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Volumn 118, Issue 10, 2005, Pages 2279-2293

tGolgin-1 (p230, golgin-245) modulates Shiga-toxin transport to the Golgi and Golgi motility towards the microtubule-organizing centre

Author keywords

Centrosome; Dynactin; Dynein; Endosome; Retrograde transport

Indexed keywords

BREFELDIN A; DYNACTIN; DYNEIN ADENOSINE TRIPHOSPHATASE; GOLGIN 1; MEMBRANE PROTEIN; OLIGONUCLEOTIDE; SHIGA TOXIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 21044446690     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.02358     Document Type: Article
Times cited : (82)

References (82)
  • 1
    • 0033535617 scopus 로고    scopus 로고
    • A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins
    • Barr, F. A. (1999). A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins. Curr. Biol. 9, 381-384.
    • (1999) Curr. Biol. , vol.9 , pp. 381-384
    • Barr, F.A.1
  • 2
    • 0022401488 scopus 로고
    • Localization of galactosyl- and sialyltransferase by immunofluoresconce: Evidence for different sites
    • Berger, E. G. and Hesford, F. J. (1985). Localization of galactosyl- and sialyltransferase by immunofluoresconce: evidence for different sites. Proc. Natl. Acad. Sci. USA 82, 4736-4739.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4736-4739
    • Berger, E.G.1    Hesford, F.J.2
  • 3
    • 0343986043 scopus 로고
    • Passage of an integral membrane protein, the vesicular stomatitis virus glycoprotein, through the Golgi apparatus en route to the plasma membrane
    • Bergmann, J. E., Tokuyasu, K. T. and Singer, S. J. (1981). Passage of an integral membrane protein, the vesicular stomatitis virus glycoprotein, through the Golgi apparatus en route to the plasma membrane. Proc. Natl. Acad. Sci. USA 78, 1746-1750.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 1746-1750
    • Bergmann, J.E.1    Tokuyasu, K.T.2    Singer, S.J.3
  • 4
    • 0037986392 scopus 로고    scopus 로고
    • Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis
    • Berson, J. F., Theos, A. C., Harper, D. C., Tenza, D., Raposo, G. and Marks, M. S. (2003). Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis. J. Cell Biol. 161, 521-533.
    • (2003) J. Cell Biol. , vol.161 , pp. 521-533
    • Berson, J.F.1    Theos, A.C.2    Harper, D.C.3    Tenza, D.4    Raposo, G.5    Marks, M.S.6
  • 5
    • 0025114865 scopus 로고
    • Colocalized transmembrane determinants for ER degradation and subunit assembly explain the intracellular fate of TCR chains
    • Bonifacino, J. S., Cosson, P. and Klausner, R. D. (1990). Colocalized transmembrane determinants for ER degradation and subunit assembly explain the intracellular fate of TCR chains. Cell 63, 503-513.
    • (1990) Cell , vol.63 , pp. 503-513
    • Bonifacino, J.S.1    Cosson, P.2    Klausner, R.D.3
  • 6
    • 0035013167 scopus 로고    scopus 로고
    • The GRIP domain is a specific targeting sequence for a population of trans-Golgi network derived tubulo-vesicular carriers
    • Brown, D. L., Heimann, K., Lock, J., Kjer-Nielsen, L., van Vliet, C., Stow, J. L. and Gleeson, P. A. (2001). The GRIP domain is a specific targeting sequence for a population of trans-Golgi network derived tubulo-vesicular carriers. Traffic 2, 336-344.
    • (2001) Traffic , vol.2 , pp. 336-344
    • Brown, D.L.1    Heimann, K.2    Lock, J.3    Kjer-Nielsen, L.4    van Vliet, C.5    Stow, J.L.6    Gleeson, P.A.7
  • 7
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organization in biomembranes: What physical studies of model membranes reveal
    • Brown, R. E. (1998). Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. J. Cell Sci. 111, 1-9.
    • (1998) J. Cell Sci. , vol.111 , pp. 1-9
    • Brown, R.E.1
  • 8
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • Burkhardt, J. K., Echeverri, C. J., Nilsson, T. and Vallee, R. B. (1997). Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution. J. Cell Biol. 139, 469-484.
