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Volumn , Issue , 2010, Pages

Conserved molecular mechanisms underlying homeostasis of the Golgi complex

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 1; COAT PROTEIN COMPLEX I; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; LIPID; RAB PROTEIN; SNARE PROTEIN;

EID: 78349285565     PISSN: 16878876     EISSN: 16878884     Source Type: Journal    
DOI: 10.1155/2010/758230     Document Type: Review
Times cited : (8)

References (92)
  • 2
    • 26844526297 scopus 로고    scopus 로고
    • Holding it all together? Candidate proteins for the plant Golgi matrix
    • Latijnhouwers M., Hawes C., Carvalho C., Holding it all together? Candidate proteins for the plant Golgi matrix Current Opinion in Plant Biology 2005 8 6 632 639
    • (2005) Current Opinion in Plant Biology , vol.8 , Issue.6 , pp. 632-639
    • Latijnhouwers, M.1    Hawes, C.2    Carvalho, C.3
  • 3
    • 70450223327 scopus 로고    scopus 로고
    • The Golgi apparatus: Lessons from Drosophila
    • Kondylis V., Rabouille C., The Golgi apparatus: lessons from Drosophila FEBS Letters 2009 583 23 3827 3838
    • (2009) FEBS Letters , vol.583 , Issue.23 , pp. 3827-3838
    • Kondylis, V.1    Rabouille, C.2
  • 4
    • 0027056183 scopus 로고
    • Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy
    • Preuss D., Mulholland J., Franzusoff A., Segev N., Botstein D., Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy Molecular Biology of the Cell 1992 3 7 789 803
    • (1992) Molecular Biology of the Cell , vol.3 , Issue.7 , pp. 789-803
    • Preuss, D.1    Mulholland, J.2    Franzusoff, A.3    Segev, N.4    Botstein, D.5
  • 5
    • 0034930079 scopus 로고    scopus 로고
    • Three dimensional configuration of the secretory pathway and segregation of secretion granules in the yeast Saccharomyces cerevisiae
    • Rambourg A., Jackson C. L., Clermont Y., Three dimensional configuration of the secretory pathway and segregation of secretion granules in the yeast Saccharomyces cerevisiae The Journal of Cell Science 2001 114 12 2231 2239
    • (2001) The Journal of Cell Science , vol.114 , Issue.12 , pp. 2231-2239
    • Rambourg, A.1    Jackson, C.L.2    Clermont, Y.3
  • 7
    • 0031665836 scopus 로고    scopus 로고
    • The dynamics of Golgi protein traffic visualized in living yeast cells
    • Wooding S., Pelham H. R. B., The dynamics of Golgi protein traffic visualized in living yeast cells Molecular Biology of the Cell 1998 9 9 2667 2680
    • (1998) Molecular Biology of the Cell , vol.9 , Issue.9 , pp. 2667-2680
    • Wooding, S.1    Pelham, H.R.B.2
  • 8
    • 0035969241 scopus 로고    scopus 로고
    • Evidence that the entire Golgi apparatus cycles in interphase HeLa cells: Sensitivity of Golgi matrix proteins to an ER exit block
    • Miles S., McManus H., Forsten K. E., Storrie B., Evidence that the entire Golgi apparatus cycles in interphase HeLa cells: sensitivity of Golgi matrix proteins to an ER exit block Journal of Cell Biology 2001 155 3 543 555
    • (2001) Journal of Cell Biology , vol.155 , Issue.3 , pp. 543-555
    • Miles, S.1    McManus, H.2    Forsten, K.E.3    Storrie, B.4
  • 11
    • 34248176797 scopus 로고    scopus 로고
    • Mechanisms of COPII vesicle formation and protein sorting
    • Sato K., Nakano A., Mechanisms of COPII vesicle formation and protein sorting FEBS Letters 2007 581 11 2076 2082
    • (2007) FEBS Letters , vol.581 , Issue.11 , pp. 2076-2082
