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Volumn 583, Issue 23, 2009, Pages 3804-3810

Emerging new roles of the pre-Golgi intermediate compartment in biosynthetic-secretory trafficking

Author keywords

Centrosome; Endosome; Golgi bypass pathway; Intermediate compartment; Polarized trafficking

Indexed keywords

COAT PROTEIN COMPLEX I; ENDOPLASMIC RETICULUM GOLGI INTERMEDIATE COMPARTMENT PROTEIN 53; PROTEIN P58; RAB PROTEIN;

EID: 70450221903     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.10.084     Document Type: Review
Times cited : (29)

References (78)
  • 1
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein secretion
    • Palade G.E. Intracellular aspects of the process of protein secretion. Science 189 (1975) 347-358
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.E.1
  • 2
    • 13444257689 scopus 로고    scopus 로고
    • Regulated exocytosis: new organelles for non-secretory purposes
    • Chieregatti E., and Meldolesi J. Regulated exocytosis: new organelles for non-secretory purposes. Nat. Rev. Mol. Cell Biol. 6 (2005) 181-187
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 181-187
    • Chieregatti, E.1    Meldolesi, J.2
  • 3
    • 62849088750 scopus 로고    scopus 로고
    • Plasma membrane expansion: a neuron's Herculean task
    • Pfenninger K.H. Plasma membrane expansion: a neuron's Herculean task. Nat. Rev. Neurosci. 10 (2009) 251-261
    • (2009) Nat. Rev. Neurosci. , vol.10 , pp. 251-261
    • Pfenninger, K.H.1
  • 4
    • 33748466150 scopus 로고    scopus 로고
    • Endocytic recycling pathways: emerging regulators of cell migration
    • Jones M.C., Caswell P.T., and Norman J.C. Endocytic recycling pathways: emerging regulators of cell migration. Curr. Opin. Cell Biol. 18 (2006) 549-557
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 549-557
    • Jones, M.C.1    Caswell, P.T.2    Norman, J.C.3
  • 6
    • 33750610006 scopus 로고    scopus 로고
    • Rab35 regulates an endocytic recycling pathway essential for the terminal steps of cytokinesis
    • Kouranti I., Sachse M., Arouche N., Goud B., and Echard A. Rab35 regulates an endocytic recycling pathway essential for the terminal steps of cytokinesis. Curr. Biol. 16 (2006) 1719-1725
    • (2006) Curr. Biol. , vol.16 , pp. 1719-1725
    • Kouranti, I.1    Sachse, M.2    Arouche, N.3    Goud, B.4    Echard, A.5
  • 7
    • 70350417461 scopus 로고    scopus 로고
    • Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia
    • Poincloux R., Lizárraga F., and Chavrier P. Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia. J. Cell Sci. 122 (2009) 3015-3030
    • (2009) J. Cell Sci. , vol.122 , pp. 3015-3030
    • Poincloux, R.1    Lizárraga, F.2    Chavrier, P.3
  • 8
    • 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
  • 9
    • 0036141434 scopus 로고    scopus 로고
    • The exocyst complex binds the small GTPase RalA to mediate filopodia formation
    • Sugihara K., Asano S., Tanaka K., Iwamatsu A., Okawa K., and Ohta Y. The exocyst complex binds the small GTPase RalA to mediate filopodia formation. Nat. Cell Biol. 4 (2002) 73-78
    • (2002) Nat. Cell Biol. , vol.4 , pp. 73-78
    • Sugihara, K.1    Asano, S.2    Tanaka, K.3    Iwamatsu, A.4    Okawa, K.5    Ohta, Y.6
  • 11
    • 38849095347 scopus 로고    scopus 로고
    • DGRASP-mediated noncanonical integrin secretion is required for Drosophila epithelial remodeling
    • Schotman H., Karhinen L., and Rabouille C. DGRASP-mediated noncanonical integrin secretion is required for Drosophila epithelial remodeling. Dev. Cell 14 (2008) 171-182