    • (1997) J. Cell Biol. , vol.139 , pp. 469-484
    • Burkhardt, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 9
    • 0029972823 scopus 로고    scopus 로고
    • Golgi dispersal during microtubule disruption: Regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites
    • Cole, N. B., Sciaky, N., Marotta, A., Song, J. and Lippincott-Schwartz, J. (1996a). Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites. Mol. Biol. Cell 7, 631-650.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 631-650
    • Cole, N.B.1    Sciaky, N.2    Marotta, A.3    Song, J.4    Lippincott-Schwartz, J.5
  • 11
    • 0026760941 scopus 로고
    • Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex
    • Corthesy-Theulaz, I., Pauloin, A. and Pfeffer, S. R. (1992). Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex. J. Cell Biol. 118, 1333-1345.
    • (1992) J. Cell Biol. , vol.118 , pp. 1333-1345
    • Corthesy-Theulaz, I.1    Pauloin, A.2    Pfeffer, S.R.3
  • 12
    • 0036056634 scopus 로고    scopus 로고
    • Characterization of mouse tGolgin-1 (golgin-245/ trans Golgi p230/ 256kD golgin) and its upregulation during oligodendrocyte development
    • Cowan, D. A., Gay, D., Bieler, B. M., Zhao, H., Yoshino, A., Davis, J. G., Tomayko, M. M., Murali, R., Greene, M. I. and Marks, M. S. (2002). Characterization of mouse tGolgin-1 (golgin-245/ trans Golgi p230/ 256kD golgin) and its upregulation during oligodendrocyte development. DNA Cell Biol. 21, 505-517.
    • (2002) DNA Cell Biol. , vol.21 , pp. 505-517
    • Cowan, D.A.1    Gay, D.2    Bieler, B.M.3    Zhao, H.4    Yoshino, A.5    Davis, J.G.6    Tomayko, M.M.7    Murali, R.8    Greene, M.I.9    Marks, M.S.10
  • 13
    • 12344320665 scopus 로고    scopus 로고
    • Mammalian GRIP domain proteins differ in their membrane binding properties and are recruited to distinct domains of the TGN
    • Derby, M. C., van Vliet, C., Brown, D., Luke, M. R., Lu, L., Hong, W., Stow, J. L. and Gleeson, P. A. (2004). Mammalian GRIP domain proteins differ in their membrane binding properties and are recruited to distinct domains of the TGN. J. Cell Sci. 117, 5865-5874.
    • (2004) J. Cell Sci. , vol.117 , pp. 5865-5874
    • Derby, M.C.1    van Vliet, C.2    Brown, D.3    Luke, M.R.4    Lu, L.5    Hong, W.6    Stow, J.L.7    Gleeson, P.A.8
  • 14
    • 0037455546 scopus 로고    scopus 로고
    • The coiled-coil membrane protein golgin-84 is a novel Rab effector required for Golgi ribbon formation
    • Diao, A., Rahman, D., Pappin, D. J. C., Lucocq, J. and Lowe, M. (2003). The coiled-coil membrane protein golgin-84 is a novel Rab effector required for Golgi ribbon formation. J. Cell Biol. 160, 201-212.
    • (2003) J. Cell Biol. , vol.160 , pp. 201-212
    • Diao, A.1    Rahman, D.2    Pappin, D.J.C.3    Lucocq, J.4    Lowe, M.5
  • 15
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K. and Tuschl, T. (2001). Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411, 494-498.
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3    Yalcin, A.4    Weber, K.5    Tuschl, T.6
  • 16
    • 0029873481 scopus 로고    scopus 로고
    • Molecular characterization of trans-Golgi p230. A human peripheral membrane protein encoded by a gene on chromosome 6p12-22 contains extensive coiled-coil α-helical domains and a granin motif
    • Erlich, R., Gleeson, P. A., Campbell, P., Dietzsch, E. and Toh, B.-H. (1996). Molecular characterization of trans-Golgi p230. A human peripheral membrane protein encoded by a gene on chromosome 6p12-22 contains extensive coiled-coil α-helical domains and a granin motif. J. Biol. Chem. 271, 8328-8337.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8328-8337
    • Erlich, R.1    Gleeson, P.A.2    Campbell, P.3    Dietzsch, E.4    Toh, B.-H.5
  • 17
    • 0035168061 scopus 로고    scopus 로고
    • Targeting of Shiga toxin B-subunit to retrograde transport route in association with detergent-resistant membranes
    • Falguières, T., Mallard, F., Baron, C., Hanau, D., Lingwood, C., Goud, B., Salamero, J. and Johannes, L. (2001). Targeting of Shiga toxin B-subunit to retrograde transport route in association with detergent-resistant membranes. Mol. Biol. Cell 12, 2453-2468.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2453-2468
    • Falguières, T.1    Mallard, F.2    Baron, C.3    Hanau, D.4    Lingwood, C.5    Goud, B.6    Salamero, J.7    Johannes, L.8
  • 18
    • 0029417349 scopus 로고
    • Molecular characterization of golgin-245, a novel Golgi complex protein containing a granin signature
    • Fritzler, M. J., Lung, C.-C., Hamel, J. C., Griffith, K. J. and Chan, E. K. L. (1995). Molecular characterization of golgin-245, a novel Golgi complex protein containing a granin signature. J. Biol. Chem. 270, 31262-31268.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31262-31268
    • Fritzler, M.J.1    Lung, C.-C.2    Hamel, J.C.3    Griffith, K.J.4    Chan, E.K.L.5
  • 19
    • 0032563568 scopus 로고    scopus 로고
    • An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells
    • Ghosh, R. N., Mallet, W. G., Soe, T. T., McGraw, T. E. and Maxfield, F. R. (1998). An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells. J. Cell Biol. 142, 923-936.
