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Volumn 583, Issue 23, 2009, Pages 3847-3856

Shaping tubular carriers for intracellular membrane transport

Author keywords

Biosynthetic pathway; Endocytosis; Membrane tubule; Transport carrier

Indexed keywords

CLATHRIN; COAT PROTEIN COMPLEX I; DYNAMIN;

EID: 70450240894     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.10.031     Document Type: Review
Times cited : (21)

References (112)
  • 3
    • 0025228404 scopus 로고
    • Tubulovesicular processes emerge from trans-Golgi cisternae, extend along microtubules, and interlink adjacent trans-golgi elements into a reticulum
    • Cooper M.S., Cornell-Bell A.H., Chernjavsky A., Dani J.W., and Smith S.J. Tubulovesicular processes emerge from trans-Golgi cisternae, extend along microtubules, and interlink adjacent trans-golgi elements into a reticulum. Cell 61 (1990) 135-145
    • (1990) Cell , vol.61 , pp. 135-145
    • Cooper, M.S.1    Cornell-Bell, A.H.2    Chernjavsky, A.3    Dani, J.W.4    Smith, S.J.5
  • 4
    • 0028339264 scopus 로고
    • In migrating fibroblasts, recycling receptors are concentrated in narrow tubules in the pericentriolar area, and then routed to the plasma membrane of the leading lamella
    • Hopkins C.R., Gibson A., Shipman M., Strickland D.K., and Trowbridge I.S. In migrating fibroblasts, recycling receptors are concentrated in narrow tubules in the pericentriolar area, and then routed to the plasma membrane of the leading lamella. J. Cell Biol. 125 (1994) 1265-1274
    • (1994) J. Cell Biol. , vol.125 , pp. 1265-1274
    • Hopkins, C.R.1    Gibson, A.2    Shipman, M.3    Strickland, D.K.4    Trowbridge, I.S.5
  • 6
    • 17744372521 scopus 로고    scopus 로고
    • Dynamics of secretory membrane trafficking
    • Lippincott-Schwartz J. Dynamics of secretory membrane trafficking. Ann. NY Acad. Sci. 1038 (2004) 115-124
    • (2004) Ann. NY Acad. Sci. , vol.1038 , pp. 115-124
    • Lippincott-Schwartz, J.1
  • 8
    • 33748313351 scopus 로고    scopus 로고
    • Retrograde transport from endosomes to the trans-Golgi network
    • Bonifacino J.S., and Rojas R. Retrograde transport from endosomes to the trans-Golgi network. Nat. Rev. Mol. Cell Biol. 7 (2006) 568-579
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 568-579
    • Bonifacino, J.S.1    Rojas, R.2
  • 9
    • 0035071569 scopus 로고    scopus 로고
    • Illuminating the secretory pathway: when do we need vesicles?
    • Stephens D.J., and Pepperkok R. Illuminating the secretory pathway: when do we need vesicles?. J. Cell Sci. 114 (2001) 1053-1059
    • (2001) J. Cell Sci. , vol.114 , pp. 1053-1059
    • Stephens, D.J.1    Pepperkok, R.2
  • 10
    • 33751168961 scopus 로고    scopus 로고
    • The formation of TGN-to-plasma-membrane transport carriers
    • Bard F., and Malhotra V. The formation of TGN-to-plasma-membrane transport carriers. Annu. Rev. Cell Dev. Biol. 22 (2006) 439-455
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 439-455
    • Bard, F.1    Malhotra, V.2
  • 11
    • 0345687308 scopus 로고    scopus 로고
    • Mechanism of constitutive export from the golgi: bulk flow via the formation, protrusion, and en bloc cleavage of large trans-golgi network tubular domains
    • Polishchuk E.V., Di Pentima A., Luini A., and Polishchuk R.S. Mechanism of constitutive export from the golgi: bulk flow via the formation, protrusion, and en bloc cleavage of large trans-golgi network tubular domains. Mol. Biol. Cell 14 (2003) 4470-4485
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4470-4485
    • Polishchuk, E.V.1    Di Pentima, A.2    Luini, A.3    Polishchuk, R.S.4
  • 12
    • 18844393740 scopus 로고    scopus 로고
    • Possible role of deep tubular invaginations of the plasma membrane in MHC-I trafficking
    • Massol R.H., Larsen J.E., and Kirchhausen T. Possible role of deep tubular invaginations of the plasma membrane in MHC-I trafficking. Exp. Cell Res. 306 (2005) 142-149
    • (2005) Exp. Cell Res. , vol.306 , pp. 142-149
    • Massol, R.H.1    Larsen, J.E.2    Kirchhausen, T.3
  • 13
    • 1842681953 scopus 로고    scopus 로고
    • Direct continuities between cisternae at different levels of the Golgi complex in glucose-stimulated mouse islet beta cells
    • Marsh B.J., Volkmann N., McIntosh J.R., and Howell K.E. Direct continuities between cisternae at different levels of the Golgi complex in glucose-stimulated mouse islet beta cells. Proc. Natl. Acad. Sci. USA 101 (2004) 5565-5570
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5565-5570
    • Marsh, B.J.1    Volkmann, N.2    McIntosh, J.R.3    Howell, K.E.4
  • 14
    • 7944220328 scopus 로고    scopus 로고