    • (2008) Dev. Cell , vol.14 , pp. 171-182
    • Schotman, H.1    Karhinen, L.2    Rabouille, C.3
  • 12
  • 13
    • 69249106881 scopus 로고    scopus 로고
    • Pathways and mechanisms of endocytic recycling
    • Grant B.D., and Donaldson J.G. Pathways and mechanisms of endocytic recycling. Nat. Rev. Mol. Cell Biol. 10 (2009) 597-608
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 597-608
    • Grant, B.D.1    Donaldson, J.G.2
  • 15
    • 33744532148 scopus 로고    scopus 로고
    • Recycling endosomes
    • van Ijzendoorn S.C. Recycling endosomes. J. Cell Sci. 119 (2006) 1679-1681
    • (2006) J. Cell Sci. , vol.119 , pp. 1679-1681
    • van Ijzendoorn, S.C.1
  • 16
    • 33745841364 scopus 로고    scopus 로고
    • The exocyst defrocked, a framework of rods revealed
    • Munson M., and Novick P. The exocyst defrocked, a framework of rods revealed. Nat. Struct. Mol. Biol. 13 (2006) 577-581
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 577-581
    • Munson, M.1    Novick, P.2
  • 17
    • 67949106616 scopus 로고    scopus 로고
    • The exocyst complex in polarized exocytosis
    • He B., and Guo W. The exocyst complex in polarized exocytosis. Curr. Opin. Cell Biol. 21 (2009) 537-542
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 537-542
    • He, B.1    Guo, W.2
  • 18
    • 69949103110 scopus 로고    scopus 로고
    • The role of the exocyst in matrix metalloproteinase secretion and actin dynamics during tumor cell invadopodia formation
    • Liu J., Yue P., Artym V.V., Mueller S.C., and Guo W. The role of the exocyst in matrix metalloproteinase secretion and actin dynamics during tumor cell invadopodia formation. Mol. Biol. Cell 20 (2009) 3763-3771
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3763-3771
    • Liu, J.1    Yue, P.2    Artym, V.V.3    Mueller, S.C.4    Guo, W.5
  • 20
    • 8444221583 scopus 로고    scopus 로고
    • Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane in MDCK cells
    • Ang A.L., Taguchi T., Francis S., Fölsch H., Murrels L.J., Pypaert M., Warren G., and Mellman I. Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane in 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    Fölsch, H.4    Murrels, L.J.5    Pypaert, M.6    Warren, G.7    Mellman, I.8
  • 21
    • 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
  • 22
    • 70350120449 scopus 로고    scopus 로고
    • The function of the intermediate compartment in pre-Golgi trafficking involves its stable connection with the centrosome
    • Marie M., Dale H.A., Sannerud R., and Saraste J. The function of the intermediate compartment in pre-Golgi trafficking involves its stable connection with the centrosome. Mol. Biol. Cell 20 (2009) 4458-4470
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4458-4470
    • Marie, M.1    Dale, H.A.2    Sannerud, R.3    Saraste, J.4
  • 23
    • 0026934508 scopus 로고
    • Pathways of protein sorting and membrane traffic between the endoplasmic reticulum and the Golgi complex
    • Saraste J., and Kuismanen E. Pathways of protein sorting and membrane traffic between the endoplasmic reticulum and the Golgi complex. Sem. Cell Biol. 3 (1992) 343-355
    • (1992) Sem. Cell Biol. , vol.3 , pp. 343-355
    • Saraste, J.1    Kuismanen, E.2
  • 25
    • 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
  • 26
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment: in search of its identity and function
    • Appenzeller-Herzog C., and Hauri H.-P. The ER-Golgi intermediate compartment: in search of its identity and function. J. Cell Sci. 119 (2006) 2173-2183
