메뉴 건너뛰기




Volumn 43, Issue 4, 1999, Pages 334-348

Morphological changes in the Golgi complex correlate with actin cytoskeleton rearrangements

Author keywords

Actin; Brefeldin A (BFA); Cytochalasin D; Golgi complex; Jasplakinolide; PI3K

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; ACTIN; BREFELDIN A; CYTOCHALASIN D; EPIDERMAL GROWTH FACTOR; GLYCOSAMINOGLYCAN; LYSOPHOSPHATIDIC ACID; MANNOSIDASE; PHORBOL 13 ACETATE 12 MYRISTATE; PHOSPHATIDYLINOSITOL 3 KINASE; WORTMANNIN;

EID: 0032773274     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0169(1999)43:4<334::AID-CM6>3.0.CO;2-3     Document Type: Article
Times cited : (52)

References (69)
  • 1
    • 0032538973 scopus 로고    scopus 로고
    • PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in formation of filopodia
    • Abo A, Qu J, Cammarano MS, Dan Ch, Fritsch A, Baud V, Belisle B, Minden A. 1998. PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in formation of filopodia. EMBO J 17:6527-6540.
    • (1998) EMBO J , vol.17 , pp. 6527-6540
    • Abo, A.1    Qu, J.2    Cammarano, M.S.3    Dan, Ch.4    Fritsch, A.5    Baud, V.6    Belisle, B.7    Minden, A.8
  • 2
    • 0026090189 scopus 로고
    • Regulation of the antigen-induced F-actin response in rat basophilic leukemia cells by protein kinase C
    • Apgar JR. 1991. Regulation of the antigen-induced F-actin response in rat basophilic leukemia cells by protein kinase C. J Cell Biol 112:1157-1163.
    • (1991) J Cell Biol , vol.112 , pp. 1157-1163
    • Apgar, J.R.1
  • 3
    • 0028316375 scopus 로고
    • Polymerization of actin in RBL-2H3 cells can be triggered through either the IgE receptor or the adenosine receptor but different signalling pathways are used
    • Apgar JR. 1994. Polymerization of actin in RBL-2H3 cells can be triggered through either the IgE receptor or the adenosine receptor but different signalling pathways are used. Mol Biol Cell 5:313-322.
    • (1994) Mol Biol Cell , vol.5 , pp. 313-322
    • Apgar, J.R.1
  • 4
    • 0029013069 scopus 로고
    • Activation of protein kinase C in rat basophilic leukemia cells stimulates increased production of phosphatidyl-inositol 4-phosphate and phosphatidylinositol 4,5-biphosphate, correlation with actin polymerization
    • Apgar JR. 1995. Activation of protein kinase C in rat basophilic leukemia cells stimulates increased production of phosphatidyl-inositol 4-phosphate and phosphatidylinositol 4,5-biphosphate, correlation with actin polymerization. Mol Biol Cell 6:97-108.
    • (1995) Mol Biol Cell , vol.6 , pp. 97-108
    • Apgar, J.R.1
  • 6
    • 0032516894 scopus 로고    scopus 로고
    • A spectrin membrane skeleton of the Golgi complex
    • Beck KA, Nelson WJ. 1998. A spectrin membrane skeleton of the Golgi complex. Biochem Biophys Acta 1404:153-160.
    • (1998) Biochem Biophys Acta , vol.1404 , pp. 153-160
    • Beck, K.A.1    Nelson, W.J.2
  • 7
    • 0027993053 scopus 로고
    • Golgi spectrin, identification of an erythroid beta-spectrin homolog associated with the Golgi complex
    • Beck KA, Buchanan J, Malhotra V, Nelson WJ. 1994. Golgi spectrin, identification of an erythroid beta-spectrin homolog associated with the Golgi complex. J Cell Biol 127:707-723.
    • (1994) J Cell Biol , vol.127 , pp. 707-723
    • Beck, K.A.1    Buchanan, J.2    Malhotra, V.3    Nelson, W.J.4
  • 8
    • 0030918480 scopus 로고    scopus 로고
    • Golgi membrane skeleton, identification, localization and oligomerization of a 195Kda ankyrin isoform associated with the Golgi complex
    • Beck KA, Buchanan JA, Nelson WJ. 1997. Golgi membrane skeleton, identification, localization and oligomerization of a 195Kda ankyrin isoform associated with the Golgi complex. J Cell Sci 110:1239-1249.
