메뉴 건너뛰기




Volumn 328, Issue 2, 2014, Pages 325-339

Low cytoplasmic pH reduces ER-Golgi trafficking and induces disassembly of the Golgi apparatus

Author keywords

Acidosis; Brefeldin A; Cis Golgi; Live cell imaging; Tubular extension

Indexed keywords

2 (4 AMYLCINNAMIDO) 4 CHLOROBENZOIC ACID; BROMOENOL LACTONE; DIPEPTIDYL PEPTIDASE IV; PHOSPHOLIPASE A2; RAB PROTEIN;

EID: 84908193846     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2014.09.009     Document Type: Article
Times cited : (8)

References (75)
  • 1
    • 0036441193 scopus 로고    scopus 로고
    • Golgi architecture and inheritance
    • Shorter J., Warren G. Golgi architecture and inheritance. Annu. Rev. Cell Dev. Biol. 2002, 18:379-420. 10.1146/annurev.cellbio.18.030602.133733.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 379-420
    • Shorter, J.1    Warren, G.2
  • 2
    • 0026097957 scopus 로고
    • Localization of components involved in protein transport and processing through the yeast Golgi apparatus
    • Franzusoff A., Redding K., Crosby J., Fuller R.S., Schekman R. Localization of components involved in protein transport and processing through the yeast Golgi apparatus. J. Cell Biol. 1991, 112:27-37.
    • (1991) J. Cell Biol. , vol.112 , pp. 27-37
    • Franzusoff, A.1    Redding, K.2    Crosby, J.3    Fuller, R.S.4    Schekman, R.5
  • 4
    • 0025233925 scopus 로고
    • Three-dimensional electron microscopy: structure of the Golgi apparatus
    • Rambourg A., Clermont Y. Three-dimensional electron microscopy: structure of the Golgi apparatus. Eur. J. Cell Biol. 1990, 51:189-200.
    • (1990) Eur. J. Cell Biol. , vol.51 , pp. 189-200
    • Rambourg, A.1    Clermont, Y.2
  • 7
    • 0036796989 scopus 로고    scopus 로고
    • More than one way to replicate the Golgi apparatus
    • Munro S. More than one way to replicate the Golgi apparatus. Nat. Cell Biol. 2002, 4:E223-E224. 10.1038/ncb1002-e223.
    • (2002) Nat. Cell Biol. , vol.4 , pp. E223-E224
    • Munro, S.1
  • 8
    • 28744433842 scopus 로고    scopus 로고
    • Polarized secretory trafficking directs cargo for asymmetric dendrite growth and morphogenesis
    • Horton A.C., Rácz B., Monson E.E., Lin A.L., Weinberg R.J., Ehlers M.D. Polarized secretory trafficking directs cargo for asymmetric dendrite growth and morphogenesis. Neuron 2005, 48:757-771. 10.1016/j.neuron.2005.11.005.
    • (2005) Neuron , vol.48 , pp. 757-771
    • Horton, A.C.1    Rácz, B.2    Monson, E.E.3    Lin, A.L.4    Weinberg, R.J.5    Ehlers, M.D.6
  • 9
    • 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. Nat. Cell Biol. 2006, 8:238-248. 10.1038/ncb1366.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 238-248
    • Puthenveedu, M.A.1    Bachert, C.2    Puri, S.3    Lanni, F.4    Linstedt, A.D.5
  • 10
    • 34248176800 scopus 로고    scopus 로고
    • The biogenesis of the Golgi ribbon: the roles of membrane input from the ER and of GM130
    • Marra P., Salvatore L., Mironov A., Di Campli A., Di Tullio G., Trucco A., et al. The biogenesis of the Golgi ribbon: the roles of membrane input from the ER and of GM130. Mol. Biol. Cell 2007, 18:1595-1608. 10.1091/mbc.E06-10-0886.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1595-1608
    • Marra, P.1    Salvatore, L.2    Mironov, A.3    Di Campli, A.4    Di Tullio, G.5    Trucco, A.6
  • 11
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman R., Orci L. Coat proteins and vesicle budding. Science 1996, 271:1526-1533.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 12
    • 0035423555 scopus 로고    scopus 로고
    • ER export: public transportation by the COPII coach
    • Antonny B., Schekman R. ER export: public transportation by the COPII coach. Curr. Opin. Cell Biol. 2001, 13:438-443.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 438-443
    • Antonny, B.1    Schekman, R.2
  • 13
    • 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. 2006, 119:2173-2183. 10.1242/jcs.03019.