    • (2006) J. Cell Sci. , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.-P.2
  • 27
    • 0021148465 scopus 로고
    • Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface
    • Saraste J., and Kuismanen E. Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface. Cell 38 (1984) 535-549
    • (1984) Cell , vol.38 , pp. 535-549
    • Saraste, J.1    Kuismanen, E.2
  • 28
    • 0023916548 scopus 로고
    • Site of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59
    • Tooze S.A., Tooze J., and Warren G. Site of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59. J. Cell Biol. 106 (1988) 1475-1487
    • (1988) J. Cell Biol. , vol.106 , pp. 1475-1487
    • Tooze, S.A.1    Tooze, J.2    Warren, G.3
  • 29
    • 0023753261 scopus 로고
    • Biosynthesis of the mannose-6-phosphate recognition marker in transport-impaired mouse lymphoma cells. Demonstration of a two-step phosphorylation
    • Lazzarino D.A., and Gabel C.A. Biosynthesis of the mannose-6-phosphate recognition marker in transport-impaired mouse lymphoma cells. Demonstration of a two-step phosphorylation. J. Biol. Chem. 263 (1988) 10118-10126
    • (1988) J. Biol. Chem. , vol.263 , pp. 10118-10126
    • Lazzarino, D.A.1    Gabel, C.A.2
  • 30
    • 0024322074 scopus 로고
    • Palmitylation of viral membrane glycoproteins takes place after exit from the endoplasmic reticulum
    • Bonatti S., Migliaccio G., and Simons K. Palmitylation of viral membrane glycoproteins takes place after exit from the endoplasmic reticulum. J. Biol. Chem. 264 (1989) 12590-12595
    • (1989) J. Biol. Chem. , vol.264 , pp. 12590-12595
    • Bonatti, S.1    Migliaccio, G.2    Simons, K.3
  • 31
    • 0023647142 scopus 로고
    • Protein transport. Signals and salvage sequences
    • Warren G. Protein transport. Signals and salvage sequences. Nature 327 (1987) 17-18
    • (1987) Nature , vol.327 , pp. 17-18
    • Warren, G.1
  • 32
    • 0024427039 scopus 로고
    • Control of protein exit from the endoplasmic reticulum
    • Pelham H.R.B. Control of protein exit from the endoplasmic reticulum. Ann. Rev. Cell Biol. 5 (1989) 1-23
    • (1989) Ann. Rev. Cell Biol. , vol.5 , pp. 1-23
    • Pelham, H.R.B.1
  • 33
    • 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
  • 34
    • 0034285087 scopus 로고    scopus 로고
    • Breaking the COP monopoly on Golgi recycling
    • Storrie B., Pepperkok R., and Nilsson T. Breaking the COP monopoly on Golgi recycling. Trends Cell Biol. 10 (2000) 385-391
    • (2000) Trends Cell Biol. , vol.10 , pp. 385-391
    • Storrie, B.1    Pepperkok, R.2    Nilsson, T.3
  • 35
    • 0023581760 scopus 로고
    • Antibodies to rat pancreas Golgi subfractions: Identification of a 58 kDa cis-Golgi protein
    • Saraste J., Palade G.E., and Farquhar M.G. Antibodies to rat pancreas Golgi subfractions: Identification of a 58 kDa cis-Golgi protein. J. Cell Biol. 105 (1987) 2021-2029
    • (1987) J. Cell Biol. , vol.105 , pp. 2021-2029
    • Saraste, J.1    Palade, G.E.2    Farquhar, M.G.3
  • 36
    • 0023733211 scopus 로고
    • Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus
    • Schweizer A., Fransen J.A., Bächi T., Ginsel L., and Hauri H.P. Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J. Cell Biol. 107 (1988) 1643-1653
    • (1988) J. Cell Biol. , vol.107 , pp. 1643-1653
    • Schweizer, A.1    Fransen, J.A.2    Bächi, T.3    Ginsel, L.4    Hauri, H.P.5
  • 37
    • 0026052099 scopus 로고
    • Distribution of the intermediate elements operating in ER to Golgi transport