    • (1997) J Cell Sci , vol.110 , pp. 1239-1249
    • Beck, K.A.1    Buchanan, J.A.2    Nelson, W.J.3
  • 10
    • 0029148577 scopus 로고
    • Role of phosphatidylinositol 3′-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells
    • Brown WJ, de Wald DB, Emr SD, Putner H, Balch WE. 1995. Role of phosphatidylinositol 3′-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells. J Cell Biol 130:781-796.
    • (1995) J Cell Biol , vol.130 , pp. 781-796
    • Brown, W.J.1    De Wald, D.B.2    Emr, S.D.3    Putner, H.4    Balch, W.E.5
  • 11
    • 0028244823 scopus 로고
    • Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin
    • Bubb MR, Senderowicz AMJ, Sausville EA, Duncan KLK, Korn ED. 1994. Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J Biol Chem 269:14869-14871.
    • (1994) J Biol Chem , vol.269 , pp. 14869-14871
    • Bubb, M.R.1    Senderowicz, A.M.J.2    Sausville, E.A.3    Duncan, K.L.K.4    Korn, E.D.5
  • 13
    • 0026181461 scopus 로고
    • Stabilization and posttranslational modification of microtubules during cellular morphogenesis
    • Bulinski JC, Gundersen GG. 1991. Stabilization and posttranslational modification of microtubules during cellular morphogenesis. BioEssays 13:285-293.
    • (1991) BioEssays , vol.13 , pp. 285-293
    • Bulinski, J.C.1    Gundersen, G.G.2
  • 14
    • 0028950267 scopus 로고
    • Organization of organelles and membrane traffic by microtubules
    • Cole NB, Lippincott-Schwartz J. 1995. Organization of organelles and membrane traffic by microtubules. Curr Opin Cell Biol 7:55-64.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 55-64
    • Cole, N.B.1    Lippincott-Schwartz, J.2
  • 15
    • 0032489802 scopus 로고    scopus 로고
    • Rho guanosine triphosphatase mediates the selective stabilization of microtubules induced by lysophosphatidic acid
    • Cook TA, Nagasaki T, Gundersen GG. 1998. Rho guanosine triphosphatase mediates the selective stabilization of microtubules induced by lysophosphatidic acid. J Cell Biol 141:175-185.
    • (1998) J Cell Biol , vol.141 , pp. 175-185
    • Cook, T.A.1    Nagasaki, T.2    Gundersen, G.G.3
  • 16
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper J. 1987. Effects of cytochalasin and phalloidin on actin. J Cell Biol 105:1473-1478.
    • (1987) J Cell Biol , vol.105 , pp. 1473-1478
    • Cooper, J.1
  • 17
    • 0026760941 scopus 로고
    • Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex
    • Cotthésy-Theulaz I, Paulion A, Pfeffer SR. 1992. Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex. J Cell Biol 118:1333-1345.
    • (1992) J Cell Biol , vol.118 , pp. 1333-1345
    • Cotthésy-Theulaz, I.1    Paulion, A.2    Pfeffer, S.R.3
  • 18
    • 0029123267 scopus 로고
    • Wortmannin causes mistargeting of procathepsin D. Evidence for the involvement of phosphatidylinositol 3′-kinase in vesicular transport to lysosomes
    • Davidson D. 1995. Wortmannin causes mistargeting of procathepsin D. Evidence for the involvement of phosphatidylinositol 3′-kinase in vesicular transport to lysosomes. J Cell Biol 130:797-805.
    • (1995) J Cell Biol , vol.130 , pp. 797-805
    • Davidson, D.1
  • 19
    • 0029898290 scopus 로고    scopus 로고
    • Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds B1Σ spectrin and associates with the Golgi apparatus
    • Devarajan P, Stabach PR, Mann AS, Ardito T, Kashgarian M, Morrow JS. 1996. Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds B1Σ spectrin and associates with the Golgi apparatus. J Cell Biol 133:919-830.