    • (2006) J. Cell Sci. , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.-P.2
  • 14
    • 0026503134 scopus 로고
    • The Golgi complex: in vitro veritas?
    • Mellman I., Simons K. The Golgi complex: in vitro veritas?. Cell 1992, 68:829-840.
    • (1992) Cell , vol.68 , pp. 829-840
    • Mellman, I.1    Simons, K.2
  • 15
    • 0043162027 scopus 로고
    • Long coiled-coil proteins and membrane traffic
    • Gillingham A.K., Munro S. Long coiled-coil proteins and membrane traffic. Biochim. Biophys. Acta 1641, 2003:71-85. 10.1016/S0167-4889(03)00088-0.
    • (1641) Biochim. Biophys. Acta , vol.2003 , pp. 71-85
    • Gillingham, A.K.1    Munro, S.2
  • 16
    • 20544455617 scopus 로고    scopus 로고
    • Golgins and GTPases, giving identity and structure to the Golgi apparatus
    • Short B., Haas A., Barr F.A. Golgins and GTPases, giving identity and structure to the Golgi apparatus. Biochim. Biophys. Acta-Mol. Cell Res. 2005, 1744:383-395. 10.1016/j.bbamcr.2005.02.001.
    • (2005) Biochim. Biophys. Acta-Mol. Cell Res. , vol.1744 , pp. 383-395
    • Short, B.1    Haas, A.2    Barr, F.A.3
  • 17
    • 0032146589 scopus 로고    scopus 로고
    • The organisation of the Golgi apparatus
    • Warren G., Malhotra V. The organisation of the Golgi apparatus. Curr. Opin. Cell Biol. 1998, 10:493-498.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 493-498
    • Warren, G.1    Malhotra, V.2
  • 18
    • 0034664730 scopus 로고    scopus 로고
    • The debate about transport in the Golgi-two sides of the same coin?
    • Pelham H.R., Rothman J.E. The debate about transport in the Golgi-two sides of the same coin?. Cell 2000, 102:713-719.
    • (2000) Cell , vol.102 , pp. 713-719
    • Pelham, H.R.1    Rothman, J.E.2
  • 19
    • 0034278528 scopus 로고    scopus 로고
    • Gut thoughts on the Golgi complex
    • Griffiths G. Gut thoughts on the Golgi complex. Traffic 2000, 1:738-745.
    • (2000) Traffic , vol.1 , pp. 738-745
    • Griffiths, G.1
  • 20
    • 0035945341 scopus 로고    scopus 로고
    • Traffic through the Golgi apparatus
    • Pelham H.R.B. Traffic through the Golgi apparatus. J. Cell Biol. 2001, 155:1099-1101. 10.1083/jcb.200110160.
    • (2001) J. Cell Biol. , vol.155 , pp. 1099-1101
    • Pelham, H.R.B.1
  • 21
  • 22
    • 0023008846 scopus 로고
    • Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes
    • Misumi Y., Misumi Y., Maki K., Takatsuki A., Tamura G., Ikehara Y. Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes. J. Biol. Chem. 1986, 261:11398-11403.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11398-11403
    • Misumi, Y.1    Misumi, Y.2    Maki, K.3    Takatsuki, A.4    Tamura, G.5    Ikehara, Y.6
  • 23
    • 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 1989, 56:801-813.
