메뉴 건너뛰기




Volumn 14, Issue 6, 2013, Pages 382-392

Organization of the ER-Golgi interface for membrane traffic control

Author keywords

[No Author keywords available]

Indexed keywords

COAT PROTEIN COMPLEX I; COAT PROTEIN COMPLEX II; COLLAGEN FIBER;

EID: 84878253184     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3588     Document Type: Review
Times cited : (404)

References (147)
  • 2
    • 0035983848 scopus 로고    scopus 로고
    • Membrane protein transport between the endoplasmic reticulum and the Golgi in tobacco leaves is energy dependent but cytoskeleton independent: Evidence from selective photobleaching
    • Brandizzi, F., Snapp, E. L., Roberts, A. G., Lippincott-Schwartz, J. & Hawes, C. Membrane protein transport between the endoplasmic reticulum and the Golgi in tobacco leaves is energy dependent but cytoskeleton independent: evidence from selective photobleaching. Plant Cell 14, 1293-1309 (2002).
    • (2002) Plant Cell , vol.14 , pp. 1293-1309
    • Brandizzi, F.1    Snapp, E.L.2    Roberts, A.G.3    Lippincott-Schwartz, J.4    Hawes, C.5
  • 4
    • 0031975699 scopus 로고    scopus 로고
    • The Golgi apparatus: 100 years of progress and controversy
    • Farquhar, M. G. & Palade, G. E. The Golgi apparatus: 100 years of progress and controversy. Trends Cell Biol. 8, 2-10 (1998).
    • (1998) Trends Cell Biol. , vol.8 , pp. 2-10
    • Farquhar, M.G.1    Palade, G.E.2
  • 5
    • 0002278346 scopus 로고    scopus 로고
    • eds. Berger, E. G.and Roth, J.) Birkhäuser Verlag
    • Driouich, A. & Staehelin, L. A. in The Golgi Apparatus (eds. Berger, E. G.and Roth, J.) 275-301 (Birkhäuser Verlag, 1997).
    • (1997) The Golgi Apparatus , pp. 275-301
    • Driouich, A.1    Staehelin, L.A.2
  • 6
    • 0027351945 scopus 로고
    • Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth
    • Carpita, N. C. & Gibeaut, D. M. Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth. Plant J. 3, 1-30 (1993).
    • (1993) Plant J. , vol.3 , pp. 1-30
    • Carpita, N.C.1    Gibeaut, D.M.2
  • 7
    • 52649158139 scopus 로고    scopus 로고
    • Disrupting two Arabidopsis thaliana xylosyltransferase genes results in plants deficient in xyloglucan, a major primary cell wall component
    • Cavalier, D. M. et al. Disrupting two Arabidopsis thaliana xylosyltransferase genes results in plants deficient in xyloglucan, a major primary cell wall component. Plant Cell 20, 1519-1537 (2008).
    • (2008) Plant Cell , vol.20 , pp. 1519-1537
    • Cavalier, D.M.1
  • 8
    • 0036715728 scopus 로고    scopus 로고
    • The Golgi localization of Arabidopsis thaliana β1, 2-xylosyltransferase in plant cells is dependent on its cytoplasmic and transmembrane sequences
    • Dirnberger, D., Bencur, P., Mach, L. & Steinkellner, H. The Golgi localization of Arabidopsis thaliana β1, 2-xylosyltransferase in plant cells is dependent on its cytoplasmic and transmembrane sequences. Plant Mol. Biol. 50, 273-281 (2002).
    • (2002) Plant Mol. Biol. , vol.50 , pp. 273-281
    • Dirnberger, D.1    Bencur, P.2    MacH, L.3    Steinkellner, H.4
  • 9
    • 0033213560 scopus 로고    scopus 로고
    • Biosynthesis and immunolocalization of Lewis a-containing N-glycans in the plant cell
    • Fitchette, A. C. et al. Biosynthesis and immunolocalization of Lewis a-containing N-glycans in the plant cell. Plant Physiol. 121, 333-344 (1999).
    • (1999) Plant Physiol. , vol.121 , pp. 333-344
    • Fitchette, A.C.1
  • 11
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • De Matteis, M. A. & Morrow, J. S. Spectrin tethers and mesh in the biosynthetic pathway. J. Cell Sci. 113, 2331-2343 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 2331-2343
    • De Matteis, M.A.1    Morrow, J.S.2
  • 12
    • 22744448198 scopus 로고    scopus 로고
    • Control of MAP kinase signaling to the nucleus
    • Kondoh, K., Torii, S. & Nishida, E. Control of MAP kinase signaling to the nucleus. Chromosoma 114, 86-91 (2005).
    • (2005) Chromosoma , vol.114 , pp. 86-91
    • Kondoh, K.1    Torii, S.2    Nishida, E.3
  • 13
    • 33845762779 scopus 로고    scopus 로고
    • Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway
    • Saint-Jore-Dupas, C. et al. Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway. Plant Cell 18, 3182-3200 (2006).
    • (2006) Plant Cell , vol.18 , pp. 3182-3200
    • Saint-Jore-Dupas, C.1
  • 14
    • 0028905820 scopus 로고
    • Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides
    • Rabouille, C. et al. Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J. Cell Sci. 108, 1617-1627 (1995).
    • (1995) J. Cell Sci. , vol.108 , pp. 1617-1627
    • Rabouille, C.1
  • 15
    • 0033667627 scopus 로고    scopus 로고
    • The growing Golgi: In search of its independence
    • Klumperman, J. The growing Golgi: in search of its independence. Nature Cell Biol. 2, E217-E219 (2000).
    • (2000) Nature Cell Biol. , vol.2
    • Klumperman, J.1
  • 16
    • 39749200034 scopus 로고    scopus 로고
    • Imaging and imagination: Understanding the endo-lysosomal system
    • van Meel, E. & Klumperman, J. Imaging and imagination: understanding the endo-lysosomal system. Histochem. Cell Biol. 129, 253-266 (2008).
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 253-266
    • Van Meel, E.1    Klumperman, J.2
  • 17
    • 33646245286 scopus 로고    scopus 로고
    • Arabidopsis vacuolar H-ATPase subunit e isoform 1 is required for Golgi organization and vacuole function in embryogenesis
    • Dettmer, J., Hong-Hermesdorf, A., Stierhof, Y. D. & Schumacher, K. Arabidopsis vacuolar H-ATPase subunit E isoform 1 is required for Golgi organization and vacuole function in embryogenesis. Plant Cell 18, 715-730 (2006).
    • (2006) Plant Cell , vol.18 , pp. 715-730
    • Dettmer, J.1    Hong-Hermesdorf, A.2    Stierhof, Y.D.3    Schumacher, K.4
  • 18
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • Nickel, W. & Rabouille, C. Mechanisms of regulated unconventional protein secretion. Nature Rev. Mol. Cell Biol. 10, 148-155 (2009).