    • (1996) J Cell Biol , vol.133 , pp. 919-1830
    • Devarajan, P.1    Stabach, P.R.2    Mann, A.S.3    Ardito, T.4    Kashgarian, M.5    Morrow, J.S.6
  • 20
    • 0030923518 scopus 로고    scopus 로고
    • Na,K-ATPase transport from the endoplasmic reticulum to Golgi requires the Golgi spectrin-ankyrin G119 skeleton in Madin Darby canine kidney cells
    • Devarajan P, Stabach PR, De Matteis MA, Morrow JS. 1997. Na,K-ATPase transport from the endoplasmic reticulum to Golgi requires the Golgi spectrin-ankyrin G119 skeleton in Madin Darby canine kidney cells. Proc Natl Acad Sci USA 94:10711-10716.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10711-10716
    • Devarajan, P.1    Stabach, P.R.2    De Matteis, M.A.3    Morrow, J.S.4
  • 21
    • 0026527780 scopus 로고
    • Phorbol ester-induced actin assembly in neutrophils, role of protein kinase C
    • Downey GP, Chan CK, Lea P, Takai A, Grinstein S. 1992. Phorbol ester-induced actin assembly in neutrophils, role of protein kinase C. J Cell Biol 116:695-706.
    • (1992) J Cell Biol , vol.116 , pp. 695-706
    • Downey, G.P.1    Chan, C.K.2    Lea, P.3    Takai, A.4    Grinstein, S.5
  • 22
    • 0030042764 scopus 로고    scopus 로고
    • Actin filaments facilitate two steps of endocytosis
    • Durrbach A, Louvard D, Coudrier E. 1996. Actin filaments facilitate two steps of endocytosis. J Cell Sci 109:457-465.
    • (1996) J Cell Sci , vol.109 , pp. 457-465
    • Durrbach, A.1    Louvard, D.2    Coudrier, E.3
  • 23
    • 0029998595 scopus 로고    scopus 로고
    • Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus
    • Erickson JW, Zhang Jahn RA, Evans T, Cerione RA. 1996. Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus. J Biol Chem 271:26850-26854.
    • (1996) J Biol Chem , vol.271 , pp. 26850-26854
    • Erickson, J.W.1    Zhang Jahn, R.A.2    Evans, T.3    Cerione, R.A.4
  • 24
    • 0027967774 scopus 로고
    • Export of protein from the endoplasmic reticulum is regulated by a diacylglycerol/phorbol ester binding protein
    • Fabbri M, Bannykh S, Balch WE. 1994. Export of protein from the endoplasmic reticulum is regulated by a diacylglycerol/phorbol ester binding protein. J Biol Chem 269:26848-26857.
    • (1994) J Biol Chem , vol.269 , pp. 26848-26857
    • Fabbri, M.1    Bannykh, S.2    Balch, W.E.3
  • 25
    • 0027393092 scopus 로고
    • Golgi-derived vesicles from developing epithelial cells bind actin filaments and posses myosin-I as a cytoplasmically oriented peripheral membrane protein
    • Fath KR, Burgess DR. 1993. Golgi-derived vesicles from developing epithelial cells bind actin filaments and posses myosin-I as a cytoplasmically oriented peripheral membrane protein. J Cell Biol 120:117-127.
    • (1993) J Cell Biol , vol.120 , pp. 117-127
    • Fath, K.R.1    Burgess, D.R.2
  • 26
    • 0028026746 scopus 로고
    • Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells
    • Fath KR, Trimbus GM, Burgess DR. 1994. Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells. J Cell Biol 126:661-675.
    • (1994) J Cell Biol , vol.126 , pp. 661-675
    • Fath, K.R.1    Trimbus, G.M.2    Burgess, D.R.3
  • 27
    • 0030780090 scopus 로고    scopus 로고
    • Molecular motors and a spectrin matrix associate with Golgi membranes in vitro
    • Fath KA, Trimbur GM, Burgess DR. 1997. Molecular motors and a spectrin matrix associate with Golgi membranes in vitro. J Cell Biol 139:1169-1181.