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 25
    • 0343487717 scopus 로고    scopus 로고
    • Characterization of brefeldin A induced vesicular structures containing cycling proteins of the intermediate compartment/cis-Golgi network
    • Füllekrug J., Sönnichsen B., Schäfer U., Van P.N., Söling H.-D., Mieskes G. Characterization of brefeldin A induced vesicular structures containing cycling proteins of the intermediate compartment/cis-Golgi network. FEBS Lett. 1997, 404:75-81.
    • (1997) FEBS Lett. , vol.404 , pp. 75-81
    • Füllekrug, J.1    Sönnichsen, B.2    Schäfer, U.3    Van, P.N.4    Söling, H.-D.5    Mieskes, G.6
  • 27
    • 11144353649 scopus 로고    scopus 로고
    • Dynamics of Golgi matrix proteins after the blockage of ER to Golgi transport
    • Yoshimura S.-I., Yamamoto A., Misumi Y., Sohda M., Barr F.A., Fujii G., et al. Dynamics of Golgi matrix proteins after the blockage of ER to Golgi transport. J. Biochem. 2004, 135:201-216. 10.1093/jb/mvh024.
    • (2004) J. Biochem. , vol.135 , pp. 201-216
    • Yoshimura, S.-I.1    Yamamoto, A.2    Misumi, Y.3    Sohda, M.4    Barr, F.A.5    Fujii, G.6
  • 28
    • 0029972823 scopus 로고    scopus 로고
    • Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites
    • Cole N.B., Sciaky N., Marotta A., Song J., Lippincott-Schwartz J. Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites. Mol. Biol. Cell 1996, 7:631-650.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 631-650
    • Cole, N.B.1    Sciaky, N.2    Marotta, A.3    Song, J.4    Lippincott-Schwartz, J.5
  • 29
    • 0032517823 scopus 로고    scopus 로고
    • Recycling of Golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering
    • Storrie B., White J., Röttger S., Stelzer E.H.K., Suganuma T., Nilsson T. Recycling of Golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J. Cell Biol. 1998, 143:1505-1521.
    • (1998) J. Cell Biol. , vol.143 , pp. 1505-1521
    • Storrie, B.1    White, J.2    Röttger, S.3    Stelzer, E.H.K.4    Suganuma, T.5    Nilsson, T.6
  • 31
    • 0028827095 scopus 로고
    • Mitotic disassembly of the mammalian Golgi-apparatus
    • Warren G., Levine T., Misteli T. Mitotic disassembly of the mammalian Golgi-apparatus. Trends Cell Biol. 1995, 5:413-416.
    • (1995) Trends Cell Biol. , vol.5 , pp. 413-416
    • Warren, G.1    Levine, T.2    Misteli, T.3
  • 32
    • 0030953187 scopus 로고    scopus 로고
    • The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner
    • Nakamura N., Lowe M., Levine T.P., Rabouille C., Warren G. The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner. Cell 1997, 89:445-455.
    • (1997) Cell , vol.89 , pp. 445-455
    • Nakamura, N.1    Lowe, M.2    Levine, T.P.3    Rabouille, C.4    Warren, G.5
  • 33
    • 0032544440 scopus 로고    scopus 로고
    • Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis
    • Lowe M., Rabouille C., Nakamura N., Watson R., Jackman M., Jämsä E., et al. Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis. Cell 1998, 94:783-793.
    • (1998) Cell , vol.94 , pp. 783-793
    • Lowe, M.1    Rabouille, C.2    Nakamura, N.3    Watson, R.4    Jackman, M.5    Jämsä, E.6
  • 34
    • 0034678436 scopus 로고    scopus 로고
    • The mitotic phosphorylation cycle of the cis-Golgi matrix protein GM130
    • Lowe M., Gonatas N.K., Warren G. The mitotic phosphorylation cycle of the cis-Golgi matrix protein GM130. J. Cell Biol. 2000, 149:341-356.
    • (2000) J. Cell Biol. , vol.149 , pp. 341-356
    • Lowe, M.1    Gonatas, N.K.2    Warren, G.3
  • 35
    • 0024523485 scopus 로고
    • Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH
    • Heuser J. Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH. J. Cell Biol. 1989, 108:855-864.