    • Sato, K.1    Nakano, A.2
  • 12
    • 0035889085 scopus 로고    scopus 로고
    • The concept of self-organization in cellular architecture
    • Misteli T., The concept of self-organization in cellular architecture Journal of Cell Biology 2001 155 2 181 185
    • (2001) Journal of Cell Biology , vol.155 , Issue.2 , pp. 181-185
    • Misteli, T.1
  • 14
    • 0033948977 scopus 로고    scopus 로고
    • Organization of the Golgi apparatus
    • Glick B. S., Organization of the Golgi apparatus Current Opinion in Cell Biology 2000 12 4 450 456
    • (2000) Current Opinion in Cell Biology , vol.12 , Issue.4 , pp. 450-456
    • Glick, B.S.1
  • 16
    • 33847208186 scopus 로고    scopus 로고
    • Conservation of the TRAPPII-specific subunits of a Ypt/Rab exchanger complex
    • Cox R., Chen S. H., Yoo E., Segev N., Conservation of the TRAPPII-specific subunits of a Ypt/Rab exchanger complex BMC Evolutionary Biology 2007 7, article 12
    • (2007) BMC Evolutionary Biology , vol.712
    • Cox, R.1    Chen, S.H.2    Yoo, E.3    Segev, N.4
  • 18
    • 0033984895 scopus 로고    scopus 로고
    • Organization of the yeast Golgi complex into at least four funtionally distinct compartments
    • Brigance W. T., Barlowe C., Graham T. R., Organization of the yeast Golgi complex into at least four funtionally distinct compartments Molecular Biology of the Cell 2000 11 1 171 182
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.1 , pp. 171-182
    • Brigance, W.T.1    Barlowe, C.2    Graham, T.R.3
  • 19
    • 0035827374 scopus 로고    scopus 로고
    • What can yeast tell us about N-linked glycosylation in the Golgi apparatus?
    • Munro S., What can yeast tell us about N-linked glycosylation in the Golgi apparatus? FEBS Letters 2001 498 2-3 223 227
    • (2001) FEBS Letters , vol.498 , Issue.23 , pp. 223-227
    • Munro, S.1
  • 20
    • 0034697118 scopus 로고    scopus 로고
    • Medial Golgi but not late golgi glycosyltransferases exist as high molecular weight complexes. Role of luminal domain in complex formation and localization
    • Opat A. S., Houghton F., Gleeson P. A., Medial Golgi but not late golgi glycosyltransferases exist as high molecular weight complexes. Role of luminal domain in complex formation and localization The Journal of Biological Chemistry 2000 275 16 11836 11845
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.16 , pp. 11836-11845
    • Opat, A.S.1    Houghton, F.2    Gleeson, P.A.3
  • 22
    • 0037168471 scopus 로고    scopus 로고
    • Biosynthesis and trafficking of sphingolipids in the yeast Saccharomyces cerevisiae
    • Funato K., Valle B., Riezman H., Biosynthesis and trafficking of sphingolipids in the yeast Saccharomyces cerevisiae Biochemistry 2002 41 51 15105 15114
    • (2002) Biochemistry , vol.41 , Issue.51 , pp. 15105-15114
    • Funato, K.1    Valle, B.2    Riezman, H.3
  • 25
    • 72749086098 scopus 로고    scopus 로고
    • Evolutionary conservation and adaptation in the mechanism that regulates SREBP action: What a long, strange tRIP it's been
    • Osborne T. F., Espenshade P. J., Evolutionary conservation and adaptation in the mechanism that regulates SREBP action: what a long, strange tRIP it's been Genes and Development 2009 23 22 2578 2591
    • (2009) Genes and Development , vol.23 , Issue.22 , pp. 2578-2591
    • Osborne, T.F.1    Espenshade, P.J.2
  • 26
    • 70349333981 scopus 로고    scopus 로고
    • Regulation of Golgi function via phosphoinositide lipids