    • Secretory traffic triggers the formation of tubular continuities across Golgi sub-compartments
    • Trucco A., et al. Secretory traffic triggers the formation of tubular continuities across Golgi sub-compartments. Nat. Cell Biol. 6 (2004) 1071-1081
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1071-1081
    • Trucco, A.1
  • 15
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon H.T., and Gallop J.L. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438 (2005) 590-596
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 16
    • 33745737926 scopus 로고    scopus 로고
    • Membrane deformation by protein coats
    • Antonny B. Membrane deformation by protein coats. Curr. Opin. Cell Biol. 18 (2006) 386-394
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 386-394
    • Antonny, B.1
  • 17
    • 45849124923 scopus 로고    scopus 로고
    • Endosomal sorting and signalling: an emerging role for sorting nexins
    • Cullen P.J. Endosomal sorting and signalling: an emerging role for sorting nexins. Nat. Rev. Mol. Cell Biol. 9 (2008) 574-582
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 574-582
    • Cullen, P.J.1
  • 18
    • 0037605881 scopus 로고    scopus 로고
    • Phospholipase A2 (PLA2) enzymes in membrane trafficking: mediators of membrane shape and function
    • Brown W.J., Chambers K., and Doody A. Phospholipase A2 (PLA2) enzymes in membrane trafficking: mediators of membrane shape and function. Traffic 4 (2003) 214-221
    • (2003) Traffic , vol.4 , pp. 214-221
    • Brown, W.J.1    Chambers, K.2    Doody, A.3
  • 19
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Zimmerberg J., and Kozlov M.M. How proteins produce cellular membrane curvature. Nat. Rev. Mol. Cell Biol. 7 (2006) 9-19
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2
  • 20
    • 0346729923 scopus 로고    scopus 로고
    • The calcium binding loops of the cytosolic phospholipase A2 C2 domain specify targeting to Golgi and ER in live cells
    • Evans J.H., Gerber S.H., Murray D., and Leslie C.C. The calcium binding loops of the cytosolic phospholipase A2 C2 domain specify targeting to Golgi and ER in live cells. Mol. Biol. Cell 15 (2004) 371-383
    • (2004) Mol. Biol. Cell , vol.15 , pp. 371-383
    • Evans, J.H.1    Gerber, S.H.2    Murray, D.3    Leslie, C.C.4
  • 21
    • 70349976317 scopus 로고    scopus 로고
    • Group IV phospholipase A(2)alpha controls the formation of inter-cisternal continuities involved in intra-golgi transport
    • San Pietro E., et al. Group IV phospholipase A(2)alpha controls the formation of inter-cisternal continuities involved in intra-golgi transport. PLoS Biol. 7 (2009) e1000194
    • (2009) PLoS Biol. , vol.7
    • San Pietro, E.1
  • 22
    • 47349085612 scopus 로고    scopus 로고
    • Biophysical approaches to protein-induced membrane deformations in trafficking
    • Sens P., Johannes L., and Bassereau P. Biophysical approaches to protein-induced membrane deformations in trafficking. Curr. Opin. Cell Biol. 20 (2008) 476-482
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 476-482
    • Sens, P.1    Johannes, L.2    Bassereau, P.3
  • 28
    • 0344119435 scopus 로고    scopus 로고
    • Prefission constriction of Golgi tubular carriers driven by local lipid metabolism: a theoretical model
    • Shemesh T., Luini A., Malhotra V., Burger K.N., and Kozlov M.M. Prefission constriction of Golgi tubular carriers driven by local lipid metabolism: a theoretical model. Biophys. J. 85 (2003) 3813-3827
    • (2003) Biophys. J. , vol.85 , pp. 3813-3827
    • Shemesh, T.1    Luini, A.2    Malhotra, V.3    Burger, K.N.4    Kozlov, M.M.5
  • 29
    • 18444366155 scopus 로고    scopus 로고
    • Role of curvature and phase transition in lipid sorting and fission of membrane tubules
    • Roux A., Cuvelier D., Nassoy P., Prost J., Bassereau P., and Goud B. Role of curvature and phase transition in lipid sorting and fission of membrane tubules. EMBO J. 24 (2005) 1537-1545
    • (2005) EMBO J. , vol.24 , pp. 1537-1545
    • Roux, A.1    Cuvelier, D.2    Nassoy, P.3    Prost, J.4    Bassereau, P.5    Goud, B.6
  • 30
    • 33644821441 scopus 로고    scopus 로고
    • The multiple activities of CtBP/BARS proteins: the Golgi view
    • Corda D., Colanzi A., and Luini A. The multiple activities of CtBP/BARS proteins: the Golgi view. Trends Cell Biol. 16 (2006) 167-173
    • (2006) Trends Cell Biol. , vol.16 , pp. 167-173
    • Corda, D.1    Colanzi, A.2    Luini, A.3
  • 31
    • 0034161330 scopus 로고    scopus 로고
    • The dynamin family of mechanoenzymes: pinching in new places
    • McNiven M.A., Cao H., Pitts K.R., and Yoon Y. The dynamin family of mechanoenzymes: pinching in new places. Trends Biochem. Sci. 25 (2000) 115-120