    • (2009) Nature Rev. Mol. Cell Biol. , vol.10 , pp. 148-155
    • Nickel, W.1    Rabouille, C.2
  • 19
    • 10144220633 scopus 로고    scopus 로고
    • The organization of endoplasmic reticulum export complexes
    • Bannykh, S. I., Rowe, T. & Balch, W. E. The organization of endoplasmic reticulum export complexes. J. Cell Biol. 135, 19-35 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 19-35
    • Bannykh, S.I.1    Rowe, T.2    Balch, W.E.3
  • 20
    • 0034493602 scopus 로고    scopus 로고
    • Dynamics of transitional endoplasmic reticulum sites in vertebrate cells
    • Hammond, A. T. & Glick, B. S. Dynamics of transitional endoplasmic reticulum sites in vertebrate cells. Mol. Biol. Cell 11, 3013-3030 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3013-3030
    • Hammond, A.T.1    Glick, B.S.2
  • 21
    • 0028966452 scopus 로고
    • Human SEC13Rp functions in yeast and is located on transport vesicles budding from the endoplasmic reticulum
    • Shaywitz, D. A., Orci, L., Ravazzola, M., Swaroop, A. & Kaiser, C. A. Human SEC13Rp functions in yeast and is located on transport vesicles budding from the endoplasmic reticulum. J. Cell Biol. 128, 769-777 (1995).
    • (1995) J. Cell Biol. , vol.128 , pp. 769-777
    • Shaywitz, D.A.1    Orci, L.2    Ravazzola, M.3    Swaroop, A.4    Kaiser, C.A.5
  • 22
    • 0033526048 scopus 로고    scopus 로고
    • Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae
    • Rossanese, O. W. et al. Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae. J. Cell Biol. 145, 69-81 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 69-81
    • Rossanese, O.W.1
  • 23
    • 0038382300 scopus 로고    scopus 로고
    • Dual modes of endoplasmic reticulum-to-Golgi transport in dendrites revealed by live-cell imaging
    • Horton, A. C. & Ehlers, M. D. Dual modes of endoplasmic reticulum-to-Golgi transport in dendrites revealed by live-cell imaging. J. Neurosci. 23, 6188-6199 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 6188-6199
    • Horton, A.C.1    Ehlers, M.D.2
  • 24
    • 3142706602 scopus 로고    scopus 로고
    • Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells
    • daSilva, L. L. et al. Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells. Plant Cell 16, 1753-1771 (2004).
    • (2004) Plant Cell , vol.16 , pp. 1753-1771
    • Dasilva, L.L.1
  • 25
    • 23944445863 scopus 로고    scopus 로고
    • Sec16 is a determinant of transitional ER organization
    • Connerly, P. L. et al. Sec16 is a determinant of transitional ER organization. Curr. Biol. 15, 1439-1447 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 1439-1447
    • Connerly, P.L.1
  • 26
    • 33750969692 scopus 로고    scopus 로고
    • Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells
    • Watson, P., Townley, A. K., Koka, P., Palmer, K. J. & Stephens, D. J. Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells. Traffic 7, 1678-1687 (2006).
    • (2006) Traffic , vol.7 , pp. 1678-1687
    • Watson, P.1    Townley, A.K.2    Koka, P.3    Palmer, K.J.4    Stephens, D.J.5
  • 27
    • 77955050742 scopus 로고    scopus 로고
    • Regulation of coat assembly-sorting things out at the ER
    • Miller, E. A. & Barlowe, C. Regulation of coat assembly-sorting things out at the ER. Curr. Opin. Cell Biol. 22, 447-453 (2010).
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 447-453
    • Miller, E.A.1    Barlowe, C.2
  • 28
    • 84863883702 scopus 로고    scopus 로고
    • Entry and exit mechanisms at the cis-face of the Golgi complex
    • 11 Apr 2011 (doi:10.1101/cshperspect.a005207)
    • Lorente-Rodriguez, A. & Barlowe, C. Entry and exit mechanisms at the cis-face of the Golgi complex. Cold Spring Harb. Perspect. Biol. 11 Apr 2011 (doi:10.1101/cshperspect.a005207).
    • Cold Spring Harb. Perspect. Biol
    • Lorente-Rodriguez, A.1    Barlowe, C.2
  • 29
    • 0032522377 scopus 로고    scopus 로고
    • Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins
    • Cao, X., Ballew, N. & Barlowe, C. Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J. 17, 2156-2165 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2156-2165
    • Cao, X.1    Ballew, N.2    Barlowe, C.3
  • 30
    • 0034698202 scopus 로고    scopus 로고
    • Rab1 recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion
    • Allan, B. B., Moyer, B. D. & Balch, W. E. Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion. Science 289, 444-448 (2000).
    • (2000) Science , vol.289 , pp. 444-448
    • Allan, B.B.1    Moyer, B.D.2    Balch, W.E.3
  • 31
    • 33847211759 scopus 로고    scopus 로고
    • TRAPPI tethers COPII vesicles by binding the coat subunit Sec23
    • Cai, H. et al. TRAPPI tethers COPII vesicles by binding the coat subunit Sec23. Nature 445, 941-944 (2007).
    • (2007) Nature , vol.445 , pp. 941-944
    • Cai, H.1
  • 32
    • 69949175597 scopus 로고    scopus 로고
    • A link between ER tethering and COP-I vesicle uncoating
    • Zink, S., Wenzel, D., Wurm, C. A. & Schmitt, H. D. A link between ER tethering and COP-I vesicle uncoating. Dev. Cell 17, 403-416 (2009).
    • (2009) Dev. Cell , vol.17 , pp. 403-416
    • Zink, S.1    Wenzel, D.2    Wurm, C.A.3    Schmitt, H.D.4
  • 33
    • 0032417711 scopus 로고    scopus 로고
    • Procollagen traverses the Golgi stack without leaving the lumen of cisternae: Evidence for cisternal maturation
    • Bonfanti, L. et al. Procollagen traverses the Golgi stack without leaving the lumen of cisternae: evidence for cisternal maturation. Cell 95, 993-1003 (1998).
    • (1998) Cell , vol.95 , pp. 993-1003
    • Bonfanti, L.1
  • 34
    • 0028233498 scopus 로고
    • COPII: A membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum
    • Barlowe, C. et al. COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77, 895-907 (1994).
    • (1994) Cell , vol.77 , pp. 895-907
    • Barlowe, C.1
  • 35
    • 48649098177 scopus 로고    scopus 로고
    • Structural basis for cargo regulation of COPII coat assembly
    • Stagg, S. M. et al. Structural basis for cargo regulation of COPII coat assembly. Cell 134, 474-484 (2008).
    • (2008) Cell , vol.134 , pp. 474-484
    • Stagg, S.M.1
  • 37
    • 30544436808 scopus 로고    scopus 로고
    • Structure of the Sec13/31 COPII coat cage
    • Stagg, S. M. et al. Structure of the Sec13/31 COPII coat cage. Nature 439, 234-238 (2006).
