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Volumn 13, Issue 3, 2012, Pages 416-432

Live-Cell Assays to Identify Regulators of ER-to-Golgi Trafficking

Author keywords

BFA; ER to Golgi trafficking; GalT; GOT1B; SACM1L; USE1; YIPF

Indexed keywords

BREFELDIN A; GALACTOSYLTRANSFERASE; HYBRID PROTEIN;

EID: 84856772585     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2011.01318.x     Document Type: Article
Times cited : (11)

References (115)
  • 2
    • 77949375577 scopus 로고    scopus 로고
    • The Golgi and the centrosome: building a functional partnership
    • 10.1083/jcb.200910001.
    • Sütterlin C, Colanzi A. The Golgi and the centrosome: building a functional partnership. J Cell Biol 2010;188:621-628. 10.1083/jcb.200910001.
    • (2010) J Cell Biol , vol.188 , pp. 621-628
    • Sütterlin, C.1    Colanzi, A.2
  • 3
    • 72249094196 scopus 로고    scopus 로고
    • Metabolism, cell surface organization, and disease
    • 10.1016/j.cell.2009.12.008.
    • Dennis JW, Nabi IR, Demetriou M. Metabolism, cell surface organization, and disease. Cell 2009;139:1229-1241. 10.1016/j.cell.2009.12.008.
    • (2009) Cell , vol.139 , pp. 1229-1241
    • Dennis, J.W.1    Nabi, I.R.2    Demetriou, M.3
  • 4
    • 70450223327 scopus 로고    scopus 로고
    • The Golgi apparatus: lessons from Drosophila
    • 10.1016/j.febslet.2009.09.048.
    • Kondylis V, Rabouille C. The Golgi apparatus: lessons from Drosophila. FEBS Lett 2009;583:3827-3838. 10.1016/j.febslet.2009.09.048.
    • (2009) FEBS Lett , vol.583 , pp. 3827-3838
    • Kondylis, V.1    Rabouille, C.2
  • 6
    • 20544435937 scopus 로고    scopus 로고
    • Golgi structure in stress sensing and apoptosis
    • 10.1016/j.bbamcr.2005.03.002.
    • Hicks SW, Machamer CE. Golgi structure in stress sensing and apoptosis. Biochimica et Biophysica Acta 2005;1744:406-414. 10.1016/j.bbamcr.2005.03.002.
    • (2005) Biochimica et Biophysica Acta , vol.1744 , pp. 406-414
    • Hicks, S.W.1    Machamer, C.E.2
  • 7
    • 0036790319 scopus 로고    scopus 로고
    • The mammalian Golgi-complex debates
    • 10.1038/nrm933.
    • Marsh BJ, Howell KE. The mammalian Golgi-complex debates. Nat Rev Mol Cell Biol 2002;3:789-795. 10.1038/nrm933.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 789-795
    • Marsh, B.J.1    Howell, K.E.2
  • 8
    • 63049118188 scopus 로고    scopus 로고
    • Correlation of 4Pi and electron microscopy to study transport through single Golgi stacks in living cells with super resolution
    • 10.1111/j.2009.00875.x.
    • Perinetti G, Müller T, Spaar A, Polishchuk R, Luini A, Egner A. Correlation of 4Pi and electron microscopy to study transport through single Golgi stacks in living cells with super resolution. Traffic 2009;10:379-391. 10.1111/j.2009.00875.x.
    • (2009) Traffic , vol.10 , pp. 379-391
    • Perinetti, G.1    Müller, T.2    Spaar, A.3    Polishchuk, R.4    Luini, A.5    Egner, A.6
  • 9
    • 42649098249 scopus 로고    scopus 로고
    • Golgi apparatus studied in vitreous sections
    • doi:10.1111/j1365-28182008.01988.x.
    • Bouchet-Marquis C, Starkuviene V, Grabenbauer M. Golgi apparatus studied in vitreous sections. J Microscopy 2008;230:308-316. doi:10.1111/j1365-28182008.01988.x.
    • (2008) J Microscopy , vol.230 , pp. 308-316
    • Bouchet-Marquis, C.1    Starkuviene, V.2    Grabenbauer, M.3
  • 10
    • 33947096851 scopus 로고    scopus 로고
    • Three-dimensional ultrastructure of the Golgi apparatus in different cells: high-resolution scanning electron microscopy of osmium-macerated tissues
    • 10.1679/aohc.69.357.
    • Koga D, Ushiki T. Three-dimensional ultrastructure of the Golgi apparatus in different cells: high-resolution scanning electron microscopy of osmium-macerated tissues. Arch Histol Cytol 2006;69:357-374. 10.1679/aohc.69.357.
    • (2006) Arch Histol Cytol , vol.69 , pp. 357-374
    • Koga, D.1    Ushiki, T.2
  • 12
    • 1842681953 scopus 로고    scopus 로고
    • Direct continuities between cisternae at different levels of the Golgi complex in glucose-stimulated mouse islet beta cells
    • 10.1073/pnas.0401242101.
    • Marsh BJ, Volkmann N, McIntosh JR, Howell KE. Direct continuities between cisternae at different levels of the Golgi complex in glucose-stimulated mouse islet beta cells. Proc Natl Acad Sci U S A 2004;101:5565-5570. 10.1073/pnas.0401242101.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 5565-5570
    • Marsh, B.J.1    Volkmann, N.2    McIntosh, J.R.3    Howell, K.E.4
  • 13
    • 1942487246 scopus 로고    scopus 로고
    • 4Pi-microscopy of the Golgi apparatus in live mammalian cells
    • 10.1016/j.jsb.2003.10.006.
    • Egner A, Verrier S, Goroshkov A, Söling H-D, Hell SW. 4Pi-microscopy of the Golgi apparatus in live mammalian cells. J Struct Biol 2004;147:70-76. 10.1016/j.jsb.2003.10.006.
    • (2004) J Struct Biol , vol.147 , pp. 70-76
    • Egner, A.1    Verrier, S.2    Goroshkov, A.3    Söling, H.-D.4    Hell, S.W.5
  • 14
    • 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
    • 10.1073/pnas.051631998.
    • Marsh BJ, Mastronarde DN, Buttle KF, Howell KE, McIntosh JR. Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography. Proc Natl Acad Sci U S A 2001;98:2399-2406. 10.1073/pnas.051631998.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 2399-2406
    • Marsh, B.J.1    Mastronarde, D.N.2    Buttle, K.F.3    Howell, K.E.4    McIntosh, J.R.5
  • 15
    • 0033594080 scopus 로고    scopus 로고
    • Golgi structure in three dimensions: functional insights from the normal rat kidney cell
    • 10.1083/jcb.144.6.1135.
