메뉴 건너뛰기




Volumn 112, Issue 17, 1999, Pages 2813-2821

VIP36 localisation to the early secretory pathway

Author keywords

Brefeldin A; Cycling; ER Golgi intermediate structure; Glycolipid raft

Indexed keywords

CARBOHYDRATE; CELL MEMBRANE MARKER; CELL MEMBRANE PROTEIN; LECTIN;

EID: 0032879945     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (96)

References (48)
  • 1
    • 0028971172 scopus 로고
    • Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport
    • Aridor, M., Bannykh, S. I., Rowe, T. and Balch, W. E. (1995). Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport. J. Cell Biol. 131, 875-893.
    • (1995) J. Cell Biol. , vol.131 , pp. 875-893
    • Aridor, M.1    Bannykh, S.I.2    Rowe, T.3    Balch, W.E.4
  • 2
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the cell surface
    • Brown, D. A. and Rose, J. K. (1992). Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the cell surface. Cell 68, 533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 3
    • 0001619084 scopus 로고    scopus 로고
    • VIP17/MAL, a lipid raft-associated protein is involved in apical transport in MCCK cells
    • Cheong, K., Zacchetti, D., Schneeberger, E. E. and Simons, K. (1999). VIP17/MAL, a lipid raft-associated protein is involved in apical transport in MCCK cells. Proc. Nat. Acad. Sci. USA 10, 6241-6248.
    • (1999) Proc. Nat. Acad. Sci. USA , vol.10 , pp. 6241-6248
    • Cheong, K.1    Zacchetti, D.2    Schneeberger, E.E.3    Simons, K.4
  • 5
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan, G. I., Lewis, G. K., Ramsay, G. and Bishop, J. M. (1985). Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell Biol. 5, 3610-3616.
    • (1985) Mol. Cell Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 6
    • 0027257099 scopus 로고
    • Glycosphingolipid-enriched, detergent-insoluble complexes in protein sorting in epithelial cells
    • Fiedler, K., Kobayashi, T., Kurzchalia, T. V. and Simons, K. (1993). Glycosphingolipid-enriched, detergent-insoluble complexes in protein sorting in epithelial cells. Biochemistry 32, 6365-6373.
    • (1993) Biochemistry , vol.32 , pp. 6365-6373
    • Fiedler, K.1    Kobayashi, T.2    Kurzchalia, T.V.3    Simons, K.4
  • 7
    • 0028233139 scopus 로고
    • A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins
    • Fiedler, K. and Simons, K. (1994). A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins. Cell 77, 625-626.
    • (1994) Cell , vol.77 , pp. 625-626
    • Fiedler, K.1    Simons, K.2
  • 8
    • 0028209329 scopus 로고
    • VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells
    • Fiedler, K., Parton, R. G., Kellner, R., Etzold, T. and Simons, K. (1994). VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells. EMBO J. 13, 1729-1740.
    • (1994) EMBO J. , vol.13 , pp. 1729-1740
    • Fiedler, K.1    Parton, R.G.2    Kellner, R.3    Etzold, T.4    Simons, K.5
  • 9
    • 0030051122 scopus 로고    scopus 로고
    • Characterization of VIP36, an animal lectin homologous to leguminous lectins
    • Fiedler, K. and Simons, K. (1996). Characterization of VIP36, an animal lectin homologous to leguminous lectins. J. Cell Sci. 109, 271-276.
    • (1996) J. Cell Sci. , vol.109 , pp. 271-276
    • Fiedler, K.1    Simons, K.2
  • 10
    • 1842410168 scopus 로고    scopus 로고
    • Human Rer1 is localized to the Golgi apparatus and complements the deletion of the homologous Rerl protein of Saccharomyces cerevisiae
    • Füllekrug, J., Boehm, J., Röttger, S., Nilsson, T., Mieskes, G. and Schmitt, H. D. (1997). Human Rer1 is localized to the Golgi apparatus and complements the deletion of the homologous Rerl protein of Saccharomyces cerevisiae. Eur. J. Cell Biol. 74, 31-40.
    • (1997) Eur. J. Cell Biol. , vol.74 , pp. 31-40
    • Füllekrug, J.1    Boehm, J.2    Röttger, S.3    Nilsson, T.4    Mieskes, G.5    Schmitt, H.D.6
  • 12
    • 0026633791 scopus 로고
    • A brefeldin A-like phenotype is induced by the overexpression of a human ERD-2-like protein, ELP-1
    • Hsu, V. W., Shah, N. and Klausner, R. D. (1992). A brefeldin A-like phenotype is induced by the overexpression of a human ERD-2-like protein, ELP-1. Cell 69, 625-635.
    • (1992) Cell , vol.69 , pp. 625-635
    • Hsu, V.W.1    Shah, N.2    Klausner, R.D.3
  • 13
    • 0026091737 scopus 로고