    • (2006) Nature , vol.439 , pp. 234-238
    • Stagg, S.M.1
  • 38
    • 34250745253 scopus 로고    scopus 로고
    • Structure and organization of coat proteins in the COPII cage
    • Fath, S., Mancias, J. D., Bi, X. & Goldberg, J. Structure and organization of coat proteins in the COPII cage. Cell 129, 1325-1336 (2007).
    • (2007) Cell , vol.129 , pp. 1325-1336
    • Fath, S.1    Mancias, J.D.2    Bi, X.3    Goldberg, J.4
  • 39
    • 84862216994 scopus 로고    scopus 로고
    • The structure of the Sec13/31 COPII cage bound to Sec23
    • Bhattacharya, N., J., O. D. & Stagg, S. M. The structure of the Sec13/31 COPII cage bound to Sec23. J. Mol. Biol. 420, 324-334 (2012).
    • (2012) J. Mol. Biol. , vol.420 , pp. 324-334
    • Bhattacharya, N.J.O.D.1    Stagg, S.M.2
  • 40
    • 33645723490 scopus 로고    scopus 로고
    • Immuno-electron tomography of ER exit sites reveals the existence of free COPII-coated transport carriers
    • Zeuschner, D. et al. Immuno-electron tomography of ER exit sites reveals the existence of free COPII-coated transport carriers. Nature Cell Biol. 8, 377-383 (2006).
    • (2006) Nature Cell Biol. , vol.8 , pp. 377-383
    • Zeuschner, D.1
  • 41
    • 84255172971 scopus 로고    scopus 로고
    • Multibudded tubules formed by COPII on artificial liposomes
    • Bacia, K. et al. Multibudded tubules formed by COPII on artificial liposomes. Sci. Rep. 1, 17 (2011).
    • (2011) Sci. Rep. , vol.1 , pp. 17
    • Bacia, K.1
  • 42
    • 33749128067 scopus 로고    scopus 로고
    • Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-Golgi trafficking
    • Boyadjiev, S. A. et al. Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-Golgi trafficking. Nature Genet. 38, 1192-1197 (2006).
    • (2006) Nature Genet. , vol.38 , pp. 1192-1197
    • Boyadjiev, S.A.1
  • 43
    • 33749151608 scopus 로고    scopus 로고
    • Secretory COPII coat component Sec23a is essential for craniofacial chondrocyte maturation
    • Lang, M. R., Lapierre, L. A., Frotscher, M., Goldenring, J. R. & Knapik, E. W. Secretory COPII coat component Sec23a is essential for craniofacial chondrocyte maturation. Nature Genet. 38, 1198-1203 (2006).
    • (2006) Nature Genet. , vol.38 , pp. 1198-1203
    • Lang, M.R.1    Lapierre, L.A.2    Frotscher, M.3    Goldenring, J.R.4    Knapik, E.W.5
  • 44
    • 35548961813 scopus 로고    scopus 로고
    • The genetic basis of a craniofacial disease provides insight into COPII coat assembly
    • Fromme, J. C. et al. The genetic basis of a craniofacial disease provides insight into COPII coat assembly. Dev. Cell 13, 623-634 (2007).
    • (2007) Dev. Cell , vol.13 , pp. 623-634
    • Fromme, J.C.1
  • 45
    • 0037656344 scopus 로고    scopus 로고
    • Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders
    • Jones, B. et al. Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders. Nature Genet. 34, 29-31 (2003).
    • (2003) Nature Genet. , vol.34 , pp. 29-31
    • Jones, B.1
  • 46
    • 56749154593 scopus 로고    scopus 로고
    • Anderson's disease (chylomicron retention disease): A new mutation in the SARA2 gene associated with muscular and cardiac abnormalities
    • Silvain, M. et al. Anderson's disease (chylomicron retention disease): a new mutation in the SARA2 gene associated with muscular and cardiac abnormalities. Clin. Genet. 74, 546-552 (2008).
    • (2008) Clin. Genet. , vol.74 , pp. 546-552
    • Silvain, M.1
  • 47
    • 84857377700 scopus 로고    scopus 로고
    • Ubiquitin-dependent regulation of COPII coat size and function
    • Jin, L. et al. Ubiquitin-dependent regulation of COPII coat size and function. Nature 482, 495-500 (2012).
    • (2012) Nature , vol.482 , pp. 495-500
    • Jin, L.1
  • 48
    • 61449242669 scopus 로고    scopus 로고
    • TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites
    • Saito, K. et al. TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites. Cell 136, 891-902 (2009).
    • (2009) Cell , vol.136 , pp. 891-902
    • Saito, K.1
  • 49
    • 79959883614 scopus 로고    scopus 로고
    • CTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites
    • Saito, K. et al. cTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites. Mol. Biol. Cell 22, 2301-2308 (2011).
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2301-2308
    • Saito, K.1
  • 50
    • 77957740755 scopus 로고    scopus 로고
    • Plant cell walls
    • Keegstra, K. Plant cell walls. Plant Physiol. 154, 483-486 (2010).
    • (2010) Plant Physiol. , vol.154 , pp. 483-486
    • Keegstra, K.1
  • 51
    • 34249785671 scopus 로고    scopus 로고
    • De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated
    • Hanton, S. L., Chatre, L., Renna, L., Matheson, L. A. & Brandizzi, F. De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated. Plant Physiol. 143, 1640-1650 (2007).
    • (2007) Plant Physiol. , vol.143 , pp. 1640-1650
    • Hanton, S.L.1    Chatre, L.2    Renna, L.3    Matheson, L.A.4    Brandizzi, F.5
  • 52
    • 49149100705 scopus 로고    scopus 로고
    • Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load
    • Farhan, H., Weiss, M., Tani, K., Kaufman, R. J. & Hauri, H. P. Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load. EMBO J. 27, 2043-2054 (2008).
    • (2008) EMBO J. , vol.27 , pp. 2043-2054
    • Farhan, H.1    Weiss, M.2    Tani, K.3    Kaufman, R.J.4    Hauri, H.P.5
  • 53
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter, P. & Ron, D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081-1086 (2011).
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 54
    • 0030955328 scopus 로고    scopus 로고
    • ER-to-Golgi transport visualized in living cells
    • Presley, J. F. et al. ER-to-Golgi transport visualized in living cells. Nature 389, 81-85 (1997).
    • (1997) Nature , vol.389 , pp. 81-85
    • Presley, J.F.1
  • 55
    • 84869120330 scopus 로고    scopus 로고
    • Functional coupling of microtubules to membranes-implications for membrane structure and dynamics
    • Stephens, D. J. Functional coupling of microtubules to membranes-implications for membrane structure and dynamics. J. Cell Sci. 125, 2795-2804 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 2795-2804
    • Stephens, D.J.1
  • 57
    • 0842265856 scopus 로고    scopus 로고
    • Dynamics of proteins in Golgi membranes: Comparisons between mammalian and plant cells highlighted by photobleaching techniques
    • Ward, T. H. & Brandizzi, F. Dynamics of proteins in Golgi membranes: comparisons between mammalian and plant cells highlighted by photobleaching techniques. Cell. Mol. Life Sci. 61, 172-185 (2004).