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 115-120
    • McNiven, M.A.1    Cao, H.2    Pitts, K.R.3    Yoon, Y.4
  • 32
    • 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 (2009) 891-902
    • (2009) Cell , vol.136 , pp. 891-902
    • Saito, K.1
  • 33
    • 18244372680 scopus 로고    scopus 로고
    • Regulatory mechanisms of dynamin-dependent endocytosis
    • Takei K., Yoshida Y., and Yamada H. Regulatory mechanisms of dynamin-dependent endocytosis. J. Biochem. 137 (2005) 243-247
    • (2005) J. Biochem. , vol.137 , pp. 243-247
    • Takei, K.1    Yoshida, Y.2    Yamada, H.3
  • 34
    • 41949093447 scopus 로고    scopus 로고
    • The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS
    • Liberali P., et al. The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS. EMBO J. 27 (2008) 970-981
    • (2008) EMBO J. , vol.27 , pp. 970-981
    • Liberali, P.1
  • 35
    • 0032503947 scopus 로고    scopus 로고
    • Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes
    • Takei K., Haucke V., Slepnev V., Farsad K., Salazar M., Chen H., and De Camilli P. Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes. Cell 94 (1998) 131-141
    • (1998) Cell , vol.94 , pp. 131-141
    • Takei, K.1    Haucke, V.2    Slepnev, V.3    Farsad, K.4    Salazar, M.5    Chen, H.6    De Camilli, P.7
  • 36
    • 0033130119 scopus 로고    scopus 로고
    • Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
    • Takei K., Slepnev V.I., Haucke V., and De Camilli P. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nat. Cell Biol. 1 (1999) 33-39
    • (1999) Nat. Cell Biol. , vol.1 , pp. 33-39
    • Takei, K.1    Slepnev, V.I.2    Haucke, V.3    De Camilli, P.4
  • 38
    • 0033785991 scopus 로고    scopus 로고
    • Lumenal targeted GFP, used as a marker of soluble cargo, visualises rapid ERGIC to Golgi traffic by a tubulo-vesicular network
    • Blum R., Stephens D.J., and Schulz I. Lumenal targeted GFP, used as a marker of soluble cargo, visualises rapid ERGIC to Golgi traffic by a tubulo-vesicular network. J. Cell Sci. 113 Pt 18 (2000) 3151-3159
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 18 , pp. 3151-3159
    • Blum, R.1    Stephens, D.J.2    Schulz, I.3
  • 39
    • 31944449219 scopus 로고    scopus 로고
    • Biogenesis of tubular ER-to-Golgi transport intermediates
    • Simpson J.C., Nilsson T., and Pepperkok R. Biogenesis of tubular ER-to-Golgi transport intermediates. Mol. Biol. Cell 17 (2006) 723-737
    • (2006) Mol. Biol. Cell , vol.17 , pp. 723-737
    • Simpson, J.C.1    Nilsson, T.2    Pepperkok, R.3
  • 40
    • 10744221460 scopus 로고    scopus 로고
    • ER-to-Golgi carriers arise through direct en bloc protrusion and multistage maturation of specialized ER exit domains
    • Mironov A.A., et al. ER-to-Golgi carriers arise through direct en bloc protrusion and multistage maturation of specialized ER exit domains. Dev. Cell 5 (2003) 583-594
    • (2003) Dev. Cell , vol.5 , pp. 583-594
    • Mironov, A.A.1
  • 41
    • 0030814254 scopus 로고    scopus 로고
    • COPII and secretory cargo capture into transport vesicles
    • Kuehn M.J., and Schekman R. COPII and secretory cargo capture into transport vesicles. Curr. Opin. Cell Biol. 9 (1997) 477-483
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 477-483
    • Kuehn, M.J.1    Schekman, R.2
  • 42
    • 0030742746 scopus 로고    scopus 로고
    • Membrane dynamics at the endoplasmic reticulum-Golgi interface
    • Bannykh S.I., and Balch W.E. Membrane dynamics at the endoplasmic reticulum-Golgi interface. J. Cell Biol. 138 (1997) 1-4
    • (1997) J. Cell Biol. , vol.138 , pp. 1-4
    • Bannykh, S.I.1    Balch, W.E.2
  • 43
    • 11244273061 scopus 로고    scopus 로고
    • Reconstitution of COPII vesicle fusion to generate a pre-Golgi intermediate compartment
    • Xu D., and Hay J.C. Reconstitution of COPII vesicle fusion to generate a pre-Golgi intermediate compartment. J. Cell Biol. 167 (2004) 997-1003
    • (2004) J. Cell Biol. , vol.167 , pp. 997-1003
    • Xu, D.1    Hay, J.C.2
  • 44
    • 0033917563 scopus 로고    scopus 로고
    • COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites
    • Stephens D.J., Lin-Marq N., Pagano A., Pepperkok R., and Paccaud J.P. COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites. J. Cell Sci. 113 Pt 12 (2000) 2177-2185
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 12 , pp. 2177-2185
    • Stephens, D.J.1    Lin-Marq, N.2    Pagano, A.3    Pepperkok, R.4    Paccaud, J.P.5
  • 45
    • 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 (1998) 993-1003
    • (1998) Cell , vol.95 , pp. 993-1003
    • Bonfanti, L.1
  • 46
    • 22044441866 scopus 로고    scopus 로고
    • COPII-coated vesicles: flexible enough for large cargo?