    • Saraste J., and Svensson K. Distribution of the intermediate elements operating in ER to Golgi transport. J. Cell Sci. 100 (1991) 415-430
    • (1991) J. Cell Sci. , vol.100 , pp. 415-430
    • Saraste, J.1    Svensson, K.2
  • 38
    • 0026488112 scopus 로고
    • Characterization of a 58 kDa cis-Golgi protein in pancreatic exocrine cells
    • Lahtinen U., Dahllöf B., and Saraste J. Characterization of a 58 kDa cis-Golgi protein in pancreatic exocrine cells. J. Cell Sci. 103 (1992) 321-333
    • (1992) J. Cell Sci. , vol.103 , pp. 321-333
    • Lahtinen, U.1    Dahllöf, B.2    Saraste, J.3
  • 40
    • 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
  • 41
    • 15544363926 scopus 로고    scopus 로고
    • The role of microtubules in transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells
    • Palmer K.J., Watson P., and Stephens D.J. The role of microtubules in transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells. Biochem. Soc. Symp. 72 (2005) 1-13
    • (2005) Biochem. Soc. Symp. , vol.72 , pp. 1-13
    • Palmer, K.J.1    Watson, P.2    Stephens, D.J.3
  • 43
    • 3142624697 scopus 로고    scopus 로고
    • Differential ER exit in yeast and mammalian cells
    • Watanabe R., and Riezman H. Differential ER exit in yeast and mammalian cells. Curr. Opin. Cell Biol. 16 (2004) 350-355
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 350-355
    • Watanabe, R.1    Riezman, H.2
  • 45
    • 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
  • 47
    • 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
  • 48
    • 0033730407 scopus 로고    scopus 로고
    • The p58-positive pre-Golgi intermediates consist of distinct subpopulations of particles that show differential binding of COPI and COPII coats and contain vacuolar proton-ATPase
    • Ying M., Flatmark T., and Saraste J. The p58-positive pre-Golgi intermediates consist of distinct subpopulations of particles that show differential binding of COPI and COPII coats and contain vacuolar proton-ATPase. J. Cell Sci. 113 (2000) 3623-3638
    • (2000) J. Cell Sci. , vol.113 , pp. 3623-3638
    • Ying, M.1    Flatmark, T.2    Saraste, J.3
  • 49
    • 0037113095 scopus 로고    scopus 로고
    • Ultrastructural characterization of endoplasmic reticulum-Golgi transport containers (EGTCs)
    • Horstmann H., Ng C.P., Tang B.L., and Hong W. Ultrastructural characterization of endoplasmic reticulum-Golgi transport containers (EGTCs). J. Cell Sci. 115 (2002) 4263-4273
    • (2002) J. Cell Sci. , vol.115 , pp. 4263-4273
    • Horstmann, H.1    Ng, C.P.2    Tang, B.L.3    Hong, W.4
  • 50
    • 0348103715 scopus 로고    scopus 로고
    • Ultrastructural analysis of transitional endoplasmic reticulum and pre-Golgi intermediates: a highway for cars and trucks
    • Fan J.Y., Roth J., and Zuber C. Ultrastructural analysis of transitional endoplasmic reticulum and pre-Golgi intermediates: a highway for cars and trucks. Histochem. Cell Biol. 120 (2003) 455-463
    • (2003) Histochem. Cell Biol. , vol.120 , pp. 455-463
    • Fan, J.Y.1    Roth, J.2    Zuber, C.3
  • 52
    • 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., and Balch W.E. Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion. Science 289 (2000) 444-448
    • (2000) Science , vol.289 , pp. 444-448
    • Allan, B.B.1    Moyer, B.D.2    Balch, W.E.3
  • 53
    • 34948874261 scopus 로고    scopus 로고
    • Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells
    • Haas A.K., Yoshimura S., Stephens D.J., Preisinger C., Fuchs E., and Barr F.A. Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells. J. Cell Sci. 120 (2007) 2997-3010
    • (2007) J. Cell Sci. , vol.120 , pp. 2997-3010
    • Haas, A.K.1    Yoshimura, S.2    Stephens, D.J.3    Preisinger, C.4    Fuchs, E.5    Barr, F.A.6
  • 54
    • 34347386746 scopus 로고    scopus 로고
    • Rab1B interacts with GBF1 and modulates both ARF1 dynamics and COPI association
    • Monetta P., Slavin I., Romero N., and Alvarez C. Rab1B interacts with GBF1 and modulates both ARF1 dynamics and COPI association. Mol. Biol. Cell 18 (2007) 2400-2410
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2400-2410
    • Monetta, P.1    Slavin, I.2    Romero, N.3    Alvarez, C.4
  • 57
    • 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
  • 58
    • 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 (2000) 3151-3159
    • (2000) J. Cell Sci. , vol.113 , pp. 3151-3159
    • Blum, R.1    Stephens, D.J.2    Schulz, I.3
  • 59
    • 22044445588 scopus 로고    scopus 로고
    • SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane
    • Jüschke C., Wächter A., Schwappach B., and Seedorf M. SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane. J. Cell Biol. 169 (2005) 613-622
    • (2005) J. Cell Biol. , vol.169 , pp. 613-622
    • Jüschke, C.1    Wächter, A.2    Schwappach, B.3    Seedorf, M.4
  • 60
    • 70350380859 scopus 로고    scopus 로고
    • Regulation of primary cilia formation by ceramide
    • Wang G., Krishnamurthy K., and Bieberich E. Regulation of primary cilia formation by ceramide. J. Lipid Res. 50 (2009) 2103-2110
    • (2009) J. Lipid Res. , vol.50 , pp. 2103-2110
    • Wang, G.1    Krishnamurthy, K.2    Bieberich, E.3
  • 61
    • 64149084265 scopus 로고    scopus 로고
    • GM130-dependent control of Cdc42 activity at the Golgi regulates centrosome organization
    • Kodani A., Kristensen I., Huang L., and Sütterlin C. GM130-dependent control of Cdc42 activity at the Golgi regulates centrosome organization. Mol. Biol. Cell 20 (2009) 1192-1200
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1192-1200
    • Kodani, A.1    Kristensen, I.2    Huang, L.3    Sütterlin, C.4
  • 62
    • 1842613600 scopus 로고    scopus 로고
    • YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3 zeta
    • Preisinger C., Short B., De Corte V., Bruyneel E., Haas A., Kopajtich R., Gettemans J., and Barr F.A. YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3 zeta. J. Cell Biol. 164 (2004) 1009-1020
    • (2004) J. Cell Biol. , vol.164 , pp. 1009-1020
    • Preisinger, C.1    Short, B.2    De Corte, V.3    Bruyneel, E.4    Haas, A.5    Kopajtich, R.6    Gettemans, J.7    Barr, F.A.8
  • 63
    • 0034718846 scopus 로고    scopus 로고
    • Matrix proteins can generate the higher order architecture of the Golgi apparatus
    • Seemann J., Jokitalo E., Pypaert M., and Warren G. Matrix proteins can generate the higher order architecture of the Golgi apparatus. Nature 407 (2000) 1022-1026
    • (2000) Nature , vol.407 , pp. 1022-1026
    • Seemann, J.1    Jokitalo, E.2    Pypaert, M.3    Warren, G.4
  • 64
    • 0026702055 scopus 로고
    • In AtT 20 and HeLa cells brefeldin A induces the fusion of tubular endosomes and changes their distribution and some of their endocytic properties
    • Tooze J., and Hollinshead M. In AtT 20 and HeLa cells brefeldin A induces the fusion of tubular endosomes and changes their distribution and some of their endocytic properties. J. Cell Biol. 118 (1992) 813-830
    • (1992) J. Cell Biol. , vol.118 , pp. 813-830
    • Tooze, J.1    Hollinshead, M.2
  • 65