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 172-185
    • Ward, T.H.1    Brandizzi, F.2
  • 58
    • 0342288633 scopus 로고    scopus 로고
    • Stop-and-go movements of plant Golgi stacks are mediated by the acto-myosin system
    • Nebenfuhr, A. et al. Stop-and-go movements of plant Golgi stacks are mediated by the acto-myosin system. Plant Physiol. 121, 1127-1142 (1999).
    • (1999) Plant Physiol. , vol.121 , pp. 1127-1142
    • Nebenfuhr, A.1
  • 59
    • 0032144201 scopus 로고    scopus 로고
    • Stacks on tracks: The plant Golgi apparatus traffics on an actin/ER network
    • Boevink, P. et al. Stacks on tracks: the plant Golgi apparatus traffics on an actin/ER network. Plant J. 15, 441-447 (1998).
    • (1998) Plant J. , vol.15 , pp. 441-447
    • Boevink, P.1
  • 60
    • 31844440878 scopus 로고    scopus 로고
    • Functional genomics reveals genes involved in protein secretion and Golgi organization
    • Bard, F. et al. Functional genomics reveals genes involved in protein secretion and Golgi organization. Nature 439, 604-607 (2006).
    • (2006) Nature , vol.439 , pp. 604-607
    • Bard, F.1
  • 61
    • 2442451357 scopus 로고    scopus 로고
    • Golgi duplication in Trypanosoma brucei
    • He, C. Y. et al. Golgi duplication in Trypanosoma brucei. J. Cell Biol. 165, 313-321 (2004).
    • (2004) J. Cell Biol. , vol.165 , pp. 313-321
    • He, C.Y.1
  • 62
    • 0032845689 scopus 로고    scopus 로고
    • The nuclear envelope serves as an intermediary between the ER and Golgi complex in the intracellular parasite Toxoplasma gondii
    • Hager, K. M., Striepen, B., Tilney, L. G. & Roos, D. S. The nuclear envelope serves as an intermediary between the ER and Golgi complex in the intracellular parasite Toxoplasma gondii. J. Cell Sci. 112, 2631-2638 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 2631-2638
    • Hager, K.M.1    Striepen, B.2    Tilney, L.G.3    Roos, D.S.4
  • 63
    • 48949107700 scopus 로고    scopus 로고
    • Myosin XI-K is required for rapid trafficking of Golgi stacks, peroxisomes, and mitochondria in leaf cells of Nicotiana benthamiana
    • Avisar, D., Prokhnevsky, A. I., Makarova, K. S., Koonin, E. V. & Dolja, V. V. Myosin XI-K is required for rapid trafficking of Golgi stacks, peroxisomes, and mitochondria in leaf cells of Nicotiana benthamiana. Plant Physiol. 146, 1098-1108 (2008).
    • (2008) Plant Physiol. , vol.146 , pp. 1098-1108
    • Avisar, D.1    Prokhnevsky, A.I.2    Makarova, K.S.3    Koonin, E.V.4    Dolja, V.V.5
  • 64
    • 48949120196 scopus 로고    scopus 로고
    • Tw o class XI myosins function in organelle trafficking and root hair development in Arabidopsis
    • Peremyslov, V. V., Prokhnevsky, A. I., Avisar, D. & Dolja, V. V. Tw o class XI myosins function in organelle trafficking and root hair development in Arabidopsis. Plant Physiol. 146, 1109-1116 (2008).
    • (2008) Plant Physiol. , vol.146 , pp. 1109-1116
    • Peremyslov, V.V.1    Prokhnevsky, A.I.2    Avisar, D.3    Dolja, V.V.4
  • 65
    • 48649091493 scopus 로고    scopus 로고
    • Truncated myosin XI tail fusions inhibit peroxisome, Golgi, and mitochondrial movement in tobacco leaf epidermal cells: A genetic tool for the next generation
    • Sparkes, I. A., Teanby, N. A. & Hawes, C. Truncated myosin XI tail fusions inhibit peroxisome, Golgi, and mitochondrial movement in tobacco leaf epidermal cells: a genetic tool for the next generation. J. Exp. Bot. 59, 2499-2512 (2008).
    • (2008) J. Exp. Bot. , vol.59 , pp. 2499-2512
    • Sparkes, I.A.1    Teanby, N.A.2    Hawes, C.3
  • 66
    • 20444386846 scopus 로고    scopus 로고
    • The plant Golgi apparatus-going with the flow
    • Hawes, C. & Satiat-Jeunemaitre, B. The plant Golgi apparatus-going with the flow. Biochim. Biophys. Acta 1744, 93-107 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 93-107
    • Hawes, C.1    Satiat-Jeunemaitre, B.2
  • 67
    • 84876106182 scopus 로고    scopus 로고
    • Cis-Golgi cisternal assembly and biosynthetic activation occur sequentially in plants and algae
    • Donohoe, B. S. et al. Cis-Golgi cisternal assembly and biosynthetic activation occur sequentially in plants and algae. Traffic 14, 551-567 (2013).
    • (2013) Traffic , vol.14 , pp. 551-567
    • Donohoe, B.S.1
  • 68
    • 33845991859 scopus 로고    scopus 로고
    • SNARE status regulates tether recruitment and function in homotypic COPII vesicle fusion
    • Bentley, M. et al. SNARE status regulates tether recruitment and function in homotypic COPII vesicle fusion. J. Biol. Chem. 281, 38825-38833 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 38825-38833
    • Bentley, M.1
  • 69
    • 11244273061 scopus 로고    scopus 로고
    • Reconstitution of COPII vesicle fusion to generate a pre-Golgi intermediate compartment
    • Xu, D. & Hay, J. C. Reconstitution of COPII vesicle fusion to generate a pre-Golgi intermediate compartment. J. Cell Biol. 167, 997-1003 (2004).
    • (2004) J. Cell Biol. , vol.167 , pp. 997-1003
    • Xu, D.1    Hay, J.C.2
  • 70
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino, J. S. & Glick, B. S. The mechanisms of vesicle budding and fusion. Cell 116, 153-166 (2004).
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 71
    • 0027078786 scopus 로고
    • Endoplasmic reticulum: A dynamic patchwork of specialized subregions
    • Sitia, R. & Meldolesi, J. Endoplasmic reticulum: a dynamic patchwork of specialized subregions. Mol. Biol. Cell 3, 1067-1072 (1992).
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1067-1072
    • Sitia, R.1    Meldolesi, J.2
  • 72
    • 0026503134 scopus 로고
    • The Golgi complex: In vitro veritas?
    • Mellman, I. & Simons, K. The Golgi complex: in vitro veritas? Cell 68, 829-840 (1992).