    • Fromme J.C., and Schekman R. COPII-coated vesicles: flexible enough for large cargo?. Curr. Opin. Cell Biol. 17 (2005) 345-352
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 345-352
    • Fromme, J.C.1    Schekman, R.2
  • 47
    • 0037087610 scopus 로고    scopus 로고
    • Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells
    • Stephens D.J., and Pepperkok R. Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells. J. Cell Sci. 115 (2002) 1149-1160
    • (2002) J. Cell Sci. , vol.115 , pp. 1149-1160
    • Stephens, D.J.1    Pepperkok, R.2
  • 48
    • 23944488301 scopus 로고    scopus 로고
    • Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle
    • Lee M.C., Orci L., Hamamoto S., Futai E., Ravazzola M., and Schekman R. Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 122 (2005) 605-617
    • (2005) Cell , vol.122 , pp. 605-617
    • Lee, M.C.1    Orci, L.2    Hamamoto, S.3    Futai, E.4    Ravazzola, M.5    Schekman, R.6
  • 51
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • Scales S.J., Pepperkok R., and Kreis T.E. Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell 90 (1997) 1137-1148
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 52
    • 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., and Klumperman J. Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI-coated vesicles. Cell 98 (1999) 81-90
    • (1999) Cell , vol.98 , pp. 81-90
    • Martinez-Menarguez, J.A.1    Geuze, H.J.2    Slot, J.W.3    Klumperman, J.4
  • 53
    • 0035203528 scopus 로고    scopus 로고
    • The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment
    • Marra P., et al. The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment. Nat. Cell Biol. 3 (2001) 1101-1113
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1101-1113
    • Marra, P.1
  • 54
    • 14044272872 scopus 로고    scopus 로고
    • Live imaging of bidirectional traffic from the ERGIC
    • Ben-Tekaya H., Miura K., Pepperkok R., and Hauri H.P. Live imaging of bidirectional traffic from the ERGIC. J. Cell Sci. 118 (2005) 357-367
    • (2005) J. Cell Sci. , vol.118 , pp. 357-367
    • Ben-Tekaya, H.1    Miura, K.2    Pepperkok, R.3    Hauri, H.P.4
  • 55
    • 0025966562 scopus 로고
    • Three-dimensional organization of the Golgi complex observed by scanning electron microscopy
    • Tanaka K., and Fukudome H. Three-dimensional organization of the Golgi complex observed by scanning electron microscopy. J. Electron Microsc. Tech. 17 (1991) 15-23
    • (1991) J. Electron Microsc. Tech. , vol.17 , pp. 15-23
    • Tanaka, K.1    Fukudome, H.2
  • 56
    • 0028081835 scopus 로고
    • Connections between the various elements of the cis- and mid-compartments of the Golgi apparatus of early rat spermatids
    • Clermont Y., Rambourg A., and Hermo L. Connections between the various elements of the cis- and mid-compartments of the Golgi apparatus of early rat spermatids. Anat. Rec. 240 (1994) 469-480
    • (1994) Anat. Rec. , vol.240 , pp. 469-480
    • Clermont, Y.1    Rambourg, A.2    Hermo, L.3
  • 57
    • 0029163053 scopus 로고
    • Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus
    • Pelham H.R. Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus. Curr. Opin. Cell Biol. 7 (1995) 530-535
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 530-535
    • Pelham, H.R.1
  • 58
    • 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., and 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 (1989) 801-813
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 59
    • 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 (1997) 1137-1155
    • (1997) J. Cell Biol. , vol.139 , pp. 1137-1155
    • Sciaky, N.1
  • 60
    • 0033571602 scopus 로고    scopus 로고
    • Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells
    • White J., et al. Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells. J. Cell Biol. 147 (1999) 743-760
    • (1999) J. Cell Biol. , vol.147 , pp. 743-760
    • White, J.1
  • 64
    • 28444472038 scopus 로고    scopus 로고
    • Opinion: the maturing role of COPI vesicles in intra-Golgi transport
    • Rabouille C., and Klumperman J. Opinion: the maturing role of COPI vesicles in intra-Golgi transport. Nat. Rev. Mol. Cell Biol. 6 (2005) 812-817
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 812-817
    • Rabouille, C.1    Klumperman, J.2
  • 65
    • 0034278528 scopus 로고    scopus 로고
    • Gut thoughts on the Golgi complex