    • (1989) J. Cell Biol. , vol.108 , pp. 855-864
    • Heuser, J.1
  • 36
    • 0032974029 scopus 로고    scopus 로고
    • Low cytoplasmic pH causes fragmentation and dispersal of the Golgi apparatus in human hepatoma cells
    • Yoshida T., Kamiya T., Imanaka-Yoshida K., Sakakura T. Low cytoplasmic pH causes fragmentation and dispersal of the Golgi apparatus in human hepatoma cells. Int. J. Exp. Pathol. 1999, 80:51-57.
    • (1999) Int. J. Exp. Pathol. , vol.80 , pp. 51-57
    • Yoshida, T.1    Kamiya, T.2    Imanaka-Yoshida, K.3    Sakakura, T.4
  • 37
    • 4043110513 scopus 로고    scopus 로고
    • Lactate metabolism: a new paradigm for the third millennium
    • Gladden L.B. Lactate metabolism: a new paradigm for the third millennium. J. Physiol. 2004, 558:5-30. 10.1113/jphysiol.2003.058701.
    • (2004) J. Physiol. , vol.558 , pp. 5-30
    • Gladden, L.B.1
  • 38
    • 8144228566 scopus 로고    scopus 로고
    • Why do cancers have high aerobic glycolysis?
    • Gatenby R.A., Gillies R.J. Why do cancers have high aerobic glycolysis?. Nat. Rev. Cancer 2004, 4:891-899.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 891-899
    • Gatenby, R.A.1    Gillies, R.J.2
  • 39
    • 0030943027 scopus 로고    scopus 로고
    • Partitioning of the Golgi apparatus during mitosis in living HeLa cells
    • Shima D.T., Halder K., Pepperkok R., Watson R., Warren G. Partitioning of the Golgi apparatus during mitosis in living HeLa cells. J. Cell Biol. 1997, 137:1211-1228.
    • (1997) J. Cell Biol. , vol.137 , pp. 1211-1228
    • Shima, D.T.1    Halder, K.2    Pepperkok, R.3    Watson, R.4    Warren, G.5
  • 40
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • Miesenbock G., De Angelis D.A., Rothman J.E. Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 1998, 394:192-195. 10.1038/28190.
    • (1998) Nature , vol.394 , pp. 192-195
    • Miesenbock, G.1    De Angelis, D.A.2    Rothman, J.E.3
  • 41
    • 34547590810 scopus 로고    scopus 로고
    • Functional dissection of Rab GTPases involved in primary cilium formation
    • Yoshimura S.-I., Egerer J., Fuchs E., Haas A.K., Barr F.A. Functional dissection of Rab GTPases involved in primary cilium formation. J. Cell Biol. 2007, 178:363-369. 10.1083/jcb.200703047.
    • (2007) J. Cell Biol. , vol.178 , pp. 363-369
    • Yoshimura, S.-I.1    Egerer, J.2    Fuchs, E.3    Haas, A.K.4    Barr, F.A.5
  • 42
    • 55349106863 scopus 로고    scopus 로고
    • YIPF5 and YIF1A recycle between the ER and the Golgi apparatus and are involved in the maintenance of the Golgi structure
    • Yoshida Y., Suzuki K., Yamamoto A., Sakai N., Bando M., Tanimoto K., et al. YIPF5 and YIF1A recycle between the ER and the Golgi apparatus and are involved in the maintenance of the Golgi structure. Exp. Cell Res. 2008, 314:3427-3443. 10.1016/j.yexcr.2008.07.023.
    • (2008) Exp. Cell Res. , vol.314 , pp. 3427-3443
    • Yoshida, Y.1    Suzuki, K.2    Yamamoto, A.3    Sakai, N.4    Bando, M.5    Tanimoto, K.6
  • 43
    • 0018764575 scopus 로고
    • Intracellular pH measurements in Ehrlich ascites tumor cells utilizing spectroscopic probes generated in situ
    • Thomas J.A., Buchsbaum R.N., Zimniak A., Racker E. Intracellular pH measurements in Ehrlich ascites tumor cells utilizing spectroscopic probes generated in situ. Biochemistry 1979, 18:2210-2218.