    • Mayinger P., Regulation of Golgi function via phosphoinositide lipids Seminars in Cell and Developmental Biology 2009 20 7 793 800
    • (2009) Seminars in Cell and Developmental Biology , vol.20 , Issue.7 , pp. 793-800
    • Mayinger, P.1
  • 27
    • 7044274618 scopus 로고    scopus 로고
    • Protein-lipid interactions in membrane trafficking at the Golgi complex
    • De Matteis M. A., Godi A., Protein-lipid interactions in membrane trafficking at the Golgi complex Biochimica et Biophysica Acta 2004 1666 1-2 264 274
    • (2004) Biochimica et Biophysica Acta , vol.1666 , Issue.12 , pp. 264-274
    • De Matteis, M.A.1    Godi, A.2
  • 29
    • 47749141468 scopus 로고    scopus 로고
    • Signal-mediated dynamic retention of glycosyltransferases in the Golgi
    • Tu L., Tai W. C. S., Chen L., Banfield D. K., Signal-mediated dynamic retention of glycosyltransferases in the Golgi Science 2008 321 5887 404 407
    • (2008) Science , vol.321 , Issue.5887 , pp. 404-407
    • Tu, L.1    Tai, W.C.S.2    Chen, L.3    Banfield, D.K.4
  • 30
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher M. S., Munro S., Cholesterol and the Golgi apparatus Science 1993 261 5126 1280 1281
    • (1993) Science , vol.261 , Issue.5126 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 31
    • 0027997974 scopus 로고
    • Localization of Sed5, a putative vesicle targeting molecule, to the cis- Golgi network involves both its transmembrane and cytoplasmic domains
    • Banfield D. K., Lewis M. J., Rabouille C., Warren G., Pelham H. R. B., Localization of Sed5, a putative vesicle targeting molecule, to the cis- Golgi network involves both its transmembrane and cytoplasmic domains Journal of Cell Biology 1994 127 2 357 371
    • (1994) Journal of Cell Biology , vol.127 , Issue.2 , pp. 357-371
    • Banfield, D.K.1    Lewis, M.J.2    Rabouille, C.3    Warren, G.4    Pelham, H.R.B.5
  • 32
    • 0030945486 scopus 로고    scopus 로고
    • Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast
    • Rayner J. C., Pelham H. R. B., Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast The EMBO Journal 1997 16 8 1832 1841
    • (1997) The EMBO Journal , vol.16 , Issue.8 , pp. 1832-1841
    • Rayner, J.C.1    Pelham, H.R.B.2
  • 34
    • 0037339478 scopus 로고    scopus 로고
    • Cholesterol-induced protein sorting: An analysis of energetic feasibility
    • Lundbk J. A., Andersen O. S., Werge T., Nielsen C., Cholesterol-induced protein sorting: an analysis of energetic feasibility Biophysical Journal 2003 84 3 2080 2089
    • (2003) Biophysical Journal , vol.84 , Issue.3 , pp. 2080-2089
    • Lundbk, J.A.1    Andersen, O.S.2    Werge, T.3    Nielsen, C.4
  • 35
    • 33846826956 scopus 로고    scopus 로고
    • Insight into the putative specific interactions between cholesterol, sphingomyelin, and palmitoyl-oleoyl phosphatidylcholine
    • Aittoniemi J., Niemel P. S., Hyvnen M. T., Karttunen M., Vattulainen I., Insight into the putative specific interactions between cholesterol, sphingomyelin, and palmitoyl-oleoyl phosphatidylcholine Biophysical Journal 2007 92 4 1125 1137
    • (2007) Biophysical Journal , vol.92 , Issue.4 , pp. 1125-1137
    • Aittoniemi, J.1    Niemel, P.S.2    Hyvnen, M.T.3    Karttunen, M.4    Vattulainen, I.5
  • 36
    • 0034844091 scopus 로고    scopus 로고
    • Trafficking and localisation of resident Golgi glycosylation enzymes