    • Griffiths G. Gut thoughts on the Golgi complex. Traffic 1 (2000) 738-745
    • (2000) Traffic , vol.1 , pp. 738-745
    • Griffiths, G.1
  • 66
    • 51249118719 scopus 로고    scopus 로고
    • Heterotypic tubular connections at the endoplasmic reticulum-Golgi complex interface
    • Vivero-Salmeron G., Ballesta J., and Martinez-Menarguez J.A. Heterotypic tubular connections at the endoplasmic reticulum-Golgi complex interface. Histochem. Cell Biol. 130 (2008) 709-717
    • (2008) Histochem. Cell Biol. , vol.130 , pp. 709-717
    • Vivero-Salmeron, G.1    Ballesta, J.2    Martinez-Menarguez, J.A.3
  • 67
    • 0030753006 scopus 로고    scopus 로고
    • Variations on the intracellular transport theme: maturing cisternae and trafficking tubules
    • Mironov A.A., Weidman P., and Luini A. Variations on the intracellular transport theme: maturing cisternae and trafficking tubules. J. Cell Biol. 138 (1997) 481-484
    • (1997) J. Cell Biol. , vol.138 , pp. 481-484
    • Mironov, A.A.1    Weidman, P.2    Luini, A.3
  • 69
    • 55549125212 scopus 로고    scopus 로고
    • Arf1-GTP-induced tubule formation suggests a function of Arf family proteins in curvature acquisition at sites of vesicle budding
    • Krauss M., Jia J.Y., Roux A., Beck R., Wieland F.T., De Camilli P., and Haucke V. Arf1-GTP-induced tubule formation suggests a function of Arf family proteins in curvature acquisition at sites of vesicle budding. J. Biol. Chem. 283 (2008) 27717-27723
    • (2008) J. Biol. Chem. , vol.283 , pp. 27717-27723
    • Krauss, M.1    Jia, J.Y.2    Roux, A.3    Beck, R.4    Wieland, F.T.5    De Camilli, P.6    Haucke, V.7
  • 70
    • 0027360627 scopus 로고
    • Golgi membrane dynamics imaged by freeze-etch electron microscopy: views of different membrane coatings involved in tubulation versus vesiculation
    • Weidman P., Roth R., and Heuser J. Golgi membrane dynamics imaged by freeze-etch electron microscopy: views of different membrane coatings involved in tubulation versus vesiculation. Cell 75 (1993) 123-133
    • (1993) Cell , vol.75 , pp. 123-133
    • Weidman, P.1    Roth, R.2    Heuser, J.3
  • 71
    • 0025233925 scopus 로고
    • Three-dimensional electron microscopy: structure of the Golgi apparatus
    • Rambourg A., and Clermont Y. Three-dimensional electron microscopy: structure of the Golgi apparatus. Eur. J. Cell Biol. 51 (1990) 189-200
    • (1990) Eur. J. Cell Biol. , vol.51 , pp. 189-200
    • Rambourg, A.1    Clermont, Y.2
  • 72
    • 0034627793 scopus 로고    scopus 로고
    • Correlative light-electron microscopy reveals the tubular-saccular ultrastructure of carriers operating between Golgi apparatus and plasma membrane
    • Polishchuk R.S., Polishchuk E.V., Marra P., Alberti S., Buccione R., Luini A., and Mironov A.A. Correlative light-electron microscopy reveals the tubular-saccular ultrastructure of carriers operating between Golgi apparatus and plasma membrane. J. Cell Biol. 148 (2000) 45-58
    • (2000) J. Cell Biol. , vol.148 , pp. 45-58
    • Polishchuk, R.S.1    Polishchuk, E.V.2    Marra, P.3    Alberti, S.4    Buccione, R.5    Luini, A.6    Mironov, A.A.7
  • 73
    • 33745764302 scopus 로고    scopus 로고
    • Ultrastructure of long-range transport carriers moving from the trans Golgi network to peripheral endosomes
    • Polishchuk R.S., San Pietro E., Di Pentima A., Tete S., and Bonifacino J.S. Ultrastructure of long-range transport carriers moving from the trans Golgi network to peripheral endosomes. Traffic 7 (2006) 1092-1103
    • (2006) Traffic , vol.7 , pp. 1092-1103
    • Polishchuk, R.S.1    San Pietro, E.2    Di Pentima, A.3    Tete, S.4    Bonifacino, J.S.5
  • 74
    • 0029040979 scopus 로고
    • Trans-Golgi network (TGN) of different cell types: three-dimensional structural characteristics and variability
    • Clermont Y., Rambourg A., and Hermo L. Trans-Golgi network (TGN) of different cell types: three-dimensional structural characteristics and variability. Anat. Rec. 242 (1995) 289-301
    • (1995) Anat. Rec. , vol.242 , pp. 289-301
    • Clermont, Y.1    Rambourg, A.2    Hermo, L.3
  • 75
    • 42149168460 scopus 로고    scopus 로고
    • A trans-Golgi network golgin is required for the regulated secretion of TNF in activated macrophages in vivo
    • Lieu Z.Z., Lock J.G., Hammond L.A., La Gruta N.L., Stow J.L., and Gleeson P.A. A trans-Golgi network golgin is required for the regulated secretion of TNF in activated macrophages in vivo. Proc. Natl. Acad. Sci. USA 105 (2008) 3351-3356