    • (1997) J Cell Biol , vol.139 , pp. 1169-1181
    • Fath, K.A.1    Trimbur, G.M.2    Burgess, D.R.3
  • 28
    • 0028019867 scopus 로고
    • Kinesin-mediated organelle translocation revealed by specific cellular manipulations
    • Feiguin F, Ferreira A, Kosic KS, Caceres A. 1994. Kinesin-mediated organelle translocation revealed by specific cellular manipulations. J Cell Biol 127:1021-1039.
    • (1994) J Cell Biol , vol.127 , pp. 1021-1039
    • Feiguin, F.1    Ferreira, A.2    Kosic, K.S.3    Caceres, A.4
  • 29
    • 0030800633 scopus 로고    scopus 로고
    • Inhibition of calcium-independent mannose 6-phosphate receptor incorporation into trans-Golgi network-derived clathrin-coated vesicles by wortmannin
    • Gaffet P, Jones AT, Clague MJ. 1997. Inhibition of calcium-independent mannose 6-phosphate receptor incorporation into trans-Golgi network-derived clathrin-coated vesicles by wortmannin. J Biol Chem 272:24170-24175.
    • (1997) J Biol Chem , vol.272 , pp. 24170-24175
    • Gaffet, P.1    Jones, A.T.2    Clague, M.J.3
  • 30
    • 0029923034 scopus 로고    scopus 로고
    • Role of type I myosins in receptor-mediated endocytosis in yeast
    • Geli MI, Riezman H. 1996. Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272:533-535.
    • (1996) Science , vol.272 , pp. 533-535
    • Geli, M.I.1    Riezman, H.2
  • 32
    • 0027166252 scopus 로고
    • Interaction between band 3 and ankyrin begins in early compartments of the secretory pathway and is essential for band 3 processing
    • Gómez S, Morgans C. 1993. Interaction between band 3 and ankyrin begins in early compartments of the secretory pathway and is essential for band 3 processing. J Biol Chem 268:19593-19597.
    • (1993) J Biol Chem , vol.268 , pp. 19593-19597
    • Gómez, S.1    Morgans, C.2
  • 33
    • 0027469161 scopus 로고
    • Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells
    • Gottlieb TA, Ivanhoe IE, Adensnik M, Sabatini DD. 1993. Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells. J Cell Biol 120:695-710.
    • (1993) J Cell Biol , vol.120 , pp. 695-710
    • Gottlieb, T.A.1    Ivanhoe, I.E.2    Adensnik, M.3    Sabatini, D.D.4
  • 34
    • 0030846186 scopus 로고    scopus 로고
    • Selective control of membrane ruffling and actin plaque assembly by the Rho GTPases Rac1 and Cdc42 in Fc epsilon RI-activated rat basophilic leukemia (RBL-2H3) cells
    • Guillemot JC, Montcourrier P, Viver E, Davoust J, Chavrier P. 1997. Selective control of membrane ruffling and actin plaque assembly by the Rho GTPases Rac1 and Cdc42 in Fc epsilon RI-activated rat basophilic leukemia (RBL-2H3) cells. J Cell Sci 110:2215-2225.
    • (1997) J Cell Sci , vol.110 , pp. 2215-2225
    • Guillemot, J.C.1    Montcourrier, P.2    Viver, E.3    Davoust, J.4    Chavrier, P.5
  • 35
    • 0031975510 scopus 로고    scopus 로고
    • Speculating about spectrin, new insights into the Golgi-associated cytoskeleton
    • Holleran EA, Holzbaur ELF. 1998. Speculating about spectrin, new insights into the Golgi-associated cytoskeleton. Trends in Cell Biol 8:26-29.
    • (1998) Trends in Cell Biol , vol.8 , pp. 26-29
    • Holleran, E.A.1    Holzbaur, E.L.F.2
  • 36
    • 0030479303 scopus 로고    scopus 로고
    • Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles
    • Holleran EA, Tokito M, Karki S, Holzbaur E. 1996. Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. J Cell Biol 135:1815-1829.
    • (1996) J Cell Biol , vol.135 , pp. 1815-1829
    • Holleran, E.A.1    Tokito, M.2    Karki, S.3    Holzbaur, E.4
  • 37
    • 0029894049 scopus 로고    scopus 로고
    • Analysis of the role of p200 containing vesicles in post-Golgi traffic
    • Ikonen E, Parton RG, Lafont F, Simons K. 1996. Analysis of the role of p200 containing vesicles in post-Golgi traffic. Mol Biol Cell 7:961-974.