    • Opat A. S., van Vliet C., Gleeson P. A., Trafficking and localisation of resident Golgi glycosylation enzymes Biochimie 2001 83 8 763 773
    • (2001) Biochimie , vol.83 , Issue.8 , pp. 763-773
    • Opat, A.S.1    Van Vliet, C.2    Gleeson, P.A.3
  • 37
    • 0033579467 scopus 로고    scopus 로고
    • The cytoplasmic, transmembrane, and stem regions of glycosyltransferases specify their in vivo functional sublocalization and stability in the Golgi
    • Grabenhorst E., Conradt H. S., The cytoplasmic, transmembrane, and stem regions of glycosyltransferases specify their in vivo functional sublocalization and stability in the Golgi The Journal of Biological Chemistry 1999 274 51 36107 36116
    • (1999) The Journal of Biological Chemistry , vol.274 , Issue.51 , pp. 36107-36116
    • Grabenhorst, E.1    Conradt, H.S.2
  • 38
    • 0034607646 scopus 로고    scopus 로고
    • Formation of insoluble oligomers correlates with ST6Gal i stable localization in the Golgi
    • Chen C., Ma J., Lazic A., Backovic M., Colley K. J., Formation of insoluble oligomers correlates with ST6Gal I stable localization in the Golgi The Journal of Biological Chemistry 2000 275 18 13819 13826
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.18 , pp. 13819-13826
    • Chen, C.1    Ma, J.2    Lazic, A.3    Backovic, M.4    Colley, K.J.5
  • 44
    • 0033568607 scopus 로고    scopus 로고
    • GTP hydrolysis by arf-1 mediates sorting and concentration of Golgi resident enzymes into functional COP i vesicles
    • Lanoix J., Ouwendijk J., Chung-Chih L., Stark A., Love H. D., Ostermann J., Nilsson T., GTP hydrolysis by arf-1 mediates sorting and concentration of Golgi resident enzymes into functional COP I vesicles The EMBO Journal 1999 18 18 4935 4948
    • (1999) The EMBO Journal , vol.18 , Issue.18 , pp. 4935-4948
    • Lanoix, J.1    Ouwendijk, J.2    Chung-Chih, L.3    Stark, A.4    Love, H.D.5    Ostermann, J.6    Nilsson, T.7
  • 46
    • 0035945348 scopus 로고    scopus 로고
    • Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport
    • Martnez-Menrguez J. A., Prekeris R., Oorschot V. M. J., Scheller R., Slot J. W., Geuze H. J., Klumperman J., Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport Journal of Cell Biology 2001 155 7 1213 1224
    • (2001) Journal of Cell Biology , vol.155 , Issue.7 , pp. 1213-1224
    • Martnez-Menrguez, J.A.1    Prekeris, R.2    Oorschot, V.M.J.3    Scheller, R.4    Slot, J.W.5    Geuze, H.J.6    Klumperman, J.7
  • 47
    • 13844317835 scopus 로고    scopus 로고
    • Golgin tethers define subpopulations of COPI vesicles
    • Malsam J., Satoh A., Pelletier L., Warren G., Golgin tethers define subpopulations of COPI vesicles Science 2005 307 5712 1095 1098
    • (2005) Science , vol.307 , Issue.5712 , pp. 1095-1098
    • Malsam, J.1    Satoh, A.2    Pelletier, L.3    Warren, G.4
  • 53
    • 67749129161 scopus 로고    scopus 로고
    • Lysophosphatidic acid acyltransferase 3 regulates Golgi complex structure and function
    • Schmidt J. A., Brown W. J., Lysophosphatidic acid acyltransferase 3 regulates Golgi complex structure and function Journal of Cell Biology 2009 186 2 211 218
    • (2009) Journal of Cell Biology , vol.186 , Issue.2 , pp. 211-218
    • Schmidt, J.A.1    Brown, W.J.2
  • 54
    • 33947228452 scopus 로고    scopus 로고
    • Low-temperature-induced Golgi tubules are transient membranes enriched in molecules regulating intra-Golgi transport