    • (1998) J. Cell Biol. , vol.142 , pp. 923-936
    • Ghosh, R.N.1    Mallet, W.G.2    Soe, T.T.3    McGraw, T.E.4    Maxfield, F.R.5
  • 20
    • 7244248570 scopus 로고    scopus 로고
    • The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi
    • Gillingham, A. K., Tong, A. H. Y., Boone, C. and Munro, S. (2004). The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi. J. Cell Biol. 167, 281-292.
    • (2004) J. Cell Biol. , vol.167 , pp. 281-292
    • Gillingham, A.K.1    Tong, A.H.Y.2    Boone, C.3    Munro, S.4
  • 22
    • 0030848727 scopus 로고    scopus 로고
    • Molecular cloning of a novel 97-kD Golgi complex autoantigen associated with Sjogren's syndrome
    • Griffith, K. J., Chan, E. K., Lung, C. C., Hamel, J. C., Guo, X., Miyachi, K. and Fritzler, M. J. (1997). Molecular cloning of a novel 97-kD Golgi complex autoantigen associated with Sjogren's syndrome. Arthritis Rheum. 40, 1693-1702.
    • (1997) Arthritis Rheum. , vol.40 , pp. 1693-1702
    • Griffith, K.J.1    Chan, E.K.2    Lung, C.C.3    Hamel, J.C.4    Guo, X.5    Miyachi, K.6    Fritzler, M.J.7
  • 23
    • 0034493602 scopus 로고    scopus 로고
    • Dynamics of transitional endoplasmic reticulum sites in vertebrate cells
    • Hammond, A. T. and Glick, B. S. (2000). Dynamics of transitional endoplasmic reticulum sites in vertebrate cells. Mol. Biol. Cell 11, 3013-3030.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3013-3030
    • Hammond, A.T.1    Glick, B.S.2
  • 24
    • 0032489870 scopus 로고    scopus 로고
    • Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein
    • Harada, A., Takei, Y., Kanai, Y., Tanaka, Y., Nonaka, S. and Hirokawa, N. (1998). Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein. J. Cell Biol. 141, 51-59.
    • (1998) J. Cell Biol. , vol.141 , pp. 51-59
    • Harada, A.1    Takei, Y.2    Kanai, Y.3    Tanaka, Y.4    Nonaka, S.5    Hirokawa, N.6
  • 25
    • 0024600674 scopus 로고
    • Reclustering of scattered Golgi elements occurs along microtubules
    • Ho, W. C., Allan, V. J., van Meer, G., Berger, E. G. and Kreis, T. E. (1989). Reclustering of scattered Golgi elements occurs along microtubules. Eur. J. Cell Biol. 48, 250-263.
    • (1989) Eur. J. Cell Biol. , vol.48 , pp. 250-263
    • Ho, W.C.1    Allan, V.J.2    van Meer, G.3    Berger, E.G.4    Kreis, T.E.5
  • 27
    • 0033526005 scopus 로고    scopus 로고
    • GMAP-210, a cis-Golgi network-associated protein, is a minus end microtubule-binding protein
    • Infante, C., Ramos-Morales, F., Fedriani, C., Bornens, M. and Rios, R. M. (1999). GMAP-210, a cis-Golgi network-associated protein, is a minus end microtubule-binding protein. J. Cell Biol. 145, 83-98.