    • Ladinsky MS, Mastronarde DN, McIntosh JR, Howell KE, Staehelin LA. Golgi structure in three dimensions: functional insights from the normal rat kidney cell. J Cell Biol 1999;144:1135-1149. 10.1083/jcb.144.6.1135.
    • (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
  • 16
    • 0033572579 scopus 로고    scopus 로고
    • Three-dimensional visualization of the Golgi apparatus: observation of Brunner's gland cells by a confocal laser scanning microscope
    • 10.1006/jsbi.1999.4175.
    • Suzaki E, Kataoka K. Three-dimensional visualization of the Golgi apparatus: observation of Brunner's gland cells by a confocal laser scanning microscope. JStruct Biol 1999;128:131-138. 10.1006/jsbi.1999.4175.
    • (1999) JStruct Biol , vol.128 , pp. 131-138
    • Suzaki, E.1    Kataoka, K.2
  • 17
    • 0025233925 scopus 로고
    • Three-dimensional electron microscopy: structure of the Golgi apparatus
    • Rambourg A, Clermont Y. Three-dimensional electron microscopy: structure of the Golgi apparatus. Eur J Cell Biol 1990;51:189-200.
    • (1990) Eur J Cell Biol , vol.51 , pp. 189-200
    • Rambourg, A.1    Clermont, Y.2
  • 18
    • 0014225557 scopus 로고
    • The Golgi apparatus: structure and function
    • Beams HW, Kessel RG. The Golgi apparatus: structure and function. Int Rev Cytol 1968;23:209-276.
    • (1968) Int Rev Cytol , vol.23 , pp. 209-276
    • Beams, H.W.1    Kessel, R.G.2
  • 19
    • 0000260364 scopus 로고
    • An observation on the functioning of the Golgi apparatus
    • 10.1083/jcb.17.1.222.
    • Mollenhayer HH, Whaley WG. An observation on the functioning of the Golgi apparatus. J Cell Biol 1963;17:222-225. 10.1083/jcb.17.1.222.
    • (1963) J Cell Biol , vol.17 , pp. 222-225
    • Mollenhayer, H.H.1    Whaley, W.G.2
  • 20
    • 41149148605 scopus 로고    scopus 로고
    • Exiting the Golgi complex
    • 10.1038/nrm2378.
    • De Matteis MA, Luini A. Exiting the Golgi complex. Nat Rev Mol Cell Biol 2008;9:273-284. 10.1038/nrm2378.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 273-284
    • De Matteis, M.A.1    Luini, A.2
  • 21
    • 18244365900 scopus 로고    scopus 로고
    • Maintenance of Golgi apparatus structure in the face of continuous protein recycling to the endoplasmic reticulum: making ends meet
    • 10.1016/S0074-7696.(05)
    • Storrie B. Maintenance of Golgi apparatus structure in the face of continuous protein recycling to the endoplasmic reticulum: making ends meet. Int Rev Cytol 2005;244:69-94. 10.1016/S0074-7696.(05)
    • (2005) Int Rev Cytol , vol.244 , pp. 69-94
    • Storrie, B.1
  • 22
    • 8444242974 scopus 로고    scopus 로고
    • Bi-directional protein transport between the ER and Golgi
    • 10.1146/annurev.cellbio.20.010403.105307.
    • Lee MCS, Miller EA, Goldberg J, Orci L, Schekman R. Bi-directional protein transport between the ER and Golgi. Ann Rev Cell Dev Biol 2004;20:87-123. 10.1146/annurev.cellbio.20.010403.105307.
    • (2004) Ann Rev Cell Dev Biol , vol.20 , pp. 87-123
    • Lee, M.C.S.1    Miller, E.A.2    Goldberg, J.3    Orci, L.4    Schekman, R.5
  • 23
    • 79952034405 scopus 로고    scopus 로고
    • Identification of ER proteins involved in the functional organisation of the early secretory pathway in Drosophila cells by a targeted RNAi screen
    • 10.1371/journal.pone.0017173.
    • Kondylis V, Tang Y, Fuchs F, Boutros M, Rabouille C. Identification of ER proteins involved in the functional organisation of the early secretory pathway in Drosophila cells by a targeted RNAi screen. PLoS One 2011;6:e17173. 10.1371/journal.pone.0017173.
    • (2011) PLoS One , vol.6
    • Kondylis, V.1    Tang, Y.2    Fuchs, F.3    Boutros, M.4    Rabouille, C.5
  • 25
    • 51849142293 scopus 로고    scopus 로고
    • Deciphering the Golgi apparatus: from imaging to genes
    • 10.1111/j.2008.00769.x.
    • Boulaflous A, Faso C, Brandizzi F. Deciphering the Golgi apparatus: from imaging to genes. Traffic 2008;9:1613-1617. 10.1111/j.2008.00769.x.
    • (2008) Traffic , vol.9 , pp. 1613-1617
    • Boulaflous, A.1    Faso, C.2    Brandizzi, F.3
  • 28
    • 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
    • 10.1083/jcb.143.6.1505.
    • Storrie B, White J, Röttger S, Stelzer EH, Suganuma T, Nilsson T. Recycling of Golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J Cell Biol 1998;143:1505-1521. 10.1083/jcb.143.6.1505.
    • (1998) J Cell Biol , vol.143 , pp. 1505-1521
    • Storrie, B.1    White, J.2    Röttger, S.3    Stelzer, E.H.4    Suganuma, T.5    Nilsson, T.6
  • 29
    • 0029972823 scopus 로고    scopus 로고
    • Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites
    • Cole NB, Sciaky N, Marotta A, Song J, Lippincott-Schwartz J. Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites. Mol Biol Cell 1996;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
  • 30
    • 33748313053 scopus 로고    scopus 로고
    • Capacity of the Golgi apparatus for cargo transport prior to complete assembly
    • 10.1091/mbc.E05-12-1112.
    • Jiang S, Rhee SW, Gleeson PA, Storrie B. Capacity of the Golgi apparatus for cargo transport prior to complete assembly. Mol Biol Cell 2006;17:4105-4117. 10.1091/mbc.E05-12-1112.
    • (2006) Mol Biol Cell , vol.17 , pp. 4105-4117
    • Jiang, S.1    Rhee, S.W.2    Gleeson, P.A.3    Storrie, B.4
  • 31
    • 0345306582 scopus 로고    scopus 로고
    • Capacity of the Golgi apparatus for biogenesis from the endoplasmic reticulum
    • 10.1091/mbc.E03-06-0437.