    • Martnez-Alonso E., Ballesta J., Martnez-Menrguez J. A., Low-temperature-induced Golgi tubules are transient membranes enriched in molecules regulating intra-Golgi transport Traffic 2007 8 4 359 368
    • (2007) Traffic , vol.8 , Issue.4 , pp. 359-368
    • Martnez-Alonso, E.1    Ballesta, J.2    Martnez-Menrguez, J.A.3
  • 60
    • 0036151274 scopus 로고    scopus 로고
    • Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different golgi compartments: Evidence for distinct functions in protein traffic
    • Zhao X., Lasell T. K. R., Melanon P., Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different golgi compartments: evidence for distinct functions in protein traffic Molecular Biology of the Cell 2002 13 1 119 133
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.1 , pp. 119-133
    • Zhao, X.1    Lasell, T.K.R.2    Melanon, P.3
  • 62
    • 69249213354 scopus 로고    scopus 로고
    • The COPI system: Molecular mechanisms and function
    • Beck R., Rawet M., Wieland F. T., Cassel D., The COPI system: molecular mechanisms and function FEBS Letters 2009 583 2701 2709
    • (2009) FEBS Letters , vol.583 , Issue.2701 , pp. 2709
    • Beck, R.1    Rawet, M.2    Wieland, F.T.3    Cassel, D.4
  • 64
    • 0034604293 scopus 로고    scopus 로고
    • Role of coatormer and phospholipids in GTPase-activating protein-dependent hydrolysis of GTP by ADP-ribosylation factor-1
    • Szafer E., Pick E., Rotman M., Zuck S., Huber I., Cassel D., Role of coatormer and phospholipids in GTPase-activating protein-dependent hydrolysis of GTP by ADP-ribosylation factor-1 The Journal of Biological Chemistry 2000 275 31 23615 23619
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.31 , pp. 23615-23619
    • Szafer, E.1    Pick, E.2    Rotman, M.3    Zuck, S.4    Huber, I.5    Cassel, D.6
  • 65
    • 0029968296 scopus 로고    scopus 로고
    • Phosphoinositides as regulators in membrane traffic
    • De Camilli P., Emr S. D., McPherson P. S., Novick P., Phosphoinositides as regulators in membrane traffic Science 1996 271 5255 1533 1539
    • (1996) Science , vol.271 , Issue.5255 , pp. 1533-1539
    • De Camilli, P.1    Emr, S.D.2    McPherson, P.S.3    Novick, P.4
  • 66
    • 0037193471 scopus 로고    scopus 로고
    • ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat
    • Rein U., Andag U., Duden R., Schmitt H. D., Spang A., ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat Journal of Cell Biology 2002 157 3 395 404
    • (2002) Journal of Cell Biology , vol.157 , Issue.3 , pp. 395-404
    • Rein, U.1    Andag, U.2    Duden, R.3    Schmitt, H.D.4    Spang, A.5
  • 68
    • 34547801651 scopus 로고    scopus 로고
    • Interaction of SNAREs with ArfGAPs precedes recruitment of Sec18p/NSF
    • Schindler C., Spang A., Interaction of SNAREs with ArfGAPs precedes recruitment of Sec18p/NSF Molecular Biology of the Cell 2007 18 8 2852 2863
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.8 , pp. 2852-2863
    • Schindler, C.1    Spang, A.2
  • 70
    • 0037193471 scopus 로고    scopus 로고
    • ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat
    • Rein U., Andag U., Duden R., Schmitt H. D., Spang A., ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat Journal of Cell Biology 2002 157 3 395 404
    • (2002) Journal of Cell Biology , vol.157 , Issue.3 , pp. 395-404
    • Rein, U.1    Andag, U.2    Duden, R.3    Schmitt, H.D.4    Spang, A.5
  • 73
    • 0029898287 scopus 로고    scopus 로고
