren, T. Nilsson: Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J. Cell Sci. 108, 1617-1627 (1995).
    • (1995) J. Cell Sci. , vol.108 , pp. 1617-1627
    • Rabouille, C.1    Hui, N.2    Hunte, F.3    Kieckbusch, R.4    Berger, E.G.5    Warren, G.6    Nilsson, T.7
  • 28
    • 0025254311 scopus 로고
    • Bovine β-1,4-galactosyltransferase: Two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains
    • Russo, R. N., N. L. Shaper, J. H. Shaper: Bovine β-1,4-galactosyltransferase: two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains. J. Biol. Chem. 265, 3324-3331 (1989).
    • (1989) J. Biol. Chem. , vol.265 , pp. 3324-3331
    • Russo, R.N.1    Shaper, N.L.2    Shaper, J.H.3
  • 29
    • 0026793378 scopus 로고
    • β-1,4-galactosyltransferase: A short NH2-terminal fragment that includes the cytoplasmic and transmembrane domain is sufficient for Golgi retention
    • Russo, R. N., N. L. Shaper, D. J. Taatjes, J. H. Shaper: β-1,4-galactosyltransferase: a short NH2-terminal fragment that includes the cytoplasmic and transmembrane domain is sufficient for Golgi retention. J. Biol. Chem. 267, 9241-9247 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 9241-9247
    • Russo, R.N.1    Shaper, N.L.2    Taatjes, D.J.3    Shaper, J.H.4
  • 31
    • 0025917462 scopus 로고
    • Intracompartmental sorting of essential myosin light chains: Molecular dissection and in vivo monitoring by epitope tagging
    • Soldati, T., J.-C. Perriard: Intracompartmental sorting of essential myosin light chains: molecular dissection and in vivo monitoring by epitope tagging. Cell 66, 277-289 (1991).
    • (1991) Cell , vol.66 , pp. 277-289
    • Soldati, T.1    Perriard, J.-C.2
  • 32
    • 0023955730 scopus 로고
    • Positive charges at the NH2 terminus convert the membrane-anchor signal peptide of cytochrome P-450 to a secretory signal peptide
    • Szczesna-Skorupa, E., N. Browne, D. Mead, B. Kemper: Positive charges at the NH2 terminus convert the membrane-anchor signal peptide of cytochrome P-450 to a secretory signal peptide. Proc. Natl. Acad. Sci. USA 85, 738-742 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 738-742
    • Szczesna-Skorupa, E.1    Browne, N.2    Mead, D.3    Kemper, B.4
  • 33
    • 0028308480 scopus 로고
    • The intracellular mobility of a viral membrane glycoprotein measured by confocal microscope fluorescence recovery after photobleaching
    • Storrie, B., R. Pepperkok, E. H. K. Stelzer, T. E. Kreis: The intracellular mobility of a viral membrane glycoprotein measured by confocal microscope fluorescence recovery after photobleaching. J. Cell Sci. 107, 1309-1319 (1994).
    • (1994) J. Cell Sci. , vol.107 , pp. 1309-1319
    • Storrie, B.1    Pepperkok, R.2    Stelzer, E.H.K.3    Kreis, T.E.4
  • 34
    • 0026686809 scopus 로고
    • The transmembrane domain of N-glucosaminetransferase I contains a Golgi retention signal
    • Tang, B. L., S. H. Wong, W. Hong: The transmembrane domain of N-glucosaminetransferase I contains a Golgi retention signal. J. Biol. Chem. 267, 10122-10126 (1991).
    • (1991) J. Biol. Chem. , vol.267 , pp. 10122-10126
    • Tang, B.L.1    Wong, S.H.2    Hong, W.3
  • 35
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • Von Heijne, G.: The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 5, 3021-3027 (1986).
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Von Heijne, G.1
  • 36
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • Von Heijne, G., Y. Gavel: Topogenic signals in integral membrane proteins. Eur. J. Biochem. 174, 671-678 (1988).
    • (1988) Eur. J. Biochem. , vol.174 , pp. 671-678
    • Von Heijne, G.1    Gavel, Y.2
  • 37
    • 0026598516 scopus 로고
    • The 17-residue transmembrane domain of β-galactoside α2,6-sialyltransferase is sufficient for Golgi retention
    • Wong, S. H., S. H. Low, W. J. Hong: The 17-residue transmembrane domain of β-galactoside α2,6-sialyltransferase is sufficient for Golgi retention. J. Cell Biol. 117, 245-258 (1992).
    • (1992) J. Cell Biol. , vol.117 , pp. 245-258
    • Wong, S.H.1    Low, S.H.2    Hong, W.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.