    • (1992) Cell , vol.68 , pp. 829-840
    • Mellman, I.1    Simons, K.2
  • 73
    • 0031743855 scopus 로고    scopus 로고
    • The recycling pathway of protein ERGIC-53 and dynamics of the ER-Golgi intermediate compartment
    • Klumperman, J. et al. The recycling pathway of protein ERGIC-53 and dynamics of the ER-Golgi intermediate compartment. J. Cell Sci. 111, 3411-3425 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 3411-3425
    • Klumperman, J.1
  • 74
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment (ERGIC): In search of its identity and function
    • Appenzeller-Herzog, C. & Hauri, H. P. The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J. Cell Sci. 119, 2173-2183 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 75
    • 0033538549 scopus 로고    scopus 로고
    • Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles
    • Martinez-Menarguez, J. A., Geuze, H. J., Slot, J. W. & Klumperman, J. Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles. Cell 98, 81-90 (1999).
    • (1999) Cell , vol.98 , pp. 81-90
    • Martinez-Menarguez, J.A.1    Geuze, H.J.2    Slot, J.W.3    Klumperman, J.4
  • 76
    • 8744259809 scopus 로고    scopus 로고
    • Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46
    • Breuza, L. et al. Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46. J. Biol. Chem. 279, 47242-47253 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 47242-47253
    • Breuza, L.1
  • 77
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • Scales, S. J., Pepperkok, R. & Kreis, T. E. Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell 90, 1137-1148 (1997).
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 78
    • 0035071569 scopus 로고    scopus 로고
    • Illuminating the secretory pathway: When do we need vesicles? J
    • Stephens, D. J. & Pepperkok, R. Illuminating the secretory pathway: when do we need vesicles? J. Cell Sci. 114, 1053-1059 (2001).
    • (2001) Cell Sci. , vol.114 , pp. 1053-1059
    • Stephens, D.J.1    Pepperkok, R.2
  • 80
    • 0033400723 scopus 로고    scopus 로고
    • Dynamic association of cytoplasmic dynein heavy chain 1a with the Golgi apparatus and intermediate compartment
    • Roghi, C. & Allan, V. J. Dynamic association of cytoplasmic dynein heavy chain 1a with the Golgi apparatus and intermediate compartment. J. Cell Sci. 112, 4673-4685 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 4673-4685
    • Roghi, C.1    Allan, V.J.2
  • 81
    • 20544465130 scopus 로고    scopus 로고
    • Spectrins and the Golgi
    • Beck, K. A. Spectrins and the Golgi. Biochim. Biophys. Acta 1744, 374-382 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 374-382
    • Beck, K.A.1
  • 82
    • 18844381624 scopus 로고    scopus 로고
    • Coatomer-bound Cdc42 regulates dynein recruitment to COPI vesicles
    • Chen, J. L. et al. Coatomer-bound Cdc42 regulates dynein recruitment to COPI vesicles. J. Cell Biol. 169, 383-389 (2005).
    • (2005) J. Cell Biol. , vol.169 , pp. 383-389
    • Chen, J.L.1
  • 83
    • 14044272872 scopus 로고    scopus 로고
    • Live imaging of bidirectional traffic from the ERGIC
    • Ben-Tekaya, H., Miura, K., Pepperkok, R. & Hauri, H. P. Live imaging of bidirectional traffic from the ERGIC. J. Cell Sci. 118, 357-367 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 357-367
    • Ben-Tekaya, H.1    Miura, K.2    Pepperkok, R.3    Hauri, H.P.4
  • 84
    • 64849095076 scopus 로고    scopus 로고
    • Grab a Golgi: Laser trapping of Golgi bodies reveals in vivo interactions with the endoplasmic reticulum
    • Sparkes, I. A., Ketelaar, T., Ruijter, N. C. & Hawes, C. Grab a Golgi: laser trapping of Golgi bodies reveals in vivo interactions with the endoplasmic reticulum. Traffic 10, 567-571 (2009).
    • (2009) Traffic , vol.10 , pp. 567-571
    • Sparkes, I.A.1    Ketelaar, T.2    Ruijter, N.C.3    Hawes, C.4
  • 85
    • 62149130111 scopus 로고    scopus 로고
    • Dynamic organization of COPII coat proteins at endoplasmic reticulum export sites in plant cells
    • Hanton, S. L., Matheson, L. A., Chatre, L. & Brandizzi, F. Dynamic organization of COPII coat proteins at endoplasmic reticulum export sites in plant cells. Plant J. 57, 963-974 (2009).
    • (2009) Plant J. , vol.57 , pp. 963-974
    • Hanton, S.L.1    Matheson, L.A.2    Chatre, L.3    Brandizzi, F.4
  • 86
    • 33646832927 scopus 로고    scopus 로고
    • In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulum and of ER export sites depends on active COPI machinery
    • Stefano, G. et al. In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulum and of ER export sites depends on active COPI machinery. Plant J. 46, 95-110 (2006).
    • (2006) Plant J. , vol.46 , pp. 95-110
    • Stefano, G.1
  • 87
    • 42649092103 scopus 로고    scopus 로고
    • Plant Sar1 isoforms with near-identical protein sequences exhibit different localisations and effects on secretion
    • Hanton, S. L. et al. Plant Sar1 isoforms with near-identical protein sequences exhibit different localisations and effects on secretion. Plant Mol. Biol. 67, 283-294 (2008).
    • (2008) Plant Mol. Biol. , vol.67 , pp. 283-294
    • Hanton, S.L.1
  • 88
    • 57349162005 scopus 로고    scopus 로고
    • Biogenesis of cytoplasmic membranous vesicles for plant potyvirus replication occurs at endoplasmic reticulum exit sites in a COPI-and COPII-dependent manner
    • Wei, T. & Wang, A. Biogenesis of cytoplasmic membranous vesicles for plant potyvirus replication occurs at endoplasmic reticulum exit sites in a COPI-and COPII-dependent manner. J. Virol. 82, 12252-12264 (2008).
    • (2008) J. Virol. , vol.82 , pp. 12252-12264
    • Wei, T.1    Wang, A.2
  • 90
    • 57549113660 scopus 로고    scopus 로고
    • +-channel KAT1 with the coat protein complex II coat component Sec24 depends on a di-acidic endoplasmic reticulum export motif
    • +-channel KAT1 with the coat protein complex II coat component Sec24 depends on a di-acidic endoplasmic reticulum export motif. Plant J. 56, 997-1006 (2008).
    • (2008) Plant J. , vol.56 , pp. 997-1006
    • Sieben, C.1    Mikosch, M.2    Brandizzi, F.3    Homann, U.4
  • 91
    • 74249088993 scopus 로고    scopus 로고
    • Golgi membrane dynamics after induction of a dominant-negative mutant Sar1 GTPase in tobacco
    • Osterrieder, A., Hummel, E., Carvalho, C. M. & Hawes, C. Golgi membrane dynamics after induction of a dominant-negative mutant Sar1 GTPase in tobacco. J. Exp. Bot. 61, 405-422 (2009).
    • (2009) J. Exp. Bot. , vol.61 , pp. 405-422
    • Osterrieder, A.1    Hummel, E.2    Carvalho, C.M.3    Hawes, C.4
  • 93
    • 58149185093 scopus 로고    scopus 로고
    • Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes
    • Schoberer, J. et al. Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes. Traffic 10, 101-115 (2009).