    • (1996) Mol Biol Cell , vol.7 , pp. 961-974
    • Ikonen, E.1    Parton, R.G.2    Lafont, F.3    Simons, K.4
  • 38
    • 0030820352 scopus 로고    scopus 로고
    • Myosin II is associated with Golgi membranes, identification of p200 as a nonmuscle myosin II on Golgi-derived vesicles
    • Ikonen E, de Almeida JB, Fath KR, Burgess DR, Ashman K, Simons K, Stow JL. 1997. Myosin II is associated with Golgi membranes, identification of p200 as a nonmuscle myosin II on Golgi-derived vesicles. J Cell Sci 110:2155-2164.
    • (1997) J Cell Sci , vol.110 , pp. 2155-2164
    • Ikonen, E.1    De Almeida, J.B.2    Fath, K.R.3    Burgess, D.R.4    Ashman, K.5    Simons, K.6    Stow, J.L.7
  • 39
    • 0028085551 scopus 로고
    • Inhibition of apical but not basolateral endocytosis of ricin and folate in CaCo-2 cells by cytochalasin D
    • Jackman MR, Shurety W, Ellis JA, Luzio JP. 1994. Inhibition of apical but not basolateral endocytosis of ricin and folate in CaCo-2 cells by cytochalasin D. J Cell Sci 107:2547-2556.
    • (1994) J Cell Sci , vol.107 , pp. 2547-2556
    • Jackman, M.R.1    Shurety, W.2    Ellis, J.A.3    Luzio, J.P.4
  • 40
    • 0030720512 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is required for the formation of constitutive transport vesicles from the TON
    • Jones SM, Howell KE. 1997. Phosphatidylinositol 3-kinase is required for the formation of constitutive transport vesicles from the TON. J Cell Biol 139:339-349.
    • (1997) J Cell Biol , vol.139 , pp. 339-349
    • Jones, S.M.1    Howell, K.E.2
  • 41
    • 0025320750 scopus 로고
    • The protein kinase C inhibitor H-7 activates human neutrophils, effects on shape, actin polymerization, fluid pinocytosis and locomotion
    • Keller HU, Niggli V, Zimmermann A, Portmann R. 1990. The protein kinase C inhibitor H-7 activates human neutrophils, effects on shape, actin polymerization, fluid pinocytosis and locomotion. J Cell Sci 96:99-106.
    • (1990) J Cell Sci , vol.96 , pp. 99-106
    • Keller, H.U.1    Niggli, V.2    Zimmermann, A.3    Portmann, R.4
  • 43
    • 0002059187 scopus 로고    scopus 로고
    • Golgi apparatus-cytoskeleton interactions
    • Berger EG, Roth J, editors. Basel: Birkhäuser Verlag
    • Kreis T, Goodson HV, Pérz F, Ranholm R. 1997. Golgi apparatus-cytoskeleton interactions. In: Berger EG, Roth J, editors. The Golgi apparatus. Basel: Birkhäuser Verlag, p 179-193.
    • (1997) The Golgi Apparatus , pp. 179-193
    • Kreis, T.1    Goodson, H.V.2    Pérz, F.3    Ranholm, R.4
  • 44
    • 0027260748 scopus 로고
    • Actin and fimbrin are required for the internalization step of endocytosis in yeast
    • Kubler E, Riezman H. 1993. Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J 12:2855-2862.
    • (1993) EMBO J , vol.12 , pp. 2855-2862
    • Kubler, E.1    Riezman, H.2
  • 47
    • 0028104096 scopus 로고
    • Association of kinesin with the Golgi apparatus in rat hepatocytes
    • Marks DL, Larkur JM, McNiven MA. 1994. Association of kinesin with the Golgi apparatus in rat hepatocytes. J Cell Sci 107:2417-2426.
    • (1994) J Cell Sci , vol.107 , pp. 2417-2426
    • Marks, D.L.1    Larkur, J.M.2    McNiven, M.A.3
  • 48
    • 0032575652 scopus 로고    scopus 로고
    • Characterization of the association of the actin-binding protein, IQGAP, and activated Cdc42 with Golgi membranes
    • McCallum SJ, Erickson JW, Cerione RA. 1998. Characterization of the association of the actin-binding protein, IQGAP, and activated Cdc42 with Golgi membranes. J Biol Chem 273:22537-22544.