    • Puri S, Linstedt AD. Capacity of the Golgi apparatus for biogenesis from the endoplasmic reticulum. Mol Biol Cell 2003;14:5011-5018. 10.1091/mbc.E03-06-0437.
    • (2003) Mol Biol Cell , vol.14 , pp. 5011-5018
    • Puri, S.1    Linstedt, A.D.2
  • 32
    • 0034680777 scopus 로고    scopus 로고
    • Kinase signaling initiates coat complex II (COPII) recruitment and export from the mammalian endoplasmic reticulum
    • 10.1074/jbc.C000449200.
    • Aridor M, Balch WE. Kinase signaling initiates coat complex II (COPII) recruitment and export from the mammalian endoplasmic reticulum. J Biol Chem 2000;275:35673-35676. 10.1074/jbc.C000449200.
    • (2000) J Biol Chem , vol.275 , pp. 35673-35676
    • Aridor, M.1    Balch, W.E.2
  • 33
    • 0033502194 scopus 로고    scopus 로고
    • Clofibrate inhibits membrane trafficking to the Golgi complex and induces its retrograde movement to the endoplasmic reticulum
    • Figueiredo P, Brown WJ. Clofibrate inhibits membrane trafficking to the Golgi complex and induces its retrograde movement to the endoplasmic reticulum. Cell Biol Toxicol 1999;15:311-323.
    • (1999) Cell Biol Toxicol , vol.15 , pp. 311-323
    • Figueiredo, P.1    Brown, W.J.2
  • 34
  • 36
    • 56749182106 scopus 로고    scopus 로고
    • Dissection of a novel molecular determinant mediating Golgi to trans-Golgi network transition
    • 10.1007/s00018-008-8446-y.
    • Schaub BE, Berger EG, Rohrer J. Dissection of a novel molecular determinant mediating Golgi to trans-Golgi network transition. Cell Mol Life Sci 2008;65:3677-3687. 10.1007/s00018-008-8446-y.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 3677-3687
    • Schaub, B.E.1    Berger, E.G.2    Rohrer, J.3
  • 37
    • 39449116332 scopus 로고    scopus 로고
    • Distinct functions for Arf guanine nucleotide exchange factors at the Golgi complex: GBF1 and BIGs are required for assembly and maintenance of the Golgi stack and trans-Golgi network, respectively
    • 10.1091/mbc.E07-04-0394.
    • Manolea F, Claude A, Chun J, Rosas J, Melançon P. Distinct functions for Arf guanine nucleotide exchange factors at the Golgi complex: GBF1 and BIGs are required for assembly and maintenance of the Golgi stack and trans-Golgi network, respectively. Mol Biol Cell 2008;19:523-535. 10.1091/mbc.E07-04-0394.
    • (2008) Mol Biol Cell , vol.19 , pp. 523-535
    • Manolea, F.1    Claude, A.2    Chun, J.3    Rosas, J.4    Melançon, P.5
  • 38
    • 0032585916 scopus 로고    scopus 로고
    • alpha1,3Fucosyltransferase VI is expressed in HepG2 cells and codistributed with beta1,4galactosyltransferase I in the Golgi apparatus and monensin-induced swollen vesicles
    • Borsig L, Imbach T, Höchli M, Berger EG. alpha1, 3Fucosyltransferase VI is expressed in HepG2 cells and codistributed with beta1, 4galactosyltransferase I in the Golgi apparatus and monensin-induced swollen vesicles. Glycobiology 1999;9:1273-1280.
    • (1999) Glycobiology , vol.9 , pp. 1273-1280
    • Borsig, L.1    Imbach, T.2    Höchli, M.3    Berger, E.G.4
  • 39
    • 57649174638 scopus 로고    scopus 로고
    • A novel small molecule regulator of guanine nucleotide exchange activity of the ADP-ribosylation factor and Golgi membrane trafficking
    • 10.1074/jbc.M806592200.
    • Pan H, Yu J, Zhang L, Carpenter A, Zhu H, Li L, Ma D, Yuan J. A novel small molecule regulator of guanine nucleotide exchange activity of the ADP-ribosylation factor and Golgi membrane trafficking. J Biol Chem 2008;283:31087-31096. 10.1074/jbc.M806592200.
    • (2008) J Biol Chem , vol.283 , pp. 31087-31096
    • Pan, H.1    Yu, J.2    Zhang, L.3    Carpenter, A.4    Zhu, H.5    Li, L.6    Ma, D.7    Yuan, J.8
  • 41
    • 0031863118 scopus 로고    scopus 로고
    • Golgi-disturbing agents
    • 10.1007/s004180050256.
    • Dinter A, Berger EG. Golgi-disturbing agents. Histochem Cell Biol 1998;109:571-590. 10.1007/s004180050256.
    • (1998) Histochem Cell Biol , vol.109 , pp. 571-590
    • Dinter, A.1    Berger, E.G.2
  • 42
    • 0033644364 scopus 로고    scopus 로고
    • Brefeldin A revealing the fundamental principles governing membrane dynamics and protein transport
    • Jackson CL. Brefeldin A revealing the fundamental principles governing membrane dynamics and protein transport. Subcell Biochem 2000;34:233-272.
    • (2000) Subcell Biochem , vol.34 , pp. 233-272
    • Jackson, C.L.1
  • 43
    • 0026561901 scopus 로고
    • Brefeldin A: insights into the control of membrane traffic and organelle structure
    • Klausner RD, Donaldson JG, Lippincott-Schwartz J. Brefeldin A: insights into the control of membrane traffic and organelle structure. J Cell Biol 1992;116:1071-1080.
    • (1992) J Cell Biol , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 44
    • 0348047597 scopus 로고    scopus 로고
    • Crystal structure of ARF1*Sec7 complexed with brefeldin A and its implications for the guanine nucleotide exchange mechanism
    • 10.1016/S1097-2765.(03)
    • Mossessova E, Corpina RA, Goldberg J. Crystal structure of ARF1*Sec7 complexed with brefeldin A and its implications for the guanine nucleotide exchange mechanism. Mol Cell 2003;12:1403-1411. 10.1016/S1097-2765.(03)
    • (2003) Mol Cell , vol.12 , pp. 1403-1411
    • Mossessova, E.1    Corpina, R.A.2    Goldberg, J.3
  • 45
    • 0346243924 scopus 로고    scopus 로고
    • Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor
    • 10.1038/nature02197.