    • (1999) J. Cell Biol. , vol.145 , pp. 83-98
    • Infante, C.1    Ramos-Morales, F.2    Fedriani, C.3    Bornens, M.4    Rios, R.M.5
  • 28
    • 0031890793 scopus 로고    scopus 로고
    • Surfing on a retrograde wave: How does Shiga toxin reach the endoplasmic reticulum?
    • Johannes, L. and Goud, B. (1998). Surfing on a retrograde wave: how does Shiga toxin reach the endoplasmic reticulum? Trends Cell Biol. 8, 158-162.
    • (1998) Trends Cell Biol. , vol.8 , pp. 158-162
    • Johannes, L.1    Goud, B.2
  • 29
    • 3242685944 scopus 로고    scopus 로고
    • Interaction between p230 and MACF1 is associated with transport of a glycosyl pbosphatidyl inositol-anchored protein from the Golgi to the cell periphery
    • Kakinuma, T., Ichikawa, H., Tsukada, Y., Nakamura, T. and Toh, B. K. (2004). Interaction between p230 and MACF1 is associated with transport of a glycosyl pbosphatidyl inositol-anchored protein from the Golgi to the cell periphery. Exp. Cell Res. 298, 388-398.
    • (2004) Exp. Cell Res. , vol.298 , pp. 388-398
    • Kakinuma, T.1    Ichikawa, H.2    Tsukada, Y.3    Nakamura, T.4    Toh, B.K.5
  • 30
    • 0033535542 scopus 로고    scopus 로고
    • A novel Golgi-localisation domain shared by a class of coiled-coil peripheral membrane proteins
    • Kjer-Nielsen, L., Teasdale, R. D., van Vliet, C. and Gleeson, P. A. (1999a). A novel Golgi-localisation domain shared by a class of coiled-coil peripheral membrane proteins. Curr. Biol. 9, 385-388.
    • (1999) Curr. Biol. , vol.9 , pp. 385-388
    • Kjer-Nielsen, L.1    Teasdale, R.D.2    van Vliet, C.3    Gleeson, P.A.4
  • 31
    • 0032981705 scopus 로고    scopus 로고
    • The Golgi targeting sequence of the peripheral membrane protein p230
    • Kjer-Nielsen, L., van Vliet, C., Erlich, R., Toh, B.-H. and Gleeson, P. A. (1999b). The Golgi targeting sequence of the peripheral membrane protein p230. J. Cell Sci. 112, 1645-1654.
    • (1999) J. Cell Sci. , vol.112 , pp. 1645-1654
    • Kjer-Nielsen, L.1    van Vliet, C.2    Erlich, R.3    Toh, B.-H.4    Gleeson, P.A.5
  • 32
    • 0033594080 scopus 로고    scopus 로고
    • Golgi structure in three dimensions: Functional insights from the Normal Rat Kidney cell
    • Ladinsky, M. S., Mastronarde, D. N., McIntosh, J. R., Howell, K. E. and Staehelin, L. A. (1999). Golgi structure in three dimensions: functional insights from the Normal Rat Kidney cell. J. Cell Biol. 144, 1135-1149.
    • (1999) J. Cell Biol. , vol.144 , pp. 1135-1149
    • Ladinsky, M.S.1    Mastronarde, D.N.2    McIntosh, J.R.3    Howell, K.E.4    Staehelin, L.A.5
  • 33
    • 0037017405 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis
    • Lane, J. D., Lucocq, J., Pryde, J., Barr, F. A., Woodman, P. G., Allan, V. J. and Lowe, M. (2002). Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis. J. Cell Biol. 156, 495-509.