    • (1998) J Biol Chem , vol.273 , pp. 22537-22544
    • McCallum, S.J.1    Erickson, J.W.2    Cerione, R.A.3
  • 49
    • 0028228643 scopus 로고
    • A possible role for stable microtubules in intracellular transport from the endoplasmic reticulum to the Golgi apparatus
    • Mizuno M, Singer SJ. 1994. A possible role for stable microtubules in intracellular transport from the endoplasmic reticulum to the Golgi apparatus. J Cell Sci 107:1321-1331.
    • (1994) J Cell Sci , vol.107 , pp. 1321-1331
    • Mizuno, M.1    Singer, S.J.2
  • 50
    • 0030823761 scopus 로고    scopus 로고
    • Myosin I interactions with actin filaments and trans-Golgi-derived vesicles in MDCK cell monolayers
    • Montes de Oca G, Lezama RA, Mondragón R, Castillo AM, Meza I. 1997. Myosin I interactions with actin filaments and trans-Golgi-derived vesicles in MDCK cell monolayers. Arch Med Res 28:321-328.
    • (1997) Arch Med Res , vol.28 , pp. 321-328
    • Montes De Oca, G.1    Lezama, R.A.2    Mondragón, R.3    Castillo, A.M.4    Meza, I.5
  • 51
    • 0028889137 scopus 로고
    • Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells
    • Muallem S, Kwiatkowska K, Xu X, Yin HL. 1995. Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells. J Cell Biol 128:589-598.
    • (1995) J Cell Biol , vol.128 , pp. 589-598
    • Muallem, S.1    Kwiatkowska, K.2    Xu, X.3    Yin, H.L.4
  • 52
    • 0040971539 scopus 로고    scopus 로고
    • Myosin II is involved in the production of constitutive transport vesicles from the TGN
    • Müsch A, Cohen D, Rodríguez-Boulan E. 1997. Myosin II is involved in the production of constitutive transport vesicles from the TGN. J Cell Biol 138:291-306.
    • (1997) J Cell Biol , vol.138 , pp. 291-306
    • Müsch, A.1    Cohen, D.2    Rodríguez-Boulan, E.3
  • 53
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes CD, Hall A. 1995. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 54
    • 0028837170 scopus 로고
    • Activation of the small GTP-binding proteins rho and rac by growth factor receptors
    • Nobes C, Hawkins P, Stephens L, Hall A. 1995. Activation of the small GTP-binding proteins rho and rac by growth factor receptors. J Cell Sci 108:225-233.
    • (1995) J Cell Sci , vol.108 , pp. 225-233
    • Nobes, C.1    Hawkins, P.2    Stephens, L.3    Hall, A.4
  • 55
    • 85069134763 scopus 로고    scopus 로고
    • Spatial segregation of tropomyosin and actin isoforms in synchronized NIH3T3 cells
    • Percival J, Weinberger R, Jeffrey P, Gunning P. 1997. Spatial segregation of tropomyosin and actin isoforms in synchronized NIH3T3 cells. Mol Biol Cell 8:271a.
    • (1997) Mol Biol Cell , vol.8
    • Percival, J.1    Weinberger, R.2    Jeffrey, P.3    Gunning, P.4
  • 57
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley AJ, Hall A. 1992. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 58
    • 0026778133 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley AJ, Paterson HJ, Johnston CL, Diekmann D, Hall A. 1992. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Paterson, H.J.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 59
    • 0021135281 scopus 로고
    • Associations of elements of the Golgi apparatus with microtubules
    • Rogalski A, Singer SJ. 1984. Associations of elements of the Golgi apparatus with microtubules. J Cell Biol 99:1092-1100.
    • (1984) J Cell Biol , vol.99 , pp. 1092-1100
    • Rogalski, A.1    Singer, S.J.2
  • 60
    • 0029097640 scopus 로고
    • Involvement of the GTP binding protein Rho in constitutive endocytosis in Xenopus laevis oocytes
    • Schmalzing G, Richter HP, Hansen A, Schwarz W, Just I, Aktories K. 1995. Involvement of the GTP binding protein Rho in constitutive endocytosis in Xenopus laevis oocytes. J Cell Biol 130:1319-1332.