    • 0037016677 scopus 로고    scopus 로고
    • Vesicular and non-vesicular sterol transport in living cells. The endocytic recycling compartment is a major sterol storage organelle
    • Hao M., Lin S.X., Karylowski O.J., Wüstner D., McGraw T.E., and Maxfield F.R. Vesicular and non-vesicular sterol transport in living cells. The endocytic recycling compartment is a major sterol storage organelle. J. Biol. Chem. 277 (2002) 609-617
    • (2002) J. Biol. Chem. , vol.277 , pp. 609-617
    • Hao, M.1    Lin, S.X.2    Karylowski, O.J.3    Wüstner, D.4    McGraw, T.E.5    Maxfield, F.R.6
  • 68
    • 0037010141 scopus 로고    scopus 로고
    • Transport of protein toxins into cells: pathways used by ricin, cholera toxin and shiga toxin
    • Sandvig K., and van Deurs B. Transport of protein toxins into cells: pathways used by ricin, cholera toxin and shiga toxin. FEBS Lett. 529 (2002) 49-53
    • (2002) FEBS Lett. , vol.529 , pp. 49-53
    • Sandvig, K.1    van Deurs, B.2
  • 70
    • 33746641737 scopus 로고    scopus 로고
    • MBet3p is required for homotypic COPII vesicle tethering in mammalian cells
    • Yu S., Satoh A., Pypaert M., Mullen K., Hay J.C., and Ferro-Novick S. MBet3p is required for homotypic COPII vesicle tethering in mammalian cells. J. Cell Biol. 174 (2006) 359-368
    • (2006) J. Cell Biol. , vol.174 , pp. 359-368
    • Yu, S.1    Satoh, A.2    Pypaert, M.3    Mullen, K.4    Hay, J.C.5    Ferro-Novick, S.6
  • 72
    • 0032168280 scopus 로고    scopus 로고
    • Specific binding to a novel and essential Golgi membrane protein (Yip1p) functionally links the transport GTPases Ypt1p and Ypt31p
    • Yang H., Matern H.T., and Gallwitz D. Specific binding to a novel and essential Golgi membrane protein (Yip1p) functionally links the transport GTPases Ypt1p and Ypt31p. EMBO J. 17 (1998) 4954-4963
    • (1998) EMBO J. , vol.17 , pp. 4954-4963
    • Yang, H.1    Matern, H.T.2    Gallwitz, D.3
  • 73
    • 0034724182 scopus 로고    scopus 로고
    • Lipid raft function in biosynthetic delivery of proteins to the cell surface in yeast
    • Bagnat M., Keränen S., Shevchenko A., Shevchenko A., and Simons K. Lipid raft function in biosynthetic delivery of proteins to the cell surface in yeast. J. Biol. Chem. 97 (2000) 3254-3259
    • (2000) J. Biol. Chem. , vol.97 , pp. 3254-3259
    • Bagnat, M.1    Keränen, S.2    Shevchenko, A.3    Shevchenko, A.4    Simons, K.5
  • 74
  • 76
    • 67749127352 scopus 로고    scopus 로고
    • Plasma membrane area increases with spread area by exocytosis of a GPI-anchored protein compartment
    • Gauthier N.C., Rossier O.M., Mathurm A., Hone J.C., and Sheetz M.P. Plasma membrane area increases with spread area by exocytosis of a GPI-anchored protein compartment. Mol. Biol. Cell 20 (2009) 3261-3272
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3261-3272
    • Gauthier, N.C.1    Rossier, O.M.2    Mathurm, A.3    Hone, J.C.4    Sheetz, M.P.5
  • 77
    • 38849131487 scopus 로고    scopus 로고
    • How many ways through the Golgi maze?
    • Prydz K., Dick G., and Tveit H. How many ways through the Golgi maze?. Traffic 9 (2008) 299-304
    • (2008) Traffic , vol.9 , pp. 299-304
    • Prydz, K.1    Dick, G.2    Tveit, H.3
  • 78
    • 34247282758 scopus 로고    scopus 로고
    • Functional symmetry of endomembranes
    • Saraste J., and Goud B. Functional symmetry of endomembranes. Mol. Biol. Cell 18 (2007) 1430-1436
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1430-1436
    • Saraste, J.1    Goud, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.