    • (1979) Biochemistry , vol.18 , pp. 2210-2218
    • Thomas, J.A.1    Buchsbaum, R.N.2    Zimniak, A.3    Racker, E.4
  • 44
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider C.A., Rasband W.S., Eliceiri K.W. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods 2012, 9:671-675. 10.1038/nmeth.2089.
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 45
    • 0026524273 scopus 로고
    • Purification and characterisation of the vimentin-specific protease in mouse myeloid leukaemia cells
    • Nakamura N., Tsuru A., Hirayoshi K., Nagata K. Purification and characterisation of the vimentin-specific protease in mouse myeloid leukaemia cells. Eur. J. Biochem. 1992, 205:947-949.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 947-949
    • Nakamura, N.1    Tsuru, A.2    Hirayoshi, K.3    Nagata, K.4
  • 46
    • 0024237306 scopus 로고
    • Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum
    • Fujiwara T., Oda K., Yokoda S., Takatsuki A., Ikehara Y. Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum. J. Biol. Chem. 1988, 263:18545-18552.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18545-18552
    • Fujiwara, T.1    Oda, K.2    Yokoda, S.3    Takatsuki, A.4    Ikehara, Y.5
  • 47
    • 0347064341 scopus 로고    scopus 로고
    • Identification and characterization of GCP16, a novel acylated Golgi protein that interacts with GCP170
    • Ohta E., Misumi Y., Sohda M., Fujiwara T., Yano A., Ikehara Y. Identification and characterization of GCP16, a novel acylated Golgi protein that interacts with GCP170. J. Biol. Chem. 2003, 278:51957-51967. 10.1074/jbc.M310014200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51957-51967
    • Ohta, E.1    Misumi, Y.2    Sohda, M.3    Fujiwara, T.4    Yano, A.5    Ikehara, Y.6
  • 49
    • 0030812940 scopus 로고    scopus 로고
    • A di-acidic signal required for selective export from the endoplamic reticulum
    • Nishimura N., Balch W.E. A di-acidic signal required for selective export from the endoplamic reticulum. Science 1997, 277:556-558.
    • (1997) Science , vol.277 , pp. 556-558
    • Nishimura, N.1    Balch, W.E.2
  • 50
    • 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 1997, 90:1137-1148.
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 51
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz J., Donaldson J.G., Schweizer A., Berger E.G., Hauri H.P., Yuan L.C., et al. Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 1990, 60:821-836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6
  • 52
    • 84856531732 scopus 로고    scopus 로고
    • A PLA1-2 punch regulates the Golgi complex
    • Bechler M.E., de Figueiredo P., Brown W.J. A PLA1-2 punch regulates the Golgi complex. Trends Cell Biol. 2011, 22:116-124. 10.1016/j.tcb.2011.10.003.
    • (2011) Trends Cell Biol. , vol.22 , pp. 116-124
    • Bechler, M.E.1    de Figueiredo, P.2    Brown, W.J.3
  • 54
    • 0032757458 scopus 로고    scopus 로고
    • Phospholipase A(2) antagonists inhibit nocodazole-induced Golgi ministack formation: evidence of an ER intermediate and constitutive cycling
    • Drecktrah D., Brown W.J. Phospholipase A(2) antagonists inhibit nocodazole-induced Golgi ministack formation: evidence of an ER intermediate and constitutive cycling. Mol. Biol. Cell 1999, 10:4021-4032.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4021-4032
    • Drecktrah, D.1    Brown, W.J.2
  • 58
    • 0025829695 scopus 로고
    • PH-induced microtubule-dependent redistribution of late endosomes in neuronal and epithelial cells
    • Parton R.G., Dotti C.G., Bacallao R., Kurtz I., Simons K., Prydz K. pH-induced microtubule-dependent redistribution of late endosomes in neuronal and epithelial cells. J. Cell Biol. 1991, 113:261-274.