    • (2009) Traffic , vol.10 , pp. 101-115
    • Schoberer, J.1
  • 94
    • 73249134381 scopus 로고    scopus 로고
    • A missense mutation in the Arabidopsis COPII coat protein Sec24A induces the formation of clusters of the endoplasmic reticulum and Golgi apparatus
    • Faso, C. et al. A missense mutation in the Arabidopsis COPII coat protein Sec24A induces the formation of clusters of the endoplasmic reticulum and Golgi apparatus. Plant Cell 21, 3655-3671 (2009).
    • (2009) Plant Cell , vol.21 , pp. 3655-3671
    • Faso, C.1
  • 95
    • 84871897748 scopus 로고    scopus 로고
    • Cis-Golgi proteins accumulate near the ER exit sites and act as the scaffold for Golgi regeneration after brefeldin A treatment in tobacco BY-2 cells
    • Ito, Y. et al. cis-Golgi proteins accumulate near the ER exit sites and act as the scaffold for Golgi regeneration after brefeldin A treatment in tobacco BY-2 cells. Mol. Biol. Cell 23, 3203-3214 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3203-3214
    • Ito, Y.1
  • 96
    • 84871340049 scopus 로고    scopus 로고
    • ER import sites and their relationship to ER exit sites: A new model for bidirectional ER-Golgi transport in higher plants
    • Lerich, A. et al. ER import sites and their relationship to ER exit sites: a new model for bidirectional ER-Golgi transport in higher plants. Front. Plant Sci. 3, 143 (2012).
    • (2012) Front. Plant Sci. , vol.3 , pp. 143
    • Lerich, A.1
  • 98
    • 84877655719 scopus 로고    scopus 로고
    • The ER/Golgi interface-is there anything in-between? Front
    • Hawes, C. The ER/Golgi interface-is there anything in-between? Front. Plant Sci. 3, 73 (2012).
    • (2012) Plant Sci. , vol.3 , pp. 73
    • Hawes, C.1
  • 99
    • 33846041607 scopus 로고    scopus 로고
    • Identification and characterization of COPIa-and COPIb-type vesicle classes associated with plant and algal Golgi
    • Donohoe, B. S., Kang, B. H. & Staehelin, L. A. Identification and characterization of COPIa-and COPIb-type vesicle classes associated with plant and algal Golgi. Proc. Natl Acad. Sci. 104, 163-168 (2007).
    • (2007) Proc. Natl Acad. Sci. , vol.104 , pp. 163-168
    • Donohoe, B.S.1    Kang, B.H.2    Staehelin, L.A.3
  • 100
    • 33845737821 scopus 로고    scopus 로고
    • Optical tweezer micromanipulation of filamentous fungi
    • Wright, G. D., Arlt, J., Poon, W. C. & Read, N. D. Optical tweezer micromanipulation of filamentous fungi. Fungal Genet. Biol. 44, 1-13 (2007).
    • (2007) Fungal Genet. Biol. , vol.44 , pp. 1-13
    • Wright, G.D.1    Arlt, J.2    Poon, W.C.3    Read, N.D.4
  • 101
    • 79955642453 scopus 로고    scopus 로고
    • TFG-1 function in protein secretion and oncogenesis
    • Witte, K. et al. TFG-1 function in protein secretion and oncogenesis. Nature Cell Biol. 13, 550-558 (2011).
    • (2011) Nature Cell Biol. , vol.13 , pp. 550-558
    • Witte, K.1
  • 102
    • 79955880405 scopus 로고    scopus 로고
    • Sequential interactions with Sec23 control the direction of vesicle traffic
    • Lord, C. et al. Sequential interactions with Sec23 control the direction of vesicle traffic. Nature 473, 181-186 (2011).
    • (2011) Nature , vol.473 , pp. 181-186
    • Lord, C.1
  • 103
    • 0023987210 scopus 로고
    • High pressure freezing of intact plant tissues. Evaluation and characterization of novel features of the endoplasmic reticulum and associated membrane systems
    • Craig, S. & Staehelin, L. A. High pressure freezing of intact plant tissues. Evaluation and characterization of novel features of the endoplasmic reticulum and associated membrane systems. Eur. J. Cell Biol. 46, 81-93 (1988).
    • (1988) Eur. J. Cell Biol. , vol.46 , pp. 81-93
    • Craig, S.1    Staehelin, L.A.2
  • 104
    • 0036007958 scopus 로고    scopus 로고
    • Reevaluation of the effects of brefeldin A on plant cells using tobacco Bright Yellow 2 cells expressing Golgi-targeted green fluorescent protein and COPI antisera
    • Ritzenthaler, C. et al. Reevaluation of the effects of brefeldin A on plant cells using tobacco Bright Yellow 2 cells expressing Golgi-targeted green fluorescent protein and COPI antisera. Plant Cell 14, 237-261 (2002).
    • (2002) Plant Cell , vol.14 , pp. 237-261
    • Ritzenthaler, C.1
  • 105
    • 0031170901 scopus 로고    scopus 로고
    • The plant ER: A dynamic organelle composed of a large number of discrete functional domains
    • Staehelin, L. A. The plant ER: a dynamic organelle composed of a large number of discrete functional domains. Plant J. 11, 1151-1165 (1997).
    • (1997) Plant J. , vol.11 , pp. 1151-1165
    • Staehelin, L.A.1
  • 106
    • 57249095874 scopus 로고    scopus 로고
    • ER-to-Golgi transport by COPII vesicles in Arabidopsis involves a ribosome-excluding scaffold that is transferred with the vesicles to the Golgi matrix
    • Kang, B. H. & Staehelin, L. A. ER-to-Golgi transport by COPII vesicles in Arabidopsis involves a ribosome-excluding scaffold that is transferred with the vesicles to the Golgi matrix. Protoplasma 234, 51-64 (2008).
    • (2008) Protoplasma , vol.234 , pp. 51-64
    • Kang, B.H.1    Staehelin, L.A.2
  • 107
    • 84862303678 scopus 로고    scopus 로고
    • The structures of COPI-coated vesicles reveal alternate coatomer conformations and interactions
    • Faini, M. et al. The structures of COPI-coated vesicles reveal alternate coatomer conformations and interactions. Science 336, 1451-1454 (2012).
    • (2012) Science , vol.336 , pp. 1451-1454
    • Faini, M.1
  • 108
    • 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. Curr. Opin. Plant Biol. 8, 632-639 (2005).
    • (2005) Curr. Opin. Plant Biol. , vol.8 , pp. 632-639
    • Latijnhouwers, M.1    Hawes, C.2    Carvalho, C.3
  • 109
    • 84862194725 scopus 로고    scopus 로고
    • Tales of tethers and tentacles: Golgins in plants
    • Osterrieder, A. Tales of tethers and tentacles: golgins in plants. J. Microsc. 247, 68-77 (2012).