    • (1995) J Cell Biol , vol.130 , pp. 1319-1332
    • Schmalzing, G.1    Richter, H.P.2    Hansen, A.3    Schwarz, W.4    Just, I.5    Aktories, K.6
  • 61
    • 0021315324 scopus 로고
    • The inhibition of dictyosome vesicle formation in higher cells by cytochalasin D
    • Shannon TM, Picton JM, Steer MW. 1984. The inhibition of dictyosome vesicle formation in higher cells by cytochalasin D. Eur J Cell Biol 33:144-147.
    • (1984) Eur J Cell Biol , vol.33 , pp. 144-147
    • Shannon, T.M.1    Picton, J.M.2    Steer, M.W.3
  • 62
    • 0031921773 scopus 로고    scopus 로고
    • Fluid-phase markers in the basolateral endocytic pathway accumulate in response to the actin assembly-promoting drug jasplakinolide
    • Shurety W, Stewart NL, Stow JL. 1998. Fluid-phase markers in the basolateral endocytic pathway accumulate in response to the actin assembly-promoting drug jasplakinolide. Mol Biol Cell 9:957-975.
    • (1998) Mol Biol Cell , vol.9 , pp. 957-975
    • Shurety, W.1    Stewart, N.L.2    Stow, J.L.3
  • 64
    • 0031663239 scopus 로고    scopus 로고
    • Adenovirus endocytosis requires actin cytoskeleton reorganization mediated by Rho family GTPases
    • Stupack LE, Bokoch GM, Nemerow GR. 1998. Adenovirus endocytosis requires actin cytoskeleton reorganization mediated by Rho family GTPases. J Virol 72:8806-8812.
    • (1998) J Virol , vol.72 , pp. 8806-8812
    • Stupack, L.E.1    Bokoch, G.M.2    Nemerow, G.R.3
  • 65
    • 0022412716 scopus 로고
    • Microtubules and the organization of the Golgi complex
    • Thyberg J, Moskalewski S. 1985. Microtubules and the organization of the Golgi complex. Exp Cell Res 159:1-16.
    • (1985) Exp Cell Res , vol.159 , pp. 1-16
    • Thyberg, J.1    Moskalewski, S.2
  • 66
    • 0031779777 scopus 로고    scopus 로고
    • Actin microfilaments are essential for the cytological positioning and morphology of the Golgi complex
    • Valderrama F, Babià T, Ayala I, Kok JW, Renau-Piqueras J, Egea G. 1998. Actin microfilaments are essential for the cytological positioning and morphology of the Golgi complex. Eur J Cell Biol 76:9-17.
    • (1998) Eur J Cell Biol , vol.76 , pp. 9-17
    • Valderrama, F.1    Babià, T.2    Ayala, I.3    Kok, J.W.4    Renau-Piqueras, J.5    Egea, G.6
  • 67
    • 0028940724 scopus 로고
    • Delivery to lysosomes in human carcinoma cell line HepG-2 involves an actin filament-facilitated fusion between mature endosomes and pre-existing lysosomes
    • van Deurs B, Holm PK, Kayser L, Sandvig K. 1995. Delivery to lysosomes in human carcinoma cell line HepG-2 involves an actin filament-facilitated fusion between mature endosomes and pre-existing lysosomes. Eur J Cell Biol 66:309-323.
    • (1995) Eur J Cell Biol , vol.66 , pp. 309-323
    • Van Deurs, B.1    Holm, P.K.2    Kayser, L.3    Sandvig, K.4
  • 68
    • 0027361181 scopus 로고
    • The actin-binding protein comitin (p24) is a component of the Golgi apparatus
    • Weiner O, Murphy J, Griffiths G, Schleicher M, Noegel AA. 1993. The actin-binding protein comitin (p24) is a component of the Golgi apparatus. J Cell Biol 123:23-34.
    • (1993) J Cell Biol , vol.123 , pp. 23-34
    • Weiner, O.1    Murphy, J.2    Griffiths, G.3    Schleicher, M.4    Noegel, A.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.