    • (1991) J. Cell Biol. , vol.113 , pp. 261-274
    • Parton, R.G.1    Dotti, C.G.2    Bacallao, R.3    Kurtz, I.4    Simons, K.5    Prydz, K.6
  • 59
    • 0024537032 scopus 로고
    • Low cytoplasmic pH inhibits endocytosis and transport from the trans-Golgi network to the cell surface
    • Cosson P., de Curtis I., Pouyssegur J., Griffiths G., Davoust J. Low cytoplasmic pH inhibits endocytosis and transport from the trans-Golgi network to the cell surface. J. Cell Biol. 1989, 108:377-387.
    • (1989) J. Cell Biol. , vol.108 , pp. 377-387
    • Cosson, P.1    de Curtis, I.2    Pouyssegur, J.3    Griffiths, G.4    Davoust, J.5
  • 61
    • 0032895860 scopus 로고    scopus 로고
    • Osmotically induced cell volume changes alter anterograde and retrograde transport, Golgi structure, and COPI dissociation
    • Lee T.H., Linstedt A.D. Osmotically induced cell volume changes alter anterograde and retrograde transport, Golgi structure, and COPI dissociation. Mol. Biol. Cell 1999, 10:1445-1462.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1445-1462
    • Lee, T.H.1    Linstedt, A.D.2
  • 62
    • 0024586284 scopus 로고
    • Potassium depletion inhibits the intracellular transport of secretory proteins between the endoplasmic reticulum and the Golgi complex
    • Judah J.D., Howell K.E., Taylor J.A., Quinn P.S. Potassium depletion inhibits the intracellular transport of secretory proteins between the endoplasmic reticulum and the Golgi complex. J. Cell Sci. 1989, 92:173-185.
    • (1989) J. Cell Sci. , vol.92 , pp. 173-185
    • Judah, J.D.1    Howell, K.E.2    Taylor, J.A.3    Quinn, P.S.4
  • 63
    • 0036176367 scopus 로고    scopus 로고
    • The calcium-binding protein p54/NEFA is a novel luminal resident of medial Golgi cisternae that traffics independently of mannosidase II
    • Morel-Huaux V.M., Pypaert M., Wouters S., Tartakoff A.M., Jurgan U., Gevaert K., et al. The calcium-binding protein p54/NEFA is a novel luminal resident of medial Golgi cisternae that traffics independently of mannosidase II. Eur. J. Cell Biol. 2002, 81:87-100. 10.1078/0171-9335-00224.
    • (2002) Eur. J. Cell Biol. , vol.81 , pp. 87-100
    • Morel-Huaux, V.M.1    Pypaert, M.2    Wouters, S.3    Tartakoff, A.M.4    Jurgan, U.5    Gevaert, K.6
  • 64
    • 0033549551 scopus 로고    scopus 로고
    • A role for the vesicle tethering protein, p115, in the post-mitotic stacking of reassembling Golgi cisternae in a cell-free system
    • Shorter J., Warren G. A role for the vesicle tethering protein, p115, in the post-mitotic stacking of reassembling Golgi cisternae in a cell-free system. J. Cell Biol. 1999, 146:57-70.
    • (1999) J. Cell Biol. , vol.146 , pp. 57-70
    • Shorter, J.1    Warren, G.2
  • 65
    • 0013086420 scopus 로고    scopus 로고
    • Structural integrity of the Golgi is temperature sensitive in conditional-lethal mutants with no detectable GM130
    • Vasile E., Perez T., Nakamura N., Krieger M. Structural integrity of the Golgi is temperature sensitive in conditional-lethal mutants with no detectable GM130. Traffic 2003, 4:254-272.