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3351-3356
    • Lieu, Z.Z.1    Lock, J.G.2    Hammond, L.A.3    La Gruta, N.L.4    Stow, J.L.5    Gleeson, P.A.6
  • 76
    • 0032517767 scopus 로고    scopus 로고
    • Kinetic analysis of secretory protein traffic and characterization of golgi to plasma membrane transport intermediates in living cells
    • Hirschberg K., Miller C.M., Ellenberg J., Presley J.F., Siggia E.D., Phair R.D., and Lippincott-Schwartz J. Kinetic analysis of secretory protein traffic and characterization of golgi to plasma membrane transport intermediates in living cells. J. Cell Biol. 143 (1998) 1485-1503
    • (1998) J. Cell Biol. , vol.143 , pp. 1485-1503
    • Hirschberg, K.1    Miller, C.M.2    Ellenberg, J.3    Presley, J.F.4    Siggia, E.D.5    Phair, R.D.6    Lippincott-Schwartz, J.7
  • 79
    • 0029890064 scopus 로고    scopus 로고
    • The role of the membrane-spanning domain and stalk region of N-acetylglucosaminyltransferase I in retention, kin recognition and structural maintenance of the Golgi apparatus in HeLa cells
    • Nilsson T., Rabouille C., Hui N., Watson R., and Warren G. The role of the membrane-spanning domain and stalk region of N-acetylglucosaminyltransferase I in retention, kin recognition and structural maintenance of the Golgi apparatus in HeLa cells. J. Cell Sci. 109 Pt 7 (1996) 1975-1989
    • (1996) J. Cell Sci. , vol.109 , Issue.PART 7 , pp. 1975-1989
    • Nilsson, T.1    Rabouille, C.2    Hui, N.3    Watson, R.4    Warren, G.5
  • 81
    • 0037031658 scopus 로고    scopus 로고
    • Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network
    • Doray B., Ghosh P., Griffith J., Geuze H.J., and Kornfeld S. Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network. Science 297 (2002) 1700-1703
    • (2002) Science , vol.297 , pp. 1700-1703
    • Doray, B.1    Ghosh, P.2    Griffith, J.3    Geuze, H.J.4    Kornfeld, S.5
  • 82
    • 67749122634 scopus 로고    scopus 로고
    • A gene network regulating lysosomal biogenesis and function
    • Sardiello M., et al. A gene network regulating lysosomal biogenesis and function. Science 325 (2009) 473-477
    • (2009) Science , vol.325 , pp. 473-477
    • Sardiello, M.1
  • 83
    • 34347346147 scopus 로고    scopus 로고
    • High-pressure freezing provides insights into Weibel-Palade body biogenesis
    • Zenner H.L., Collinson L.M., Michaux G., and Cutler D.F. High-pressure freezing provides insights into Weibel-Palade body biogenesis. J. Cell Sci. 120 (2007) 2117-2125
    • (2007) J. Cell Sci. , vol.120 , pp. 2117-2125
    • Zenner, H.L.1    Collinson, L.M.2    Michaux, G.3    Cutler, D.F.4
  • 85
    • 34249885619 scopus 로고    scopus 로고
    • Lipid-transfer proteins in membrane trafficking at the Golgi complex
    • De Matteis M.A., Di Campli A., and D'Angelo G. Lipid-transfer proteins in membrane trafficking at the Golgi complex. Biochim. Biophys. Acta 1771 (2007) 761-768
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 761-768
    • De Matteis, M.A.1    Di Campli, A.2    D'Angelo, G.3
  • 87
    • 34548498611 scopus 로고    scopus 로고
    • Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide
    • D'Angelo G., et al. Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide. Nature 449 (2007) 62-67
    • (2007) Nature , vol.449 , pp. 62-67
    • D'Angelo, G.1
  • 88
    • 0032975218 scopus 로고    scopus 로고
    • Modulation of nanotube formation by structural modifications of sphingolipids
    • Kulkarni V.S., Boggs J.M., and Brown R.E. Modulation of nanotube formation by structural modifications of sphingolipids. Biophys. J. 77 (1999) 319-330
    • (1999) Biophys. J. , vol.77 , pp. 319-330
    • Kulkarni, V.S.1    Boggs, J.M.2    Brown, R.E.3
  • 89
    • 2342556630 scopus 로고    scopus 로고
    • FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P
    • Godi A., et al. FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. Nat. Cell Biol. 6 (2004) 393-404
    • (2004) Nat. Cell Biol. , vol.6 , pp. 393-404
    • Godi, A.1
  • 90
    • 0032897432 scopus 로고    scopus 로고
    • Dual-color visualization of trans-Golgi network to plasma membrane traffic along microtubules in living cells
    • Toomre D., Keller P., White J., Olivo J.C., and Simons K. Dual-color visualization of trans-Golgi network to plasma membrane traffic along microtubules in living cells. J. Cell Sci. 112 Pt 1 (1999) 21-33