    • (2002) J. Cell Biol. , vol.156 , pp. 495-509
    • Lane, J.D.1    Lucocq, J.2    Pryde, J.3    Barr, F.A.4    Woodman, P.G.5    Allan, V.J.6    Lowe, M.7
  • 34
    • 0029904263 scopus 로고    scopus 로고
    • Mutation of the Rab6 homologue of Saccharomyces cerevisiae, YPT6, inhibits both early Golgi function and ribosome biosynthesis
    • Li, B. and Warner, J. R. (1996). Mutation of the Rab6 homologue of Saccharomyces cerevisiae, YPT6, inhibits both early Golgi function and ribosome biosynthesis. J. Biol. Chem. 271, 16813-16819.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16813-16819
    • Li, B.1    Warner, J.R.2
  • 35
    • 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
  • 36
    • 0141856316 scopus 로고    scopus 로고
    • Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97 and golgin-245/p230 onto the Golgi
    • Lu, L. and Hong, W. (2003). Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97 and golgin-245/p230 onto the Golgi. Mol. Biol. Cell 14, 3767-3781.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3767-3781
    • Lu, L.1    Hong, W.2
  • 37
    • 4644352428 scopus 로고    scopus 로고
    • Autoantigen golgin-97, an effector of Arl1 GTPase, participates in traffic from the endosome to the TGN
    • Lu, L., Tai, G. and Hong, W. (2004). Autoantigen golgin-97, an effector of Arl1 GTPase, participates in traffic from the endosome to the TGN. Mol. Biol. Cell 15, 4426-4443.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4426-4443
    • Lu, L.1    Tai, G.2    Hong, W.3
  • 38
    • 0037423287 scopus 로고    scopus 로고
    • GRIP domain-mediated targeting of two new coiled coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network
    • Luke, M. R., Kjer-Nielsen, L., Brown, D. L., Stow, J. L. and Gleeson, P. A. (2003). GRIP domain-mediated targeting of two new coiled coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network. J. Biol. Chem. 278, 4216-4226.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4216-4226
    • Luke, M.R.1    Kjer-Nielsen, L.2    Brown, D.L.3    Stow, J.L.4    Gleeson, P.A.5
  • 39
    • 0032538927 scopus 로고    scopus 로고
    • Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of Shiga toxin B-fragment transport
    • Mallard, F., Antony, C., Tenza, D., Salamero, J., Goud, B. and Johannes, L. (1998). Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of Shiga toxin B-fragment transport. J. Cell Biol. 143, 973-990.
    • (1998) J. Cell Biol. , vol.143 , pp. 973-990
    • Mallard, F.1    Antony, C.2    Tenza, D.3    Salamero, J.4    Goud, B.5    Johannes, L.6
  • 41
    • 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
  • 42
    • 13844317835 scopus 로고    scopus 로고
    • Golgin tethers define subpopulations of COPI vesicles
    • Malsam, J., Satoh, A., Pelletier, L. and Warren, G. (2005). Golgin tethers define subpopulations of COPI vesicles. Science 307, 1095-1098.
    • (2005) Science , vol.307 , pp. 1095-1098
    • Malsam, J.1    Satoh, A.2    Pelletier, L.3    Warren, G.4
  • 43
    • 0036901168 scopus 로고    scopus 로고
    • Endocytosis and sorting of glycosphingolipids in sphingolipid storage disease
    • Marks, D. L. and Pagano, R. E. (2002). Endocytosis and sorting of glycosphingolipids in sphingolipid storage disease. Trends Cell Biol. 12, 605-613.
    • (2002) Trends Cell Biol. , vol.12 , pp. 605-613
    • Marks, D.L.1    Pagano, R.E.2
  • 44
    • 0028820625 scopus 로고
    • A lysosomal targeting signal in the cytoplasmic tail of the β chain directs HLA-DM to the 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 β chain directs HLA-DM to the 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
  • 45
    • 0030003317 scopus 로고    scopus 로고
    • Protein targeting by tyrosine- and di-leucine-based signals: Evidence for distinct saturable components
    • Marks, M. S., Woodruff, L., Ohno, H. and Bonifacino, J. S. (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
  • 46
    • 0035956989 scopus 로고    scopus 로고
    • Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography
    • Marsh, B. J., Mastronarde, D. N., Buttle, K. F., Howell, K. E. and McIntosh, R. J. (2001). Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography. Proc. Natl. Acad. Sci. USA 98, 2399-2406.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2399-2406
    • Marsh, B.J.1    Mastronarde, D.N.2    Buttle, K.F.3    Howell, K.E.4    McIntosh, R.J.5
  • 48
    • 0029088005 scopus 로고
    • Localization of GTPases (GTP-binding proteins) by indirect immunofluorescence and immunoelectron microscopy
    • McCaffery, J. M. and Farquhar, M. G. (1995). Localization of GTPases (GTP-binding proteins) by indirect immunofluorescence and immunoelectron microscopy. Methods Enzymol. 257, 259-279.
    • (1995) Methods Enzymol. , vol.257 , pp. 259-279
    • McCaffery, J.M.1    Farquhar, M.G.2
  • 49
    • 0033535585 scopus 로고    scopus 로고
    • The GRIP domain - A novel Golgi-targeting domain found in several coiled-coil proteins
    • Munro, S. and Nichols, B. J. (1999). The GRIP domain - a novel Golgi-targeting domain found in several coiled-coil proteins. Curr. Biol. 9, 377-380.