    • (2003) Traffic , vol.4 , pp. 254-272
    • Vasile, E.1    Perez, T.2    Nakamura, N.3    Krieger, M.4
  • 66
    • 0021189557 scopus 로고
    • Effect of microtubule assembly status on the intracellular processing and surface expression of an integral protein of the plasma membrane
    • Rogalski A.A., Bergmann J.E., Singer S.J. Effect of microtubule assembly status on the intracellular processing and surface expression of an integral protein of the plasma membrane. J. Cell Biol. 1984, 99:1101-1109.
    • (1984) J. Cell Biol. , vol.99 , pp. 1101-1109
    • Rogalski, A.A.1    Bergmann, J.E.2    Singer, S.J.3
  • 67
    • 0025267442 scopus 로고
    • Role of microtubules in the organisation of the Golgi apparatus
    • Kreis T.E. Role of microtubules in the organisation of the Golgi apparatus. Cell Motil. Cytoskelet. 1990, 15:67-70. 10.1002/cm.970150202.
    • (1990) Cell Motil. Cytoskelet. , vol.15 , pp. 67-70
    • Kreis, T.E.1
  • 68
    • 0032489870 scopus 로고    scopus 로고
    • Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein
    • Harada A., Takei Y., Kanai Y., Tanaka Y., Nonaka S., Hirokawa N. Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein. J. Cell Biol. 1998, 141:51-59.
    • (1998) J. Cell Biol. , vol.141 , pp. 51-59
    • Harada, A.1    Takei, Y.2    Kanai, Y.3    Tanaka, Y.4    Nonaka, S.5    Hirokawa, N.6
  • 69
    • 70349835304 scopus 로고    scopus 로고
    • GOLPH3 bridges phosphatidylinositol-4-phosphate and actomyosin to stretch and shape the Golgi to promote budding
    • Dippold H.C., Ng M.M., Farber-Katz S.E., Lee S.-K., Kerr M.L., Peterman M.C., et al. GOLPH3 bridges phosphatidylinositol-4-phosphate and actomyosin to stretch and shape the Golgi to promote budding. Cell 2009, 139:337-351. 10.1016/j.cell.2009.07.052.
    • (2009) Cell , vol.139 , pp. 337-351
    • Dippold, H.C.1    Ng, M.M.2    Farber-Katz, S.E.3    Lee, S.-K.4    Kerr, M.L.5    Peterman, M.C.6
  • 70
    • 77954724096 scopus 로고    scopus 로고
    • The phospholipase complex PAFAH Ib regulates the functional organization of the Golgi complex
    • Bechler M.E., Doody A.M., Racoosin E., Lin L., Lee K.H., Brown W.J. The phospholipase complex PAFAH Ib regulates the functional organization of the Golgi complex. J. Cell. Biol. 2010, 190:45-53. 10.1083/jcb.200908105.
    • (2010) J. Cell. Biol. , vol.190 , pp. 45-53
    • Bechler, M.E.1    Doody, A.M.2    Racoosin, E.3    Lin, L.4    Lee, K.H.5    Brown, W.J.6
  • 71
    • 0026488394 scopus 로고
    • GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex
    • Tisdale E.J., Bourne J.R., Khosravi-Far R., Der C.J., Balch W.E. GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex. J. Cell Biol. 1992, 119:749-761.
    • (1992) J. Cell Biol. , vol.119 , pp. 749-761
    • Tisdale, E.J.1    Bourne, J.R.2    Khosravi-Far, R.3    Der, C.J.4    Balch, W.E.5
  • 74
    • 70349316853 scopus 로고    scopus 로고
    • Rab GTPase function in Golgi trafficking
    • Barr F.A. Rab GTPase function in Golgi trafficking. Semin. Cell Dev. Biol. 2009, 20:780-783. 10.1016/j.semcdb.2009.03.007.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 780-783
    • Barr, F.A.1
  • 75
    • 80053344208 scopus 로고    scopus 로고
    • Rab GTPases and microtubule motors
    • Horgan C.P., McCaffrey M.W. Rab GTPases and microtubule motors. Biochem. Soc. Trans. 2011, 39:1202-1206. 10.1042/BST0391202.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1202-1206
    • Horgan, C.P.1    McCaffrey, M.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.