    • Renault L, Guibert B, Cherfils J. Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor. Nature 2003;426:525-530. 10.1038/nature02197.
    • (2003) Nature , vol.426 , pp. 525-530
    • Renault, L.1    Guibert, B.2    Cherfils, J.3
  • 46
    • 0002955384 scopus 로고    scopus 로고
    • Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain
    • 10.1016/S1097-2765.(00)
    • Peyroche A, Antonny B, Robineau S, Acker J, Cherfils J, Jackson CL. Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain. Mol Cell 1999;3:275-285. 10.1016/S1097-2765.(00)
    • (1999) Mol Cell , vol.3 , pp. 275-285
    • Peyroche, A.1    Antonny, B.2    Robineau, S.3    Acker, J.4    Cherfils, J.5    Jackson, C.L.6
  • 47
    • 0027953550 scopus 로고
    • Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus
    • Dascher C, Balch WE. Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus. J Biol Chem 1994;269:1437-1448.
    • (1994) J Biol Chem , vol.269 , pp. 1437-1448
    • Dascher, C.1    Balch, W.E.2
  • 48
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER
    • 10.1016/0092-8674.(89)
    • Lippincott-Schwartz J, Yuan LC, Bonifacino JS, Klausner RD. Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 1989;56:801-813. 10.1016/0092-8674.(89)
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 49
    • 0024237306 scopus 로고
    • Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum
    • Fujiwara T, Oda K, Yokota S, Takatsuki A, Ikehara Y. Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum. J Biol Chem 1988;263:18545-18552.
    • (1988) J Biol Chem , vol.263 , pp. 18545-18552
    • Fujiwara, T.1    Oda, K.2    Yokota, S.3    Takatsuki, A.4    Ikehara, Y.5
  • 50
    • 23844432616 scopus 로고    scopus 로고
    • On the action of brefeldin A on Sec7-stimulated membrane-recruitment and GDP/GTP exchange of Arf proteins
    • 10.1042/BST0330635.
    • Cherfils J, Melançon P. On the action of brefeldin A on Sec7-stimulated membrane-recruitment and GDP/GTP exchange of Arf proteins. Biochem Soc Trans 2005;33:635-638. 10.1042/BST0330635.
    • (2005) Biochem Soc Trans , vol.33 , pp. 635-638
    • Cherfils, J.1    Melançon, P.2
  • 51
    • 14844333247 scopus 로고    scopus 로고
    • Dynamics of GBF1, a brefeldin A-sensitive Arf1 exchange factor at the Golgi
    • 10.1091/mbc.E04-07-0599.
    • Niu T-K, Pfeifer AC, Lippincott-Schwartz J, Jackson CL. Dynamics of GBF1, a brefeldin A-sensitive Arf1 exchange factor at the Golgi. Mol Biol Cell 2005;16:1213-1222. 10.1091/mbc.E04-07-0599.
    • (2005) Mol Biol Cell , vol.16 , pp. 1213-1222
    • Niu, T.-K.1    Pfeifer, A.C.2    Lippincott-Schwartz, J.3    Jackson, C.L.4
  • 52
    • 1542297767 scopus 로고    scopus 로고
    • Nuclear localization and molecular partners of BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors
    • 10.1073/pnas.0307345101.
    • Padilla PI, Pacheco-Rodriguez G, Moss J, Vaughan M. Nuclear localization and molecular partners of BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors. Proc Natl Acad Sci U S A 2004;101:2752-2757. 10.1073/pnas.0307345101.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 2752-2757
    • Padilla, P.I.1    Pacheco-Rodriguez, G.2    Moss, J.3    Vaughan, M.4
  • 53
    • 0033549576 scopus 로고    scopus 로고
    • GBF1: a novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5
    • 10.1083/jcb.146.1.71.
    • Claude A, Zhao BP, Kuziemsky CE, Dahan S, Berger SJ, Yan JP, Armold AD, Sullivan EM, Melançon P. GBF1: a novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5. J Cell Biol 1999;146:71-84. 10.1083/jcb.146.1.71.
    • (1999) J Cell Biol , vol.146 , pp. 71-84
    • Claude, A.1    Zhao, B.P.2    Kuziemsky, C.E.3    Dahan, S.4    Berger, S.J.5    Yan, J.P.6    Armold, A.D.7    Sullivan, E.M.8    Melançon, P.9
  • 54
    • 0029051356 scopus 로고
    • Cytotoxicity of brefeldin A correlates with its inhibitory effect on membrane binding of COP coat proteins
    • Torii S, Banno T, Watanabe T, Ikehara Y, Murakami K, Nakayama K. Cytotoxicity of brefeldin A correlates with its inhibitory effect on membrane binding of COP coat proteins. J Biol Chem 1995;270:11574-11580.
    • (1995) J Biol Chem , vol.270 , pp. 11574-11580
    • Torii, S.1    Banno, T.2    Watanabe, T.3    Ikehara, Y.4    Murakami, K.5    Nakayama, K.6
  • 55
    • 23844523182 scopus 로고    scopus 로고
    • The role of ARF1 and rab GTPases in polarization of the Golgi stack
    • 10.1111/j.2005.00319.x.
    • Bannykh SI, Plutner H, Matteson J, Balch WE. The role of ARF1 and rab GTPases in polarization of the Golgi stack. Traffic 2005;6:803-819. 10.1111/j.2005.00319.x.
    • (2005) Traffic , vol.6 , pp. 803-819
    • Bannykh, S.I.1    Plutner, H.2    Matteson, J.3    Balch, W.E.4
  • 56
    • 33646754513 scopus 로고    scopus 로고
    • Ordered assembly of the duplicating Golgi in Trypanosoma brucei
    • 10.1073/pnas.0602595103.
    • Ho HH, He CY, Graffenried CL, Murrells LJ, Warren G. Ordered assembly of the duplicating Golgi in Trypanosoma brucei. Proc Natl Acad Sci U SA 2006;103:7676-7681. 10.1073/pnas.0602595103.
    • (2006) Proc Natl Acad Sci U SA , vol.103 , pp. 7676-7681
    • Ho, H.H.1    He, C.Y.2    Graffenried, C.L.3    Murrells, L.J.4    Warren, G.5
  • 57
    • 31944440900 scopus 로고    scopus 로고
    • Golgi inheritance in mammalian cells is mediated through endoplasmic reticulum export activities
    • 10.1091/mbc.E05-02-0155.