    • Transport of an external Lys-Asp-Glu-Leu (KDEL) protein from the plasma membrane to the endoplasmic reticulum: Studies with cholera toxin in Vero cells
    • Majoul I. V., Bastiaens P. I. H., Sling H.-D., Transport of an external Lys-Asp-Glu-Leu (KDEL) protein from the plasma membrane to the endoplasmic reticulum: studies with cholera toxin in Vero cells Journal of Cell Biology 1996 133 4 777 789
    • (1996) Journal of Cell Biology , vol.133 , Issue.4 , pp. 777-789
    • Majoul, I.V.1    Bastiaens, P.I.H.2    Sling, H.-D.3
  • 76
    • 70350378203 scopus 로고    scopus 로고
    • The COG complex, Rab6 and COPI define a novel golgi retrograde trafficking pathway that is exploited by SubAB toxin
    • Smith R. D., Willett R., Kudlyk T., Pokrovskaya I., Paton A. W., Paton J. C., Lupashin V. V., The COG complex, Rab6 and COPI define a novel golgi retrograde trafficking pathway that is exploited by SubAB toxin Traffic 2009 10 10 1502 1517
    • (2009) Traffic , vol.10 , Issue.10 , pp. 1502-1517
    • Smith, R.D.1    Willett, R.2    Kudlyk, T.3    Pokrovskaya, I.4    Paton, A.W.5    Paton, J.C.6    Lupashin, V.V.7
  • 77
    • 0027095750 scopus 로고
    • The small GTP-binding protein rab6p is distributed from medial Golgi to the trans-Golgi network as determined by a confocal microscopic approach
    • Antony C., Cibert C., Geraud G., Santa Maria A., Maro B., Mayau V., Goud B., The small GTP-binding protein rab6p is distributed from medial Golgi to the trans-Golgi network as determined by a confocal microscopic approach Journal of Cell Science 1992 103 3 785 796
    • (1992) Journal of Cell Science , vol.103 , Issue.3 , pp. 785-796
    • Antony, C.1    Cibert, C.2    Geraud, G.3    Santa Maria, A.4    Maro, B.5    Mayau, V.6    Goud, B.7
  • 78
    • 34948888155 scopus 로고    scopus 로고
    • Rab6 regulates both ZW10/RINT-1- and conserved oligomeric Golgi complex-dependent Golgi trafficking and homeostasis
    • Sun Y., Shestakova A., Hunt L., Sehgal S., Lupashin V., Storrie B., Rab6 regulates both ZW10/RINT-1- and conserved oligomeric Golgi complex-dependent Golgi trafficking and homeostasis Molecular Biology of the Cell 2007 18 10 4129 4142
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.10 , pp. 4129-4142
    • Sun, Y.1    Shestakova, A.2    Hunt, L.3    Sehgal, S.4    Lupashin, V.5    Storrie, B.6
  • 79
    • 0035489304 scopus 로고    scopus 로고
    • The Sec34/35 Golgi Transport Complex Is Related to the Exocyst, Defining a Family of Complexes Involved in Multiple Steps of Membrane Traffic
    • Whyte J. R. C., Munro S., The Sec34/35 Golgi Transport Complex Is Related to the Exocyst, Defining a Family of Complexes Involved in Multiple Steps of Membrane Traffic Developmental Cell 2001 1 4 527 537
    • (2001) Developmental Cell , vol.1 , Issue.4 , pp. 527-537
    • Whyte, J.R.C.1    Munro, S.2
  • 80
    • 0037428439 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for the involvement of yeast Ypt6-GTPase in protein retrieval to different Golgi compartments
    • Luo Z., Gallwitz D., Biochemical and genetic evidence for the involvement of yeast Ypt6-GTPase in protein retrieval to different Golgi compartments The Journal of Biological Chemistry 2003 278 2 791 799
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.2 , pp. 791-799
    • Luo, Z.1    Gallwitz, D.2
  • 82
    • 4544237449 scopus 로고    scopus 로고
    • Retrograde transport of the mannosyltransferase Och1p to the early Golgi requires a component of the COG transport complex