    • (1999) Curr. Biol. , vol.9 , pp. 377-380
    • Munro, S.1    Nichols, B.J.2
  • 50
    • 0035104723 scopus 로고    scopus 로고
    • Dynactin-dependent, dynein-driven vesicle transport in the absence of membrane proteins: A role for spectrin and acidic phospholipids
    • Muresan, V., Stankewich, M. C., Steffen, W., Morrow, J. S., Holzbaur, E. L. and Schnapp, B. J. (2001). Dynactin-dependent, dynein-driven vesicle transport in the absence of membrane proteins: a role for spectrin and acidic phospholipids. Mol. Cell 7, 173-183.
    • (2001) Mol. Cell , vol.7 , pp. 173-183
    • Muresan, V.1    Stankewich, M.C.2    Steffen, W.3    Morrow, J.S.4    Holzbaur, E.L.5    Schnapp, B.J.6
  • 51
    • 6344274847 scopus 로고    scopus 로고
    • A cycling cis Golgi protein mediates endosome-to-Golgi traffic
    • Natarajan, R. and Linstedt, A. D. (2004). A cycling cis Golgi protein mediates endosome-to-Golgi traffic. Mol. Biol. Cell 15, 4798-4806.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4798-4806
    • Natarajan, R.1    Linstedt, A.D.2
  • 52
    • 0242266897 scopus 로고    scopus 로고
    • Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus
    • Panic, B., Perisic, O., Veprintsev, D. B., Williams, R. L. and Munro, S. (2003a). Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus. Mol. Cell 12, 863-874.
    • (2003) Mol. Cell , vol.12 , pp. 863-874
    • Panic, B.1    Perisic, O.2    Veprintsev, D.B.3    Williams, R.L.4    Munro, S.5
  • 53
    • 0037418595 scopus 로고    scopus 로고
    • The Arf-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle-tethering factors at the Golgi apparatus
    • Panic, B., Whyte, J. R. C. and Munro, S. (2003b). The Arf-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle-tethering factors at the Golgi apparatus. Curr. Biol. 13, 405-410.
    • (2003) Curr. Biol. , vol.13 , pp. 405-410
    • Panic, B.1    Whyte, J.R.C.2    Munro, S.3
  • 54
    • 0037128212 scopus 로고    scopus 로고
    • CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family
    • Perez, F., Pernet-Gallay, K., Nizak, C., Goodson, H. V., Kreis, T. E. and Goud, B. (2002). CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family. J. Cell Biol. 156, 631-642.
    • (2002) J. Cell Biol. , vol.156 , pp. 631-642
    • Perez, F.1    Pernet-Gallay, K.2    Nizak, C.3    Goodson, H.V.4    Kreis, T.E.5    Goud, B.6
  • 55
    • 0036843024 scopus 로고    scopus 로고
    • The overexpression of GMAP-210 blocks anterograde and retrograde transport between the ER and the Golgi apparatus
    • Pernet-Gallay, K., Antony, C., Johannes, L., Bornens, M., Goud, B. and Rios, R. M. (2002). The overexpression of GMAP-210 blocks anterograde and retrograde transport between the ER and the Golgi apparatus. Traffic 3, 822-832.
    • (2002) Traffic , vol.3 , pp. 822-832
    • Pernet-Gallay, K.1    Antony, C.2    Johannes, L.3    Bornens, M.4    Goud, B.5    Rios, R.M.6
  • 57
    • 0026570788 scopus 로고
    • Perturbation of the morphology of the trans-Golgi network following brefeldin A treatment: Redistribution of a TGN-specific integral membrane protein, TGN38
    • Reaves, B. and Banting, G. (1992). Perturbation of the morphology of the trans-Golgi network following brefeldin A treatment: redistribution of a TGN-specific integral membrane protein, TGN38. J. Cell Biol. 116, 85-94.
    • (1992) J. Cell Biol. , vol.116 , pp. 85-94
    • Reaves, B.1    Banting, G.2
  • 58
    • 0037223631 scopus 로고    scopus 로고
    • The Golgi apparatus at the cell centre
    • Rios, R. M. and Bornens, M. (2003). The Golgi apparatus at the cell centre. Curr. Opin. Cell Biol. 15, 60-66.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 60-66
    • Rios, R.M.1    Bornens, M.2
  • 59
    • 4043107077 scopus 로고    scopus 로고
    • GMAP-210 recruits γ-tubulin complexes to cis-Golgi membranes and is required for Golgi ribbon formation
    • Rios, R. M., Sanchis, A., Tassin, A. M., Fedriani, C. and Bornens, M. (2004). GMAP-210 recruits γ-tubulin complexes to cis-Golgi membranes and is required for Golgi ribbon formation. Cell 118, 323-335.