    • Selective inhibition of transcytosis by brefeldin A in MDCK cells
    • Hunziker, W., Whitney, J. A. and Mellman, I. (1991). Selective inhibition of transcytosis by brefeldin A in MDCK cells. Cell 67, 617-627.
    • (1991) Cell , vol.67 , pp. 617-627
    • Hunziker, W.1    Whitney, J.A.2    Mellman, I.3
  • 14
    • 0029001946 scopus 로고
    • A novel endocytosis signal related to the KKXX ER-retrieval signal
    • Itin, C., Kappeler, F., Linstedt, A. D. and Hauri, H. P. (1995). A novel endocytosis signal related to the KKXX ER-retrieval signal. EMBO J. 14, 2250-2256.
    • (1995) EMBO J. , vol.14 , pp. 2250-2256
    • Itin, C.1    Kappeler, F.2    Linstedt, A.D.3    Hauri, H.P.4
  • 15
    • 0029876344 scopus 로고    scopus 로고
    • ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins
    • Itin, C., Roche, A. C., Monsigny, M. and Hauri, H. P. (1996). ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins. Mol. Biol. Cell 7, 483-493.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 483-493
    • Itin, C.1    Roche, A.C.2    Monsigny, M.3    Hauri, H.P.4
  • 16
    • 0028214108 scopus 로고
    • A dual role for COOH-terminal lysine residues in pre-Golgi retention and endocytosis of ERGIC-53
    • Kappeler, F., Itin, C., Schindler, R. and Hauri, H. P. (1994). A dual role for COOH-terminal lysine residues in pre-Golgi retention and endocytosis of ERGIC-53. J. Biol. Chem. 269, 6279-6281.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6279-6281
    • Kappeler, F.1    Itin, C.2    Schindler, R.3    Hauri, H.P.4
  • 17
    • 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
  • 18
    • 0025339825 scopus 로고
    • Methods for introducing DNA into mammalian cells
    • Keown, W. A., Campbell, C. R. and Kucherlapati, R. S. (1990). Methods for introducing DNA into mammalian cells. Meth. Enzymol. 185, 527-537.
    • (1990) Meth. Enzymol. , vol.185 , pp. 527-537
    • Keown, W.A.1    Campbell, C.R.2    Kucherlapati, R.S.3
  • 19
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R. D., Donaldson, J. G. and Lippincott-Schwartz, J. (1992). Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116, 1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 20
    • 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
  • 21
    • 0026640940 scopus 로고
    • VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles
    • Kurzchalia, T. V., Dupree, P., Parton, R. G., Kellner, R., Virta, H., Lehnert, M. and Simons, K. (1992). VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles. J. Cell Biol. 118, 1003-1014.
    • (1992) J. Cell Biol. , vol.118 , pp. 1003-1014
    • Kurzchalia, T.V.1    Dupree, P.2    Parton, R.G.3    Kellner, R.4    Virta, H.5    Lehnert, M.6    Simons, K.7
  • 22
    • 0032555901 scopus 로고    scopus 로고
    • Annexin XIIIb associates with lipid microdomains to function in apical delivery
    • Lafont, F., Lecat, S., Verkade, P. and Simons, K. (1998). Annexin XIIIb associates with lipid microdomains to function in apical delivery. J. Cell Biol. 142, 1413-1427.
    • (1998) J. Cell Biol. , vol.142 , pp. 1413-1427
    • Lafont, F.1    Lecat, S.2    Verkade, P.3    Simons, K.4
  • 23
  • 24
    • 0027244942 scopus 로고
    • Giantin, a novel conserved Golgi membrane-protein containing a cytoplasmic domain of at least 350-kda
    • Linstedt, A. D. and Hauri, H. P. (1993). Giantin, a novel conserved Golgi membrane-protein containing a cytoplasmic domain of at least 350-kda. Mol. Biol. Cell 4, 679-693.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 679-693
    • Linstedt, A.D.1    Hauri, H.P.2
  • 25
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz, J., Donaldson, J. G., Schweizer, A., Berger, E. G., Hauri, H. P., Yuan, L. C. and Klausner, R. D. (1990). Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 60, 821-836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 26
    • 0028920154 scopus 로고
    • The capacity to retrieve escaped ER proteins extends to the trans-most cistema of the Golgi stack
    • Miesenböck, G. and Rothman, J. E. (1995). The capacity to retrieve escaped ER proteins extends to the trans-most cistema of the Golgi stack. J. Cell Biol. 129, 309-319.
    • (1995) J. Cell Biol. , vol.129 , pp. 309-319
    • Miesenböck, G.1    Rothman, J.E.2
  • 28