    • Altan-Bonnet N, Sougrat R, Liu W, Snapp EL, Ward T, Lippincott-Schwartz J. Golgi inheritance in mammalian cells is mediated through endoplasmic reticulum export activities. Mol Biol Cell 2006;17:990-1005. 10.1091/mbc.E05-02-0155.
    • (2006) Mol Biol Cell , vol.17 , pp. 990-1005
    • Altan-Bonnet, N.1    Sougrat, R.2    Liu, W.3    Snapp, E.L.4    Ward, T.5    Lippincott-Schwartz, J.6
  • 58
    • 84924192549 scopus 로고    scopus 로고
    • Maintenance of Golgi structure and function depends on the integrity of ER export
    • 10.1083/jcb.200107045.
    • Ward TH, Polishchuk RS, Caplan S, Hirschberg K, Lippincott-Schwartz J. Maintenance of Golgi structure and function depends on the integrity of ER export. J Cell Biol 2001;155:557-570. 10.1083/jcb.200107045.
    • (2001) J Cell Biol , vol.155 , pp. 557-570
    • Ward, T.H.1    Polishchuk, R.S.2    Caplan, S.3    Hirschberg, K.4    Lippincott-Schwartz, J.5
  • 60
    • 0030022030 scopus 로고    scopus 로고
    • SCD5, a suppressor of clathrin deficiency, encodes a novel protein with a late secretory function in yeast
    • Nelson KK, Holmer M, Lemmon SK. SCD5, a suppressor of clathrin deficiency, encodes a novel protein with a late secretory function in yeast. Mol Biol Cell 1996;7:245-260.
    • (1996) Mol Biol Cell , vol.7 , pp. 245-260
    • Nelson, K.K.1    Holmer, M.2    Lemmon, S.K.3
  • 61
    • 17344391184 scopus 로고    scopus 로고
    • ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1
    • 10.1091/mbc.E02-11-0730.
    • García-Mata R, Szul T, Alvarez C, Sztul E. ADP-ribosylation factor/COPI-dependent events at the endoplasmic reticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1. Mol Biol Cell 2003;14:2250-2261. 10.1091/mbc.E02-11-0730.
    • (2003) Mol Biol Cell , vol.14 , pp. 2250-2261
    • García-Mata, R.1    Szul, T.2    Alvarez, C.3    Sztul, E.4
  • 62
    • 0036017789 scopus 로고    scopus 로고
    • GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coat
    • 10.1034/j.2002.30705.x.
    • Kawamoto K, Yoshida Y, Tamaki H, Torii S, Shinotsuka C, Yamashina S, Nakayama K. GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coat. Traffic 2002;3:483-495. 10.1034/j.2002.30705.x.
    • (2002) Traffic , vol.3 , pp. 483-495
    • Kawamoto, K.1    Yoshida, Y.2    Tamaki, H.3    Torii, S.4    Shinotsuka, C.5    Yamashina, S.6    Nakayama, K.7
  • 63
    • 37249041571 scopus 로고    scopus 로고
    • Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking
    • 10.1242/jcs.010769.
    • Szul T, Grabski R, Lyons S, Morohashi Y, Shestopal S, Lowe M, Sztul E. Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking. J Cell Sci 2007;120:3929-3940. 10.1242/jcs.010769.
    • (2007) J Cell Sci , vol.120 , pp. 3929-3940
    • Szul, T.1    Grabski, R.2    Lyons, S.3    Morohashi, Y.4    Shestopal, S.5    Lowe, M.6    Sztul, E.7
  • 64
    • 0034280113 scopus 로고    scopus 로고
    • Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing
    • 10.1093/embo-reports/kvd058.
    • Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S. Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. EMBO Rep 2000;1:287-292. 10.1093/embo-reports/kvd058.
    • (2000) EMBO Rep , vol.1 , pp. 287-292
    • Simpson, J.C.1    Wellenreuther, R.2    Poustka, A.3    Pepperkok, R.4    Wiemann, S.5
  • 65
    • 0026034357 scopus 로고
    • Beta-COP, a 110 kD protein associated with non-clathrin coated vesicles and the Golgi complex, shows homology to beta-adaptin
    • Duden R, Grifiths G, Frank R, Argos P, Kreis TE. Beta-COP, a 110 kD protein associated with non-clathrin coated vesicles and the Golgi complex, shows homology to beta-adaptin. Cell 1991;64:649-665.
    • (1991) Cell , vol.64 , pp. 649-665
    • Duden, R.1    Grifiths, G.2    Frank, R.3    Argos, P.4    Kreis, T.E.5
  • 66
    • 0025674154 scopus 로고
    • Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action
    • Donaldson JG, Lippincott-Schwartz J, Bloom GS, Kreis TE, Klausner RD. Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action. J Cell Biol 1990;111:2295-2306.
    • (1990) J Cell Biol , vol.111 , pp. 2295-2306
    • Donaldson, J.G.1    Lippincott-Schwartz, J.2    Bloom, G.S.3    Kreis, T.E.4    Klausner, R.D.5
  • 67
    • 0033280324 scopus 로고    scopus 로고
    • Adaptors for clathrin-mediated traffic
    • 10.1146/annurev.cellbio.15.1.705.
    • Kirchhausen T. Adaptors for clathrin-mediated traffic. Ann Rev Cell Dev Biol 1999;15:705-732. 10.1146/annurev.cellbio.15.1.705.
    • (1999) Ann Rev Cell Dev Biol , vol.15 , pp. 705-732
    • Kirchhausen, T.1
  • 69
    • 0030843984 scopus 로고    scopus 로고
    • A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities
    • Campbell JA, Davies GJ, Bulone V, Henrissat B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochem J 1997;326:929-939.
    • (1997) Biochem J , vol.326 , pp. 929-939
    • Campbell, J.A.1    Davies, G.J.2    Bulone, V.3    Henrissat, B.4
  • 70
    • 67649972472 scopus 로고    scopus 로고
    • Multicopy suppressor analysis of thermosensitive YIP1 alleles implicates GOT1 in transport from the ER
    • 10.1242/jcs.042457.
    • Lorente-Rodríguez A, Heidtman M, Barlowe C. Multicopy suppressor analysis of thermosensitive YIP1 alleles implicates GOT1 in transport from the ER. J Cell Sci 2009;122:1540-1550. 10.1242/jcs.042457.
    • (2009) J Cell Sci , vol.122 , pp. 1540-1550
    • Lorente-Rodríguez, A.1    Heidtman, M.2    Barlowe, C.3
  • 71
    • 53449093053 scopus 로고    scopus 로고
    • Members of a mammalian SNARE complex interact in the endoplasmic reticulum in vivo and are found in COPI vesicles
    • 10.1016/j.ejcb.2008.07.003.