    • (2004) Cell , vol.118 , pp. 323-335
    • Rios, R.M.1    Sanchis, A.2    Tassin, A.M.3    Fedriani, C.4    Bornens, M.5
  • 60
    • 0021135281 scopus 로고
    • Associations of elements of the Golgi apparatus with microtubules
    • Rogalski, A. A. and Singer, S. J. (1984). Associations of elements of the Golgi apparatus with microtubules. J. Cell Biol. 99, 1092-1100.
    • (1984) J. Cell Biol. , vol.99 , pp. 1092-1100
    • Rogalski, A.A.1    Singer, S.J.2
  • 62
    • 0037010141 scopus 로고    scopus 로고
    • Transport of protein toxins into cells: Pathways used by ricin, cholera toxin and Shiga toxin
    • Sandvig, K. and van Deurs, B. (2002). Transport of protein toxins into cells: pathways used by ricin, cholera toxin and Shiga toxin. FEBS Lett. 529, 49-53.
    • (2002) FEBS Lett. , vol.529 , pp. 49-53
    • Sandvig, K.1    van Deurs, B.2
  • 63
    • 0031669738 scopus 로고    scopus 로고
    • Endocytic clathrin-coated pit formation is independent of receptor internalization signal levels
    • Santini, F., Marks, M. S. and Keen, J. H. (1998). Endocytic clathrin-coated pit formation is independent of receptor internalization signal levels. Mol. Biol. Cell 9, 1177-1194.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1177-1194
    • Santini, F.1    Marks, M.S.2    Keen, J.H.3
  • 64
    • 2442509574 scopus 로고    scopus 로고
    • Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer
    • Seaman, M. N. (2004). Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. J. Cell Biol. 165, 111-122.
    • (2004) J. Cell Biol. , vol.165 , pp. 111-122
    • Seaman, M.N.1
  • 65
    • 0037418580 scopus 로고    scopus 로고
    • Golgi recruitment of GRIP domain proteins by ARF-like GTPase 1 (Arl1p) is regulated by Arf-like GTPase 3 (Arl3p)
    • Setty, S. R. G., Shin, M. E., Yoshino, A., Marks, M. S. and Burd, C. G. (2003). Golgi recruitment of GRIP domain proteins by ARF-like GTPase 1 (Arl1p) is regulated by Arf-like GTPase 3 (Arl3p). Curr. Biol. 13, 401-404.
    • (2003) Curr. Biol. , vol.13 , pp. 401-404
    • Setty, S.R.G.1    Shin, M.E.2    Yoshino, A.3    Marks, M.S.4    Burd, C.G.5
  • 66
    • 0037108473 scopus 로고    scopus 로고
    • The Rab6 GTPase regulates recruitment of the dynactin complex to Golgi membranes
    • Short, B., Preisinger, C., Schaletzky, J., Kopajtich, R. and Barr, F. A. (2002). The Rab6 GTPase regulates recruitment of the dynactin complex to Golgi membranes. Curr. Biol. 12, 1792-1795.
    • (2002) Curr. Biol. , vol.12 , pp. 1792-1795
    • Short, B.1    Preisinger, C.2    Schaletzky, J.3    Kopajtich, R.4    Barr, F.A.5
  • 67
    • 0034665261 scopus 로고    scopus 로고
    • Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on Ypt6p
    • Siniossoglou, S., Peak-Chew, S. Y. and Pelham, H. R. B. (2000). Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on Ypt6p. EMBO J. 19, 4885-4894.
    • (2000) EMBO J. , vol.19 , pp. 4885-4894
    • Siniossoglou, S.1    Peak-Chew, S.Y.2    Pelham, H.R.B.3
  • 69
    • 0032517823 scopus 로고    scopus 로고
    • Recycling of Golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering
    • Storrie, B., White, J., Röttger, S., Stelzer, E. H. K., Suganuma, T. and Nilsson, T. (1998). Recycling of Golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J. Cell Biol. 143, 1505-1521.