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 1 , pp. 21-33
    • Toomre, D.1    Keller, P.2    White, J.3    Olivo, J.C.4    Simons, K.5
  • 91
    • 0034599547 scopus 로고    scopus 로고
    • Fusion of constitutive membrane traffic with the cell surface observed by evanescent wave microscopy
    • Toomre D., Steyer J.A., Keller P., Almers W., and Simons K. Fusion of constitutive membrane traffic with the cell surface observed by evanescent wave microscopy. J. Cell Biol. 149 (2000) 33-40
    • (2000) J. Cell Biol. , vol.149 , pp. 33-40
    • Toomre, D.1    Steyer, J.A.2    Keller, P.3    Almers, W.4    Simons, K.5
  • 92
    • 0034599767 scopus 로고    scopus 로고
    • Imaging constitutive exocytosis with total internal reflection fluorescence microscopy
    • Schmoranzer J., Goulian M., Axelrod D., and Simon S.M. Imaging constitutive exocytosis with total internal reflection fluorescence microscopy. J. Cell Biol. 149 (2000) 23-32
    • (2000) J. Cell Biol. , vol.149 , pp. 23-32
    • Schmoranzer, J.1    Goulian, M.2    Axelrod, D.3    Simon, S.M.4
  • 93
    • 0038185307 scopus 로고    scopus 로고
    • Role of microtubules in fusion of post-Golgi vesicles to the plasma membrane
    • Schmoranzer J., and Simon S.M. Role of microtubules in fusion of post-Golgi vesicles to the plasma membrane. Mol. Biol. Cell 14 (2003) 1558-1569
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1558-1569
    • Schmoranzer, J.1    Simon, S.M.2
  • 94
    • 0344034726 scopus 로고    scopus 로고
    • Migrating fibroblasts perform polarized, microtubule-dependent exocytosis towards the leading edge
    • Schmoranzer J., Kreitzer G., and Simon S.M. Migrating fibroblasts perform polarized, microtubule-dependent exocytosis towards the leading edge. J. Cell Sci. 116 (2003) 4513-4519
    • (2003) J. Cell Sci. , vol.116 , pp. 4513-4519
    • Schmoranzer, J.1    Kreitzer, G.2    Simon, S.M.3
  • 95
    • 2342599664 scopus 로고    scopus 로고
    • Delivery of raft-associated, GPI-anchored proteins to the apical surface of polarized MDCK cells by a transcytotic pathway
    • Polishchuk R., Di Pentima A., and Lippincott-Schwartz J. Delivery of raft-associated, GPI-anchored proteins to the apical surface of polarized MDCK cells by a transcytotic pathway. Nat. Cell Biol. 6 (2004) 297-307
    • (2004) Nat. Cell Biol. , vol.6 , pp. 297-307
    • Polishchuk, R.1    Di Pentima, A.2    Lippincott-Schwartz, J.3
  • 96
    • 0035370951 scopus 로고    scopus 로고
    • The exocyst complex associates with microtubules to mediate vesicle targeting and neurite outgrowth
    • Vega I.E., and Hsu S.C. The exocyst complex associates with microtubules to mediate vesicle targeting and neurite outgrowth. J. Neurosci. 21 (2001) 3839-3848
    • (2001) J. Neurosci. , vol.21 , pp. 3839-3848
    • Vega, I.E.1    Hsu, S.C.2
  • 98
    • 2542439729 scopus 로고    scopus 로고
    • Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon
    • Canty E.G., Lu Y., Meadows R.S., Shaw M.K., Holmes D.F., and Kadler K.E. Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon. J. Cell Biol. 165 (2004) 553-563
    • (2004) J. Cell Biol. , vol.165 , pp. 553-563
    • Canty, E.G.1    Lu, Y.2    Meadows, R.S.3    Shaw, M.K.4    Holmes, D.F.5    Kadler, K.E.6
  • 99
    • 0037175399 scopus 로고    scopus 로고
    • Neural cell adhesion molecule promotes accumulation of TGN organelles at sites of neuron-to-neuron contacts
    • Sytnyk V., Leshchyns'ka I., Delling M., Dityateva G., Dityatev A., and Schachner M. Neural cell adhesion molecule promotes accumulation of TGN organelles at sites of neuron-to-neuron contacts. J. Cell Biol. 159 (2002) 649-661
    • (2002) J. Cell Biol. , vol.159 , pp. 649-661
    • Sytnyk, V.1    Leshchyns'ka, I.2    Delling, M.3    Dityateva, G.4    Dityatev, A.5    Schachner, M.6
  • 100
    • 8444221583 scopus 로고    scopus 로고
    • Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells
    • Ang A.L., Taguchi T., Francis S., Folsch H., Murrells L.J., Pypaert M., Warren G., and Mellman I. Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells. J. Cell Biol. 167 (2004) 531-543
    • (2004) J. Cell Biol. , vol.167 , pp. 531-543
    • Ang, A.L.1    Taguchi, T.2    Francis, S.3    Folsch, H.4    Murrells, L.J.5    Pypaert, M.6    Warren, G.7    Mellman, I.8
  • 101
    • 16344363943 scopus 로고    scopus 로고
    • Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin
    • Lock J.G., and Stow J.L. Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin. Mol. Biol. Cell 16 (2005) 1744-1755