    • Verrier SE, Willmann M, Wenzel D, Winter U, Fischer von Mollard G, Söling HD. Members of a mammalian SNARE complex interact in the endoplasmic reticulum in vivo and are found in COPI vesicles. Eur J Cell Biol 2008;87:863-878. 10.1016/j.ejcb.2008.07.003.
    • (2008) Eur J Cell Biol , vol.87 , pp. 863-878
    • Verrier, S.E.1    Willmann, M.2    Wenzel, D.3    Winter, U.4    Fischer von Mollard, G.5    Söling, H.D.6
  • 75
    • 0033565631 scopus 로고    scopus 로고
    • Got1p and Sft2p: membrane proteins involved in traffic to the Golgi complex
    • 10.1093/emboj/18.14.3934.
    • Conchon S, Cao X, Barlowe C, Pelham HR. Got1p and Sft2p: membrane proteins involved in traffic to the Golgi complex. EMBO J 1999;18:3934-3946. 10.1093/emboj/18.14.3934.
    • (1999) EMBO J , vol.18 , pp. 3934-3946
    • Conchon, S.1    Cao, X.2    Barlowe, C.3    Pelham, H.R.4
  • 76
    • 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 EG, Warren G, Nilsson T. Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J Cell Sci 1995;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
  • 77
    • 0028823747 scopus 로고
    • Differential response of resident proteins and cycling proteins of the Golgi to brefeldin A
    • Tang BL, Low SH, Hong W. Differential response of resident proteins and cycling proteins of the Golgi to brefeldin A. Eur J Cell Biol 1995;68:199-205.
    • (1995) Eur J Cell Biol , vol.68 , pp. 199-205
    • Tang, B.L.1    Low, S.H.2    Hong, W.3
  • 78
    • 4143086165 scopus 로고    scopus 로고
    • Nicalin and its binding partner Nomo are novel nodal signaling antagonists
    • 10.1038/sj.emboj.7600307.
    • Haffner C, Frauli M, Topp S, Irmler M, Hofmann K, Regula JT, Bally-Cuif L, Haass C. Nicalin and its binding partner Nomo are novel nodal signaling antagonists. EMBO J 2004;23:3041-3050. 10.1038/sj.emboj.7600307.
    • (2004) EMBO J , vol.23 , pp. 3041-3050
    • Haffner, C.1    Frauli, M.2    Topp, S.3    Irmler, M.4    Hofmann, K.5    Regula, J.T.6    Bally-Cuif, L.7    Haass, C.8
  • 79
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
    • 10.1126/science.8128252.
    • Cosson P, Letourneur F. Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 1994;263:1629-1631. 10.1126/science.8128252.
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 80
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson MR, Nilsson T, Peterson PA. Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J 1990;9:3153-3162.
    • (1990) EMBO J , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 81
    • 79952804355 scopus 로고    scopus 로고
    • Cell arrays for the measurement of organelle dynamics in living cells
    • 10.1007/978-1-61737-970-3_6.
    • Erfle H, Lisauskas T, Claas C, Reymann J, Starkuviene V. Cell arrays for the measurement of organelle dynamics in living cells. Methods Mol Biol 2011;706:73-81. 10.1007/978-1-61737-970-3_6.
    • (2011) Methods Mol Biol , vol.706 , pp. 73-81
    • Erfle, H.1    Lisauskas, T.2    Claas, C.3    Reymann, J.4    Starkuviene, V.5
  • 82
    • 0018942213 scopus 로고
    • Mutants of vesicular stomatitis virus blocked at different stages in maturation of the viral glycoprotein
    • 10.1016/0092-8674.(80)90478-X.
    • Zilberstein A, Snider MD, Porter M, Lodish HF. Mutants of vesicular stomatitis virus blocked at different stages in maturation of the viral glycoprotein. Cell 1980;21:417-427. 10.1016/0092-8674.(80)90478-X.
    • (1980) Cell , vol.21 , pp. 417-427
    • Zilberstein, A.1    Snider, M.D.2    Porter, M.3    Lodish, H.F.4
  • 83
    • 0035147424 scopus 로고    scopus 로고
    • Multicolour imaging of post-Golgi sorting and trafficking in live cells
    • 10.1038/35055042.
    • Keller P, Toomre D, Díaz E, White J, Simons K. Multicolour imaging of post-Golgi sorting and trafficking in live cells. Nat Cell Biol 2001;3:140-149. 10.1038/35055042.
    • (2001) Nat Cell Biol , vol.3 , pp. 140-149
    • Keller, P.1    Toomre, D.2    Díaz, E.3    White, J.4    Simons, K.5
  • 85
    • 30044439559 scopus 로고    scopus 로고
    • Cis-Golgi matrix proteins move directly to endoplasmic reticulum exit sites by association with tubules
    • 10.1091/mbc.E05-05-0447.
    • Mardones GA, Snyder CM, Howell KE. Cis-Golgi matrix proteins move directly to endoplasmic reticulum exit sites by association with tubules. Mol Biol Cell 2006;17:525-538. 10.1091/mbc.E05-05-0447.
    • (2006) Mol Biol Cell , vol.17 , pp. 525-538
    • Mardones, G.A.1    Snyder, C.M.2    Howell, K.E.3
  • 86
    • 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
    • 10.1083/jcb.200103104.
    • Miles S, McManus H, Forsten KE, Storrie B. Evidence that the entire Golgi apparatus cycles in interphase HeLa cells: sensitivity of Golgi matrix proteins to an ER exit block. J Cell Biol 2001;155:543-555. 10.1083/jcb.200103104.
    • (2001) J Cell Biol , vol.155 , pp. 543-555
    • Miles, S.1    McManus, H.2    Forsten, K.E.3    Storrie, B.4
  • 88
    • 51349106229 scopus 로고    scopus 로고
    • The Sac1 phosphoinositide phosphatase regulates Golgi membrane morphology and mitotic spindle organization in mammals
    • 10.1091/mbc.E07-12-1290.
    • Liu Y, Boukhelifa M, Tribble E, Morin-Kensicki E, Uetrecht A, Bear JE, Bankaitis VA. The Sac1 phosphoinositide phosphatase regulates Golgi membrane morphology and mitotic spindle organization in mammals. Mol Biol Cell 2008;19:3080-3096. 10.1091/mbc.E07-12-1290.