    • Bruinsma P., Spelbrink R. G., Nothwehr S. F., Retrograde transport of the mannosyltransferase Och1p to the early Golgi requires a component of the COG transport complex The Journal of Biological Chemistry 2004 279 38 39814 39823
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.38 , pp. 39814-39823
    • Bruinsma, P.1    Spelbrink, R.G.2    Nothwehr, S.F.3
  • 83
    • 33645131266 scopus 로고    scopus 로고
    • COG complex-mediated recycling of golgi glycosyltransferases is essential for normal protein glycosylation
    • Shestakova A., Zolov S., Lupashin V., COG complex-mediated recycling of golgi glycosyltransferases is essential for normal protein glycosylation Traffic 2006 7 2 191 204
    • (2006) Traffic , vol.7 , Issue.2 , pp. 191-204
    • Shestakova, A.1    Zolov, S.2    Lupashin, V.3
  • 84
    • 45049084097 scopus 로고    scopus 로고
    • Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation
    • Smith R. D., Lupashin V. V., Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation Carbohydrate Research 2008 343 12 2024 2031
    • (2008) Carbohydrate Research , vol.343 , Issue.12 , pp. 2024-2031
    • Smith, R.D.1    Lupashin, V.V.2
  • 85
    • 33745372525 scopus 로고    scopus 로고
    • COG-7-deficient human fibroblasts exhibit altered recycling of Golgi proteins
    • Steet R., Kornfeld S., COG-7-deficient human fibroblasts exhibit altered recycling of Golgi proteins Molecular Biology of the Cell 2006 17 5 2312 2321
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.5 , pp. 2312-2321
    • Steet, R.1    Kornfeld, S.2
  • 86
    • 0037071543 scopus 로고    scopus 로고
    • The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins
    • Suvorova E. S., Duden R., Lupashin V. V., The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins Journal of Cell Biology 2002 157 4 631 643
    • (2002) Journal of Cell Biology , vol.157 , Issue.4 , pp. 631-643
    • Suvorova, E.S.1    Duden, R.2    Lupashin, V.V.3
  • 87
    • 37249008781 scopus 로고    scopus 로고
    • Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability
    • Shestakova A., Suvorova E., Pavliv O., Khaidakova G., Lupashin V., Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability Journal of Cell Biology 2007 179 6 1179 1192
    • (2007) Journal of Cell Biology , vol.179 , Issue.6 , pp. 1179-1192
    • Shestakova, A.1    Suvorova, E.2    Pavliv, O.3    Khaidakova, G.4    Lupashin, V.5
  • 88
  • 90
    • 13844252065 scopus 로고    scopus 로고
    • Generation of nonidentical compartments in vesicular transport systems
    • Heinrich R., Rapoport T. A., Generation of nonidentical compartments in vesicular transport systems Journal of Cell Biology 2005 168 2 271 280
    • (2005) Journal of Cell Biology , vol.168 , Issue.2 , pp. 271-280
    • Heinrich, R.1    Rapoport, T.A.2
  • 91
    • 50349099884 scopus 로고    scopus 로고
    • Simulated de novo assembly of Golgi compartments by selective cargo capture during vesicle budding and targeted vesicle fusion
    • Gong H., Sengupta D., Linstedt A. D., Schwartz R., Simulated de novo assembly of Golgi compartments by selective cargo capture during vesicle budding and targeted vesicle fusion Biophysical Journal 2008 95 4 1674 1688
    • (2008) Biophysical Journal , vol.95 , Issue.4 , pp. 1674-1688
    • Gong, H.1    Sengupta, D.2    Linstedt, A.D.3    Schwartz, R.4
  • 92


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