    • (1998) J. Cell Biol. , vol.143 , pp. 1505-1521
    • Storrie, B.1    White, J.2    Röttger, S.3    Stelzer, E.H.K.4    Suganuma, T.5    Nilsson, T.6
  • 71
    • 4344599512 scopus 로고    scopus 로고
    • Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in transport from the early/recycling endosome to the TGN
    • Tai, G., Lu, L., Wang, T. L., Tang, B. L., Goud, B., Johannes, L. and Hong, W. (2004). Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in transport from the early/recycling endosome to the TGN. Mol. Biol. Cell 15, 4011-4022.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4011-4022
    • Tai, G.1    Lu, L.2    Wang, T.L.3    Tang, B.L.4    Goud, B.5    Johannes, L.6    Hong, W.7
  • 72
    • 0033546152 scopus 로고    scopus 로고
    • Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the Golgi apparatus
    • Takahashi, M., Shibata, H., Shimakawa, M., Miyamoto, M., Mukai, H. and Ono, Y. (1999). Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the Golgi apparatus. J. Biol. Chem. 274, 17267-17274.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17267-17274
    • Takahashi, M.1    Shibata, H.2    Shimakawa, M.3    Miyamoto, M.4    Mukai, H.5    Ono, Y.6
  • 73
    • 0032948290 scopus 로고    scopus 로고
    • Structural and functional analysis of a novel coiled-coil protein involved in Ypt6 GTPase-regulated protein transport in yeast
    • Tsukada, M., Will, E. and Gallwitz, D. (1999). Structural and functional analysis of a novel coiled-coil protein involved in Ypt6 GTPase-regulated protein transport in yeast. Mol. Biol. Cell 10, 63-75.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 63-75
    • Tsukada, M.1    Will, E.2    Gallwitz, D.3
  • 74
    • 0037012905 scopus 로고    scopus 로고
    • Cell biology. The different hues of lipid rafts
    • van Meer, G. (2002). Cell biology. The different hues of lipid rafts. Science 296, 855-857.
    • (2002) Science , vol.296 , pp. 855-857
    • van Meer, G.1
  • 76
    • 0035809910 scopus 로고    scopus 로고
    • The Golgi-associated Hook3 protein is a member of a novel family of microtubule-binding proteins
    • Walenta, J. H., Didier, A. J., Liu, X. and Kramer, H. (2001). The Golgi-associated Hook3 protein is a member of a novel family of microtubule-binding proteins. J. Cell Biol. 152, 923-934.
    • (2001) J. Cell Biol. , vol.152 , pp. 923-934
    • Walenta, J.H.1    Didier, A.J.2    Liu, X.3    Kramer, H.4
  • 78
    • 0042421854 scopus 로고    scopus 로고
    • Platelet-derived growth factor (PDGF) stimulates glucose transport in 3T3-L1 adipocytes overexpressing PDGF receptor by a pathway independent of insulin receptor substrates
    • Whiteman, E. L., Chen, J. J. and Birnbaum, M. J. (2003). Platelet-derived growth factor (PDGF) stimulates glucose transport in 3T3-L1 adipocytes overexpressing PDGF receptor by a pathway independent of insulin receptor substrates. Endocrinology 144, 3811-3820.
    • (2003) Endocrinology , vol.144 , pp. 3811-3820
    • Whiteman, E.L.1    Chen, J.J.2    Birnbaum, M.J.3
  • 79
    • 0842269776 scopus 로고    scopus 로고
    • Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1
    • Wu, M., Lu, L., Hong, W. and Song, H. (2004). Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1. Nat. Struct. Mol. Biol. 11, 86-94.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 86-94
    • Wu, M.1    Lu, L.2    Hong, W.3    Song, H.4
  • 80
    • 0035073174 scopus 로고    scopus 로고
    • Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle
    • Wu, X., Rao, K., Bowers, M. B., Copeland, N. G., Jenkins, N. A. and Hammer, J. A. (2001). Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle. J. Cell Sci. 114, 1091-1100.
    • (2001) J. Cell Sci. , vol.114 , pp. 1091-1100
    • Wu, X.1    Rao, K.2    Bowers, M.B.3    Copeland, N.G.4    Jenkins, N.A.5    Hammer, J.A.6
  • 81
    • 0037157842 scopus 로고    scopus 로고
    • N. Role of KIFC3 motor protein in Golgi positioning and integration
    • Xu, Y., Takeda, S., Nakata, T., Noda, Y., Tanaka, Y. and Hirokawa, N. (2002). Role of KIFC3 motor protein in Golgi positioning and integration. J. Cell Biol. 158, 293-303.
    • (2002) J. Cell Biol. , vol.158 , pp. 293-303
    • Xu, Y.1    Takeda, S.2    Nakata, T.3    Noda, Y.4    Tanaka, Y.5    Hirokawa6


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