    • (2008) Mol Biol Cell , vol.19 , pp. 3080-3096
    • Liu, Y.1    Boukhelifa, M.2    Tribble, E.3    Morin-Kensicki, E.4    Uetrecht, A.5    Bear, J.E.6    Bankaitis, V.A.7
  • 89
    • 0033959784 scopus 로고    scopus 로고
    • Efficient export of the vesicular stomatitis virus G protein from the endoplasmic reticulum requires a signal in the cytoplasmic tail that includes both tyrosine-based and di-acidic motifs
    • Sevier CS, Weisz OA, Davis M, Machamer CE. Efficient export of the vesicular stomatitis virus G protein from the endoplasmic reticulum requires a signal in the cytoplasmic tail that includes both tyrosine-based and di-acidic motifs. Mol Biol Cell 2000;11:13-22.
    • (2000) Mol Biol Cell , vol.11 , pp. 13-22
    • Sevier, C.S.1    Weisz, O.A.2    Davis, M.3    Machamer, C.E.4
  • 90
    • 0030812940 scopus 로고    scopus 로고
    • A di-acidic signal required for selective export from the endoplasmic reticulum
    • 10.1126/science.277.5325.556.
    • Nishimura N, Balch WE. A di-acidic signal required for selective export from the endoplasmic reticulum. Science 1997;277:556-558. 10.1126/science.277.5325.556.
    • (1997) Science , vol.277 , pp. 556-558
    • Nishimura, N.1    Balch, W.E.2
  • 91
    • 0042357054 scopus 로고    scopus 로고
    • Persistence of Golgi matrix distribution exhibits the same dependence on Sar1p activity as a Golgi glycosyltransferase
    • 10.1034/j.2003.00122.x.
    • Stroud WJ, Jiang S, Jack G, Storrie B. Persistence of Golgi matrix distribution exhibits the same dependence on Sar1p activity as a Golgi glycosyltransferase. Traffic 2003;4:631-641. 10.1034/j.2003.00122.x.
    • (2003) Traffic , vol.4 , pp. 631-641
    • Stroud, W.J.1    Jiang, S.2    Jack, G.3    Storrie, B.4
  • 92
    • 4344702375 scopus 로고    scopus 로고
    • Dynamic nucleation of Golgi apparatus assembly from the endoplasmic reticulum in interphase Hela cells
    • doi:10.1111/j1398-92192004.00203.x
    • Kasap M, Thomas S, Danaher E, Holton V, Jiang S, Storrie B. Dynamic nucleation of Golgi apparatus assembly from the endoplasmic reticulum in interphase Hela cells. Traffic 2004;5:595-605. doi:10.1111/j1398-92192004.00203.x
    • (2004) Traffic , vol.5 , pp. 595-605
    • Kasap, M.1    Thomas, S.2    Danaher, E.3    Holton, V.4    Jiang, S.5    Storrie, B.6
  • 93
    • 18244407270 scopus 로고    scopus 로고
    • Cisternal rab proteins regulate Golgi apparatus redistribution in response to hypotonic stress
    • 10.1091/mbc.E04-10-0861.
    • Jiang S, Storrie B. Cisternal rab proteins regulate Golgi apparatus redistribution in response to hypotonic stress. Mol Biol Cell 2005;16:2586-2596. 10.1091/mbc.E04-10-0861.
    • (2005) Mol Biol Cell , vol.16 , pp. 2586-2596
    • Jiang, S.1    Storrie, B.2
  • 94
    • 34447549180 scopus 로고    scopus 로고
    • Differential requirements for ts-O45-G and procollagen biosynthetic transport
    • 10.1111/j1600-0854.2007.00582.x
    • Starkuviene V, Pepperkok R. Differential requirements for ts-O45-G and procollagen biosynthetic transport. Traffic 2007;8:1035-1051. 10.1111/j1600-0854.2007.00582.x
    • (2007) Traffic , vol.8 , pp. 1035-1051
    • Starkuviene, V.1    Pepperkok, R.2
  • 95
    • 6344222240 scopus 로고    scopus 로고
    • High-content screening microscopy identifies novel proteins with a putative role in secretory membrane traffic
    • doi:10.1101/gr.2658304.
    • Starkuviene V, Liebel U, Simpson JC, Erfle H, Poustka A, Wiemann S, Pepperkok R. High-content screening microscopy identifies novel proteins with a putative role in secretory membrane traffic. Genome Res 2004;14:1948-1956. doi:10.1101/gr.2658304.
    • (2004) Genome Res , vol.14 , pp. 1948-1956
    • Starkuviene, V.1    Liebel, U.2    Simpson, J.C.3    Erfle, H.4    Poustka, A.5    Wiemann, S.6    Pepperkok, R.7
  • 98
    • 0346732283 scopus 로고    scopus 로고
    • The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex
    • 10.1074/jbc.M307983200.
    • Rohde HM, Cheong FY, Konrad G, Paiha K, Mayinger P, Boehmelt G. The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex. J Biol Chem 2003;278:52689-52699. 10.1074/jbc.M307983200.
    • (2003) J Biol Chem , vol.278 , pp. 52689-52699
    • Rohde, H.M.1    Cheong, F.Y.2    Konrad, G.3    Paiha, K.4    Mayinger, P.5    Boehmelt, G.6
  • 100
    • 23844556829 scopus 로고    scopus 로고
    • Insights into biological functions across species: examining the role of Rab proteins in YIP1 family function
    • 10.1042/BST0330614.
    • Chen CZ, Collins RN. Insights into biological functions across species: examining the role of Rab proteins in YIP1 family function. Biochem Soc Trans 2005;33:614-618. 10.1042/BST0330614.
    • (2005) Biochem Soc Trans , vol.33 , pp. 614-618
    • Chen, C.Z.1    Collins, R.N.2
  • 101
    • 11244306490 scopus 로고    scopus 로고
    • Genetic analysis of yeast Yip1p function reveals a requirement for Golgi-localized rab proteins and rab-Guanine nucleotide dissociation inhibitor
    • 10.1534/genetics.104.032888.
    • Chen CZ, Calero M, DeRegis CJ, Heidtman M, Barlowe C, Collins RN. Genetic analysis of yeast Yip1p function reveals a requirement for Golgi-localized rab proteins and rab-Guanine nucleotide dissociation inhibitor. Genetics 2004;168:1827-1841. 10.1534/genetics.104.032888.