    • (2012) J. Microsc. , vol.247 , pp. 68-77
    • Osterrieder, A.1
  • 110
    • 33644756640 scopus 로고    scopus 로고
    • GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution
    • Puthenveedu, M. A., Bachert, C, Puri, S., Lanni, F. & Linstedt, A. D. GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution. Nature Cell Biol. 8, 238-248 (2006).
    • (2006) Nature Cell Biol. , vol.8 , pp. 238-248
    • Puthenveedu, M.A.1    Bachert, C.2    Puri, S.3    Lanni, F.4    Linstedt, A.D.5
  • 111
    • 84870293462 scopus 로고    scopus 로고
    • Plant transducers of the endoplasmic reticulum unfolded protein response
    • Iwata, Y. & Koizumi, N. Plant transducers of the endoplasmic reticulum unfolded protein response. Trends Plant Sci. 17, 720-727 (2012).
    • (2012) Trends Plant Sci. , vol.17 , pp. 720-727
    • Iwata, Y.1    Koizumi, N.2
  • 112
    • 29144454715 scopus 로고    scopus 로고
    • 2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission
    • 2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission. J. Cell Biol. 171, 919-924 (2005).
    • (2005) J. Cell Biol. , vol.171 , pp. 919-924
    • Bielli, A.1
  • 113
    • 0027467609 scopus 로고
    • Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum
    • Yoshihisa, T., Barlowe, C. & Schekman, R. Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum. Science 259, 1466-1468 (1993).
    • (1993) Science , vol.259 , pp. 1466-1468
    • Yoshihisa, T.1    Barlowe, C.2    Schekman, R.3
  • 114
    • 0037136560 scopus 로고    scopus 로고
    • Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat
    • Bi, X., Corpina, R. A. & Goldberg, J. Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature 419, 271-277 (2002).
    • (2002) Nature , vol.419 , pp. 271-277
    • Bi, X.1    Corpina, R.A.2    Goldberg, J.3
  • 115
    • 70649088120 scopus 로고    scopus 로고
    • Bulk flow revisited: Transport of a soluble protein in the secretory pathway
    • Thor, F., Gautschi, M., Geiger, R. & Helenius, A. Bulk flow revisited: transport of a soluble protein in the secretory pathway. Traffic 10, 1819-1830 (2009).
    • (2009) Traffic , vol.10 , pp. 1819-1830
    • Thor, F.1    Gautschi, M.2    Geiger, R.3    Helenius, A.4
  • 116
    • 0032495477 scopus 로고    scopus 로고
    • COPII-cargo interactions direct protein sorting into ER-derived transport vesicles
    • Kuehn, M. J., Herrmann, J. M. & Schekman, R. COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature 391, 187-190 (1998).
    • (1998) Nature , vol.391 , pp. 187-190
    • Kuehn, M.J.1    Herrmann, J.M.2    Schekman, R.3
  • 117
    • 0141521617 scopus 로고    scopus 로고
    • Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1
    • Giraudo, C. G. & Maccioni, H. J. Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1. Mol. Biol. Cell 14, 3753-3766 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3753-3766
    • Giraudo, C.G.1    MacCioni, H.J.2
  • 118
    • 33847357796 scopus 로고    scopus 로고
    • Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum
    • Wendeler, M. W., Paccaud, J. P. & Hauri, H. P. Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum. EMBO Rep. 8, 258-264 (2007).
    • (2007) EMBO Rep. , vol.8 , pp. 258-264
    • Wendeler, M.W.1    Paccaud, J.P.2    Hauri, H.P.3
  • 119
    • 0041526467 scopus 로고    scopus 로고
    • Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles
    • Miller, E. A. et al. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114, 497-509 (2003).
    • (2003) Cell , vol.114 , pp. 497-509
    • Miller, E.A.1
  • 120
    • 35549004893 scopus 로고    scopus 로고
    • Insights into COPII coat nucleation from the structure of Sec23. Sar1 complexed with the active fragment of Sec31
    • Bi, X., Mancias, J. D. & Goldberg, J. Insights into COPII coat nucleation from the structure of Sec23. Sar1 complexed with the active fragment of Sec31. Dev. Cell 13, 635-645 (2007).
    • (2007) Dev. Cell , vol.13 , pp. 635-645
    • Bi, X.1    Mancias, J.D.2    Goldberg, J.3
  • 121
    • 84858323525 scopus 로고    scopus 로고
    • ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p
    • Copic, A., Latham, C. F, Horlbeck, M. A., DArcangelo, J. G. & Miller, E. A. ER cargo properties specify a requirement for COPII coat rigidity mediated by Sec13p. Science 335, 1359-1362 (2012).
    • (2012) Science , vol.335 , pp. 1359-1362
    • Copic, A.1    Latham, C.F.2    Horlbeck, M.A.3    Darcangelo, J.G.4    Miller, E.A.5
  • 122
    • 18344405156 scopus 로고    scopus 로고
    • COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes
    • Matsuoka, K. et al. COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 93, 263-275 (1998).
    • (1998) Cell , vol.93 , pp. 263-275
    • Matsuoka, K.1
  • 124
    • 78650141466 scopus 로고    scopus 로고
    • Emergent properties of proteostasis-COPII coupled systems in human health and disease
    • Routledge, K. E., Gupta, V. & Balch, W. E. Emergent properties of proteostasis-COPII coupled systems in human health and disease. Mol. Membr. Biol. 27, 385-397 (2010).
    • (2010) Mol. Membr. Biol. , vol.27 , pp. 385-397
    • Routledge, K.E.1    Gupta, V.2    Balch, W.E.3
  • 125
    • 0026199864 scopus 로고
    • Proteins involved in vesicular transport and membrane fusion
    • Waters, M. G., Griff, I. C. & Rothman, J. E. Proteins involved in vesicular transport and membrane fusion. Curr. Opin. Cell Biol. 3, 615-620 (1991).
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 615-620
    • Waters, M.G.1    Griff, I.C.2    Rothman, J.E.3
  • 126
    • 0034254166 scopus 로고    scopus 로고
    • COP i domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP
    • Eugster, A., Frigerio, G., Dale, M. & Duden, R. COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP EMBO J. 19, 3905-3917 (2000).
    • (2000) EMBO J. , vol.19 , pp. 3905-3917
    • Eugster, A.1    Frigerio, G.2    Dale, M.3    Duden, R.4
  • 127
    • 80054729346 scopus 로고    scopus 로고
    • COPII and COPI traffic at the ER-Golgi interface
    • Szul, T & Sztul, E. COPII and COPI traffic at the ER-Golgi interface. Physiol. (Bethesda) 26, 348-364 (2011).
    • (2011) Physiol. (Bethesda) , vol.26 , pp. 348-364
    • Szul, T.1    Sztul, E.2
  • 128
    • 84866085700 scopus 로고    scopus 로고
    • ArfGAP1 function in COPI mediated membrane traffic: Currently debated models and comparison to other coat-binding ArfGAPs
    • Shiba, Y. & Randazzo, P. A. ArfGAP1 function in COPI mediated membrane traffic: currently debated models and comparison to other coat-binding ArfGAPs. Histol. Histopathol. 27, 1143-1153 (2012).