    • 0031738937 scopus 로고    scopus 로고
    • Uptake by COPI-coated vesicles of both anterograde and retrograde cargo is inhibited by GTPγS in vitro
    • Nickel, W., Malsam, J., Gorgas, K., Ravazzola, M., Jenne, N., Helms, J. B. and Wieland, F. T. (1998). Uptake by COPI-coated vesicles of both anterograde and retrograde cargo is inhibited by GTPγS in vitro. J. Cell Sci. 111, 3081-3090.
    • (1998) J. Cell Sci. , vol.111 , pp. 3081-3090
    • Nickel, W.1    Malsam, J.2    Gorgas, K.3    Ravazzola, M.4    Jenne, N.5    Helms, J.B.6    Wieland, F.T.7
  • 30
    • 0027263507 scopus 로고
    • Binding of coatomer to Golgi membranes requires ADP-ribosylation factor
    • Palmer, D. J., Helms, J. B., Beckers, C. J., Orci, L. and Rothman, J. E. (1993). Binding of coatomer to Golgi membranes requires ADP-ribosylation factor. J. Biol. Chem. 268, 12083-12089.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12083-12089
    • Palmer, D.J.1    Helms, J.B.2    Beckers, C.J.3    Orci, L.4    Rothman, J.E.5
  • 31
    • 0345683542 scopus 로고    scopus 로고
    • The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells
    • Puertollano, R., Martin-Belmonte, F., Millan, J., de Marco, M. C., Albar, J. P., Kremer, L. and Alonso, M. A. (1999). The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells. J. Cell Biol. 145, 141-151.
    • (1999) J. Cell Biol. , vol.145 , pp. 141-151
    • Puertollano, R.1    Martin-Belmonte, F.2    Millan, J.3    De Marco, M.C.4    Albar, J.P.5    Kremer, L.6    Alonso, M.A.7
  • 32
    • 0028905820 scopus 로고
    • Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides
    • Rabouille, C., Hui, N., Hunte, F., Kieckbusch, R., Berger, E. G., Warren, G. and Nilsson, T. (1995). Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J. Cell Sci. 108, 1617-1627.
    • (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
  • 33
    • 0027447921 scopus 로고
    • TGN38/41 recycles between the cell surface and the TGN: Brefeldin A affects its rate of return to the TGN
    • Reaves, B., Horn, M. and Banting, G. (1993). TGN38/41 recycles between the cell surface and the TGN: brefeldin A affects its rate of return to the TGN. Mol. Biol. Cell 4, 93-105.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 93-105
    • Reaves, B.1    Horn, M.2    Banting, G.3
  • 35
    • 0022343674 scopus 로고
    • Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation
    • Roth, J., Taatjes, D. J., Lucocq, J. M., Weinstein, J. and Paulson, J. C. (1985). Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation. Cell 43, 287-295.
    • (1985) Cell , vol.43 , pp. 287-295
    • Roth, J.1    Taatjes, D.J.2    Lucocq, J.M.3    Weinstein, J.4    Paulson, J.C.5
  • 36
    • 0021148465 scopus 로고
    • Pre-and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface
    • Saraste, J. and Kuismanen, E. (1984). Pre-and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface. Cell 38, 535-549.
    • (1984) Cell , vol.38 , pp. 535-549
    • Saraste, J.1    Kuismanen, E.2
  • 37
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • Scales, S. J., Pepperkok, R. and Kreis, T. E. (1997). Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell 90, 1137-1148.
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 38
    • 0033593321 scopus 로고    scopus 로고
    • Influenza viruses select ordered lipid domains during budding from the plasma membrane
    • Scheiffele, P., Rietveld, A., Wilk, T. and Simons, K. (1999). Influenza viruses select ordered lipid domains during budding from the plasma membrane. J. Biol. Chem. 274, 2038-2044.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2038-2044
    • Scheiffele, P.1    Rietveld, A.2    Wilk, T.3    Simons, K.4
  • 39
    • 0028840671 scopus 로고
    • The Golgi-localization of yeast Emp47p depends on its di-lysine motif but is not affected by the retl-1 mutation in alpha-COP
    • Schröder, S., Schimmöller, F., Singer-Krüger, B. and Riezman, H. (1995). The Golgi-localization of yeast Emp47p depends on its di-lysine motif but is not affected by the retl-1 mutation in alpha-COP. J. Cell Biol. 131, 895-912.
    • (1995) J. Cell Biol. , vol.131 , pp. 895-912
    • Schröder, S.1    Schimmöller, F.2    Singer-Krüger, B.3    Riezman, H.4
  • 40
    • 0023733211 scopus 로고
    • Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus
    • Schweizer, A., Fransen, J. A., Bachi, T., Ginsel, L. and Hauri, H. P. (1988). Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J. Cell Biol. 107, 1643-1653.
    • (1988) J. Cell Biol. , vol.107 , pp. 1643-1653
    • Schweizer, A.1    Fransen, J.A.2    Bachi, T.3    Ginsel, L.4    Hauri, H.P.5
  • 41
    • 0025610518 scopus 로고
    • Identification of an intermediate compartment involved in protein transport from endoplasmic reticulum to Golgi apparatus
    • Schweizer, A., Fransen, J. A., Matter, K., Kreis, T. E., Ginsel, L. and Hauri, H. P. (1990). Identification of an intermediate compartment involved in protein transport from endoplasmic reticulum to Golgi apparatus. Eur. J. Cell Biol. 53, 185-196.
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 185-196
    • Schweizer, A.1    Fransen, J.A.2    Matter, K.3    Kreis, T.E.4    Ginsel, L.5    Hauri, H.P.6
  • 42
    • 0031417668 scopus 로고    scopus 로고
    • Identification of components of trans-Golgi network-derived transport vesicles and detergent-insoluble complexes by nanoelectrospray tandem mass spectrometry
    • Shevchenko, A., Keller, P., Scheiffele, P., Mann, M. and Simons, K. (1997). Identification of components of trans-Golgi network-derived transport vesicles and detergent-insoluble complexes by nanoelectrospray tandem mass spectrometry. Electrophoresis 18, 2591-2600.
    • (1997) Electrophoresis , vol.18 , pp. 2591-2600
    • Shevchenko, A.1    Keller, P.2    Scheiffele, P.3    Mann, M.4    Simons, K.5
  • 43
    • 0027439583 scopus 로고
    • Molecular cloning, characterization, subcellular localization and dynamics of p23, the mammalian KDEL receptor
    • Tang, B. L., Wong, S. H., Qi, X. L., Low, S. H. and Hong, W. (1993). Molecular cloning, characterization, subcellular localization and dynamics of p23, the mammalian KDEL receptor. J. Cell Biol. 120, 325-328.
    • (1993) J. Cell Biol. , vol.120 , pp. 325-328
    • Tang, B.L.1    Wong, S.H.2    Qi, X.L.3    Low, S.H.4    Hong, W.5
  • 44
    • 0030995064 scopus 로고    scopus 로고
    • p53/58 binds COPI and is required for selective transport through the early secretory pathway
    • Tisdale, E. J., H. Plutner, J. Matteson, and W. E. Balch. (1997). p53/58 binds COPI and is required for selective transport through the early secretory pathway. J. Cell Biol. 137, 581-593.
    • (1997) J. Cell Biol. , vol.137 , pp. 581-593
    • Tisdale, E.J.1    Plutner, H.2    Matteson, J.3    Balch, W.E.4
  • 45
    • 0032897432 scopus 로고    scopus 로고
    • Dual-color visualization of trans-golgi network to plasma membrane traffic along microtubules in living cells
    • Toomre, D., Keller, P., White, J., Olivo, J. C. and Simons, K. (1999). Dual-color visualization of trans-golgi network to plasma membrane traffic along microtubules in living cells. J. Cell Sci. 112, 21-33.
    • (1999) J. Cell Sci. , vol.112 , pp. 21-33
    • Toomre, D.1    Keller, P.2    White, J.3    Olivo, J.C.4    Simons, K.5
  • 46
    • 0025153020 scopus 로고
    • Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells
    • Wandinger-Ness, A., Bennett, M. K., Antony, C. and Simons, K. (1990). Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells. J. Cell Biol. 111, 987-1000.
    • (1990) J. Cell Biol. , vol.111 , pp. 987-1000
    • Wandinger-Ness, A.1    Bennett, M.K.2    Antony, C.3    Simons, K.4
  • 47
    • 0032238268 scopus 로고    scopus 로고
    • VIP36 recognizes high-mannose type glycans in relation to apical membrane traffic
    • Yamashita, K., Kuge, S. and Ohkura, T. (1998). VIP36 recognizes high-mannose type glycans in relation to apical membrane traffic. Tanpakushitsu Kakusan Koso 43 (16 Suppl): 2455-2463.
    • (1998) Tanpakushitsu Kakusan Koso , vol.43 , Issue.16 SUPPL. , pp. 2455-2463
    • Yamashita, K.1    Kuge, S.2    Ohkura, T.3
  • 48
    • 0031910288 scopus 로고    scopus 로고
    • Scattered Golgi elements during microtubule disruption are initially enriched in trans-Golgi proteins
    • Yang, W. and Storrie, B. (1998). Scattered Golgi elements during microtubule disruption are initially enriched in trans-Golgi proteins. Mol. Biol. Cell 9, 191-207.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 191-207
    • Yang, W.1    Storrie, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.