    • (2004) Genetics , vol.168 , pp. 1827-1841
    • Chen, C.Z.1    Calero, M.2    DeRegis, C.J.3    Heidtman, M.4    Barlowe, C.5    Collins, R.N.6
  • 102
    • 0037181467 scopus 로고    scopus 로고
    • Identification of the novel proteins Yip4p and Yip5p as Rab GTPase interacting factors
    • 10.1016/S0014-5793.(02)02442-0
    • Calero M, Winand NJ, Collins RN. Identification of the novel proteins Yip4p and Yip5p as Rab GTPase interacting factors. FEBS Lett 2002;515:89-98. 10.1016/S0014-5793.(02)02442-0
    • (2002) FEBS Lett , vol.515 , pp. 89-98
    • Calero, M.1    Winand, N.J.2    Collins, R.N.3
  • 103
    • 0032168280 scopus 로고    scopus 로고
    • Specific binding to a novel and essential Golgi membrane protein (Yip1p) functionally links the transport GTPases Ypt1p and Ypt31p
    • 10.1093/emboj/17.17.4954.
    • Yang X, Matern HT, Gallwitz D. Specific binding to a novel and essential Golgi membrane protein (Yip1p) functionally links the transport GTPases Ypt1p and Ypt31p. EMBO J 1998;17:4954-4963. 10.1093/emboj/17.17.4954.
    • (1998) EMBO J , vol.17 , pp. 4954-4963
    • Yang, X.1    Matern, H.T.2    Gallwitz, D.3
  • 104
    • 0142091536 scopus 로고    scopus 로고
    • A role for Yip1p in COPII vesicle biogenesis
    • 10.1083/jcb.200306118.
    • Heidtman M, Chen CZ, Collins RN, Barlowe C. A role for Yip1p in COPII vesicle biogenesis. J Cell Biol 2003;163:57-69. 10.1083/jcb.200306118.
    • (2003) J Cell Biol , vol.163 , pp. 57-69
    • Heidtman, M.1    Chen, C.Z.2    Collins, R.N.3    Barlowe, C.4
  • 105
    • 0037805748 scopus 로고    scopus 로고
    • The Yip1p.Yif1p complex is required for the fusion competence of endoplasmic reticulum-derived vesicles
    • 10.1074/jbc.M302406200.
    • Barrowman J, Wang W, Zhang Y, Ferro-Novick S. The Yip1p.Yif1p complex is required for the fusion competence of endoplasmic reticulum-derived vesicles. J Biol Chem 2003;278:19878-19884. 10.1074/jbc.M302406200.
    • (2003) J Biol Chem , vol.278 , pp. 19878-19884
    • Barrowman, J.1    Wang, W.2    Zhang, Y.3    Ferro-Novick, S.4
  • 106
    • 69449088191 scopus 로고    scopus 로고
    • Yip1A regulates the COPI-independent retrograde transport from the Golgi complex to the ER
    • 10.1242/jcs.043414.
    • Kano F, Yamauchi S, Yoshida Y, Watanabe-Takahashi M, Nishikawa K, Nakamura N, Murata M. Yip1A regulates the COPI-independent retrograde transport from the Golgi complex to the ER. J Cell Sci 2009;122:2218-2227. 10.1242/jcs.043414.
    • (2009) J Cell Sci , vol.122 , pp. 2218-2227
    • Kano, F.1    Yamauchi, S.2    Yoshida, Y.3    Watanabe-Takahashi, M.4    Nishikawa, K.5    Nakamura, N.6    Murata, M.7
  • 107
    • 77951749645 scopus 로고    scopus 로고
    • Yip1A structures the mammalian endoplasmic reticulum
    • 10.1091/mbc.E09-12-1002.
    • Dykstra KM, Pokusa JE, Suhan J, Lee TH. Yip1A structures the mammalian endoplasmic reticulum. Mol Biol Cell 2010;21:1556-1568. 10.1091/mbc.E09-12-1002.
    • (2010) Mol Biol Cell , vol.21 , pp. 1556-1568
    • Dykstra, K.M.1    Pokusa, J.E.2    Suhan, J.3    Lee, T.H.4
  • 110
    • 16344363001 scopus 로고    scopus 로고
    • Yos1p is a novel subunit of the Yip1p-Yif1p complex and is required for transport between the endoplasmic reticulum and the Golgi complex
    • 10.1091/mbc.E04-10-0873.
    • Heidtman M, Chen CZ, Collins RN, Barlowe C. Yos1p is a novel subunit of the Yip1p-Yif1p complex and is required for transport between the endoplasmic reticulum and the Golgi complex. Mol Biol Cell 2005;16:1673-1683. 10.1091/mbc.E04-10-0873.
    • (2005) Mol Biol Cell , vol.16 , pp. 1673-1683
    • Heidtman, M.1    Chen, C.Z.2    Collins, R.N.3    Barlowe, C.4
  • 111
    • 70350120449 scopus 로고    scopus 로고
    • The function of the intermediate compartment in pre-Golgi trafficking involves its stable connection with the centrosome
    • 10.1091/mbc.E08-12-1229.
    • Marie M, Dale HA, Sannerud R, Saraste J. The function of the intermediate compartment in pre-Golgi trafficking involves its stable connection with the centrosome. Mol Biol Cell 2009;20:4458-4470. 10.1091/mbc.E08-12-1229.
    • (2009) Mol Biol Cell , vol.20 , pp. 4458-4470
    • Marie, M.1    Dale, H.A.2    Sannerud, R.3    Saraste, J.4
  • 112
    • 0034494870 scopus 로고    scopus 로고
    • Reconstitution of brefeldin A-induced Golgi tubulation and fusion with the endoplasmic reticulum in semi-intact chinese hamster ovary cells
    • Kano F, Sako Y, Tagaya M, Yanagida T, Murata M. Reconstitution of brefeldin A-induced Golgi tubulation and fusion with the endoplasmic reticulum in semi-intact chinese hamster ovary cells. Mol Biol Cell 2000;11:3073-3087.
    • (2000) Mol Biol Cell , vol.11 , pp. 3073-3087
    • Kano, F.1    Sako, Y.2    Tagaya, M.3    Yanagida, T.4    Murata, M.5
  • 113
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • 10.1016/S0092-8674.(00)80379-7
    • Scales SJ, Pepperkok R, Kreis TE. Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell 1997;90:1137-1148. 10.1016/S0092-8674.(00)80379-7
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 115
    • 0017691474 scopus 로고
    • Automatic measurement of sister chromatid exchange frequency
    • Zack GW, Rogers WE, Latt SA. Automatic measurement of sister chromatid exchange frequency. J Histochem Cytochem 1977;25:741-753.
    • (1977) J Histochem Cytochem , vol.25 , pp. 741-753
    • Zack, G.W.1    Rogers, W.E.2    Latt, S.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.