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1744-1755
    • Lock, J.G.1    Stow, J.L.2
  • 103
    • 62149144498 scopus 로고    scopus 로고
    • SNX9 - a prelude to vesicle release
    • Lundmark R., and Carlsson S.R. SNX9 - a prelude to vesicle release. J. Cell Sci. 122 (2009) 5-11
    • (2009) J. Cell Sci. , vol.122 , pp. 5-11
    • Lundmark, R.1    Carlsson, S.R.2
  • 104
    • 33748288113 scopus 로고    scopus 로고
    • BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature
    • Itoh T., and De Camilli P. BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature. Biochim. Biophys. Acta 1761 (2006) 897-912
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 897-912
    • Itoh, T.1    De Camilli, P.2
  • 105
    • 56949091061 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis: a unique platform for cell signaling and PM remodeling
    • Donaldson J.G., Porat-Shliom N., and Cohen L.A. Clathrin-independent endocytosis: a unique platform for cell signaling and PM remodeling. Cell Signal. 21 (2009) 1-6
    • (2009) Cell Signal. , vol.21 , pp. 1-6
    • Donaldson, J.G.1    Porat-Shliom, N.2    Cohen, L.A.3
  • 106
    • 50949133967 scopus 로고    scopus 로고
    • Arf family GTP loading is activated by, and generates, positive membrane curvature
    • Lundmark R., Doherty G.J., Vallis Y., Peter B.J., and McMahon H.T. Arf family GTP loading is activated by, and generates, positive membrane curvature. Biochem. J. 414 (2008) 189-194
    • (2008) Biochem. J. , vol.414 , pp. 189-194
    • Lundmark, R.1    Doherty, G.J.2    Vallis, Y.3    Peter, B.J.4    McMahon, H.T.5
  • 107
    • 39749200034 scopus 로고    scopus 로고
    • Imaging and imagination: understanding the endo-lysosomal system
    • van Meel E., and Klumperman J. Imaging and imagination: understanding the endo-lysosomal system. Histochem. Cell Biol. 129 (2008) 253-266
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 253-266
    • van Meel, E.1    Klumperman, J.2
  • 108
    • 13944258097 scopus 로고    scopus 로고
    • Endocytic delivery to lysosomes mediated by concurrent fusion and kissing events in living cells
    • Bright N.A., Gratian M.J., and Luzio J.P. Endocytic delivery to lysosomes mediated by concurrent fusion and kissing events in living cells. Curr. Biol. 15 (2005) 360-365
    • (2005) Curr. Biol. , vol.15 , pp. 360-365
    • Bright, N.A.1    Gratian, M.J.2    Luzio, J.P.3
  • 109
    • 0042691817 scopus 로고    scopus 로고
    • Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: role of Rab7 and RILP
    • Harrison R.E., Bucci C., Vieira O.V., Schroer T.A., and Grinstein S. Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: role of Rab7 and RILP. Mol. Cell Biol. 23 (2003) 6494-6506
    • (2003) Mol. Cell Biol. , vol.23 , pp. 6494-6506
    • Harrison, R.E.1    Bucci, C.2    Vieira, O.V.3    Schroer, T.A.4    Grinstein, S.5
  • 110
    • 0035494424 scopus 로고    scopus 로고
    • Reorganization of multivesicular bodies regulates MHC class II antigen presentation by dendritic cells
    • Kleijmeer M., et al. Reorganization of multivesicular bodies regulates MHC class II antigen presentation by dendritic cells. J. Cell Biol. 155 (2001) 53-63
    • (2001) J. Cell Biol. , vol.155 , pp. 53-63
    • Kleijmeer, M.1
  • 111
    • 34249779825 scopus 로고    scopus 로고
    • Tubulation of class II MHC compartments is microtubule dependent and involves multiple endolysosomal membrane proteins in primary dendritic cells
    • Vyas J.M., Kim Y.M., Artavanis-Tsakonas K., Love J.C., Van der Veen A.G., and Ploegh H.L. Tubulation of class II MHC compartments is microtubule dependent and involves multiple endolysosomal membrane proteins in primary dendritic cells. J. Immunol. 178 (2007) 7199-7210
    • (2007) J. Immunol. , vol.178 , pp. 7199-7210
    • Vyas, J.M.1    Kim, Y.M.2    Artavanis-Tsakonas, K.3    Love, J.C.4    Van der Veen, A.G.5    Ploegh, H.L.6
  • 112
    • 65649085175 scopus 로고    scopus 로고
    • Faciogenital dysplasia protein (FGD1) regulates export of cargo proteins from the golgi complex via Cdc42 activation
    • Egorov M.V., et al. Faciogenital dysplasia protein (FGD1) regulates export of cargo proteins from the golgi complex via Cdc42 activation. Mol. Biol. Cell 20 (2009) 2413-2427
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2413-2427
    • Egorov, M.V.1


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