    • (2012) Histol. Histopathol. , vol.27 , pp. 1143-1153
    • Shiba, Y.1    Randazzo, P.A.2
  • 129
    • 0023658351 scopus 로고
    • The rate of bulk flow from the endoplasmic reticulum to the cell surface
    • Wieland, F T., Gleason, M. L., Serafini, T. A. & Rothman, J. E. The rate of bulk flow from the endoplasmic reticulum to the cell surface. Cell 50, 289-300 (1987).
    • (1987) Cell , vol.50 , pp. 289-300
    • Wieland, F.T.1    Gleason, M.L.2    Serafini, T.A.3    Rothman, J.E.4
  • 130
    • 0023988955 scopus 로고
    • Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment
    • Pelham, H. R. Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment. EMBO J. 7, 913-918 (1988).
    • (1988) EMBO J. , vol.7 , pp. 913-918
    • Pelham, H.R.1
  • 131
    • 0024308993 scopus 로고
    • Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum
    • Doms, R. W., Russ, G. & Yewdell, J. W. Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum. J. Cell Biol. 109, 61-72 (1989).
    • (1989) J. Cell Biol. , vol.109 , pp. 61-72
    • Doms, R.W.1    Russ, G.2    Yewdell, J.W.3
  • 132
    • 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
    • Lippincott-Schwartz, J., Yuan, L. C., Bonifacino, J. S. & Klausner, R. D. Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 56, 801-813 (1989).
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 133
    • 0030782188 scopus 로고    scopus 로고
    • Golgi tubule traffic and the effects of brefeldin A visualized in living cells
    • Sciaky, N. et al. Golgi tubule traffic and the effects of brefeldin A visualized in living cells. J. Cell Biol. 139, 1137-1155 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 1137-1155
    • Sciaky, N.1
  • 134
    • 14844333247 scopus 로고    scopus 로고
    • Dynamics of GBF1, a brefeldin A-sensitive Arf1 exchange factor at the Golgi
    • Niu, T. K., Pfeifer, A. C., Lippincott-Schwartz, J. & Jackson, C. L. Dynamics of GBF1, a brefeldin A-sensitive Arf1 exchange factor at the Golgi. Mol. Biol. Cell 16, 1213-1222 (2005).
    • (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
  • 135
    • 34547202930 scopus 로고    scopus 로고
    • Functional diversification of closely related ARF-GEFs in protein secretion and recycling
    • Richter, S. et al. Functional diversification of closely related ARF-GEFs in protein secretion and recycling. Nature 448, 488-492 (2007).
    • (2007) Nature , vol.448 , pp. 488-492
    • Richter, S.1
  • 136
    • 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
    • Peyroche, A. et al. Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain. Mol. Cell 3, 275-285 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 275-285
    • Peyroche, A.1
  • 137
    • 0035024551 scopus 로고    scopus 로고
    • Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis-Golgi tethering
    • Moyer, B. D., Allan, B. B. & Balch, W. E. Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis-Golgi tethering. Traffic 2, 268-276 (2001).
    • (2001) Traffic , vol.2 , pp. 268-276
    • Moyer, B.D.1    Allan, B.B.2    Balch, W.E.3
  • 138
    • 0036544571 scopus 로고    scopus 로고
    • Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115
    • Shorter, J., Beard, M. B., Seemann, J., Dirac-Svejstrup, A. B. & Warren, G. Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115. J. Cell Biol. 157, 45-62 (2002).
    • (2002) J. Cell Biol. , vol.157 , pp. 45-62
    • Shorter, J.1    Beard, M.B.2    Seemann, J.3    Dirac-Svejstrup, A.B.4    Warren, G.5
  • 139
    • 0035102194 scopus 로고    scopus 로고
    • TRAPP i implicated in the specificity of tethering in ER-to-Golgi transport
    • Sacher, M. et al. TRAPP I implicated in the specificity of tethering in ER-to-Golgi transport. Mol. Cell 7, 433-442 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 433-442
    • Sacher, M.1
  • 140
    • 45449083834 scopus 로고    scopus 로고
    • The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes
    • Cai, Y. et al. The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes. Cell 133, 1202-1213 (2008).
    • (2008) Cell , vol.133 , pp. 1202-1213
    • Cai, Y.1
  • 141
    • 0030890594 scopus 로고    scopus 로고
    • Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells
    • Hay, J. C., Chao, D. S., Kuo, C. S. & Scheller, R. H. Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells. Cell 89, 149-158 (1997).
    • (1997) Cell , vol.89 , pp. 149-158
    • Hay, J.C.1    Chao, D.S.2    Kuo, C.S.3    Scheller, R.H.4
  • 142
    • 0032579295 scopus 로고    scopus 로고
    • Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates
    • Rowe, T., Dascher, C., Bannykh, S., Plutner, H. & Balch, W. E. Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates. Science 279, 696-700 (1998).
    • (1998) Science , vol.279 , pp. 696-700
    • Rowe, T.1    Dascher, C.2    Bannykh, S.3    Plutner, H.4    Balch, W.E.5
  • 143
    • 0034671727 scopus 로고    scopus 로고
    • Subunit structure of a mammalian ER/Golgi SNARE complex
    • Xu, D., Joglekar, A. P., Williams, A. L. & Hay, J. C. Subunit structure of a mammalian ER/Golgi SNARE complex. J. Biol. Chem. 275, 39631-39639 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 39631-39639
    • Xu, D.1    Joglekar, A.P.2    Williams, A.L.3    Hay, J.C.4
  • 144
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: Minimal machinery for membrane fusion
    • Weber, T. et al. SNAREpins: minimal machinery for membrane fusion. Cell 92, 759-772 (1998).
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1
  • 145
    • 0034648797 scopus 로고    scopus 로고
    • Topological restriction of SNARE-dependent membrane fusion
    • Parlati, F. et al. Topological restriction of SNARE-dependent membrane fusion. Nature 407, 194-198 (2000).
    • (2000) Nature , vol.407 , pp. 194-198
    • Parlati, F.1
  • 146
    • 0036193747 scopus 로고    scopus 로고
    • Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif
    • Yamaguchi, T. et al. Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif. Dev. Cell 2, 295-305 (2002).
    • (2002) Dev. Cell , vol.2 , pp. 295-305
    • Yamaguchi, T.1
  • 147
    • 84862216994 scopus 로고    scopus 로고
    • The structure of the Sec13/31 COPII cage bound to Sec23
    • Bhattacharya, N., O'Donnell, J. & Stagg, S. M. The structure of the Sec13/31 COPII cage bound to Sec23. J. Mol. Biol. 420, 324-334 (2012).
    • (2012) J. Mol. Biol. , vol.420 , pp. 324-334
    • Bhattacharya, N.1    O'Donnell, J.2    Stagg, S.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.