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Volumn 138, Issue 2, 1997, Pages 291-306

Myosin II is involved in the production of constitutive transport vesicles from the TGN

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; MYOSIN;

EID: 0040971539     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.138.2.291     Document Type: Article
Times cited : (162)

References (79)
  • 1
    • 0028971172 scopus 로고
    • Sequential coupling between CopII and CopI vesicle coats in endoplasmic reticulum and Golgi transport
    • Aridor, M., S.I. Bannykh, T. Rowe, and W.E. Balch. 1995. Sequential coupling between CopII and CopI vesicle coats in endoplasmic reticulum and Golgi transport. J. Cell Biol. 131:875-893.
    • (1995) J. Cell Biol. , vol.131 , pp. 875-893
    • Aridor, M.1    Bannykh, S.I.2    Rowe, T.3    Balch, W.E.4
  • 2
    • 0021741764 scopus 로고
    • Sequential intermediates in the pathway of intercompartmental transport in a cell-free system
    • Balch, W.E., B.S. Glick, and J.E. Rothman. 1984. Sequential intermediates in the pathway of intercompartmental transport in a cell-free system. Cell. 39:525-536.
    • (1984) Cell , vol.39 , pp. 525-536
    • Balch, W.E.1    Glick, B.S.2    Rothman, J.E.3
  • 3
    • 0027993053 scopus 로고
    • Golgi spectrin: Identification of an erythroid β-spectrin homolog associated with the Golgi complex
    • Beck, K.A., J.A. Buchanan, V. Malhotra, and W.J. Nelson. 1994. Golgi spectrin: identification of an erythroid β-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.A.2    Malhotra, V.3    Nelson, W.J.4
  • 4
    • 0029905387 scopus 로고    scopus 로고
    • The spectrin-based membrane skeleton as a membrane protein-sorting machine
    • Beck, K.A., and W.J. Nelson. 1996. The spectrin-based membrane skeleton as a membrane protein-sorting machine. Am. J. Physiol. 270:C1263-1269.
    • (1996) Am. J. Physiol. , vol.270
    • Beck, K.A.1    Nelson, W.J.2
  • 6
    • 0024552276 scopus 로고
    • The spectrin-actin junction of the erythrocyte membrane skeletons
    • Bennett, V. 1989. The spectrin-actin junction of the erythrocyte membrane skeletons. Biochim. Biophys. Acta. 988:107-121.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 107-121
    • Bennett, V.1
  • 7
    • 0023739416 scopus 로고
    • A polarized epithelial cell mutant deficient in translocation of UDP-galactose into the Golgi complex
    • Brandli, A.W., G.C. Hansson, E. Rodriguez-Boulan, and K. Simons. 1988. A polarized epithelial cell mutant deficient in translocation of UDP-galactose into the Golgi complex. J. Biol. Chem. 263:16283-16290.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16283-16290
    • Brandli, A.W.1    Hansson, G.C.2    Rodriguez-Boulan, E.3    Simons, K.4
  • 8
    • 0025720725 scopus 로고
    • Microfilament structure and function in the cortical cytoskeleton
    • Bretscher, A. 1991. Microfilament structure and function in the cortical cytoskeleton. Annu. Rev. Cell Biol. 7:337-374.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 337-374
    • Bretscher, A.1
  • 9
    • 0028900381 scopus 로고
    • Polarized exocytosis in MDCK cells is regulated by phosphorylation
    • Brewer, C.B., and M.G. Roth. 1995. Polarized exocytosis in MDCK cells is regulated by phosphorylation. J. Cell Biol. 108:789-796.
    • (1995) J. Cell Biol. , vol.108 , pp. 789-796
    • Brewer, C.B.1    Roth, M.G.2
  • 10
    • 0029098971 scopus 로고    scopus 로고
    • Myosin is involved in postmitotic cell spreading
    • Cramer, L.P., and T.J. Mitchison. 1996. Myosin is involved in postmitotic cell spreading. J. Cell Biol. 131:179-189.
    • (1996) J. Cell Biol. , vol.131 , pp. 179-189
    • Cramer, L.P.1    Mitchison, T.J.2
  • 11
    • 0029134736 scopus 로고
    • Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin
    • Damke, H., T. Baba, A.M. van der Blick, and S.L. Schmid. 1995. Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin. J. Cell Biol. 131:69-80.
    • (1995) J. Cell Biol. , vol.131 , pp. 69-80
    • Damke, H.1    Baba, T.2    Van Der Blick, A.M.3    Schmid, S.L.4
  • 12
    • 0027772999 scopus 로고
    • Binding of the cytosolic p200 protein to Golgi membranes is regulated by heterotrimeric G proteins
    • de Almeida, J.B., J. Doherty, D.A. Ausiello, and J.L. Stow. 1993. Binding of the cytosolic p200 protein to Golgi membranes is regulated by heterotrimeric G proteins. J. Cell Sci. 106:1239-1248.
    • (1993) J. Cell Sci. , vol.106 , pp. 1239-1248
    • De Almeida, J.B.1    Doherty, J.2    Ausiello, D.A.3    Stow, J.L.4
  • 13
    • 0029898290 scopus 로고    scopus 로고
    • Identification of a small cytoplasmic ankyrin (Ank G119) in the kidney and muscle that binds bIS* spectrin and associates with the Golgi apparatus
    • Devarajan, P., P.R. Stabach, A.S. Mann, T. Ardito, M. Kashgarian, and J.S. Morrow. 1996. Identification of a small cytoplasmic ankyrin (Ank G119) in the kidney and muscle that binds bIS* spectrin and associates with the Golgi apparatus. J. Cell Biol. 133:819-830.
    • (1996) J. Cell Biol. , vol.133 , pp. 819-830
    • Devarajan, P.1    Stabach, P.R.2    Mann, A.S.3    Ardito, T.4    Kashgarian, M.5    Morrow, J.S.6
  • 14
    • 0026327556 scopus 로고
    • Binding of ARF and beta-COP to Golgi membranes: Possible regulation by a trimeric G protein
    • Donaldson, J.G., R.A. Kahn, J. Lippincott-Schwartz, and R.D. Klausner. 1991. Binding of ARF and beta-COP to Golgi membranes: possible regulation by a trimeric G protein. Science (Wash. DC). 254:1197-1199.
    • (1991) Science (Wash. DC) , vol.254 , pp. 1197-1199
    • Donaldson, J.G.1    Kahn, R.A.2    Lippincott-Schwartz, J.3    Klausner, R.D.4
  • 15
    • 0028151902 scopus 로고
    • Permeabilization of MDCK cells with cholesterol binding agents: Dependence on substratum and confluency
    • Esparis-Ogando, A., C. Zurzolo, and E. Rodriguez-Boulan. 1994. Permeabilization of MDCK cells with cholesterol binding agents: dependence on substratum and confluency. Am. J. Physiol. 267:166-167.
    • (1994) Am. J. Physiol. , vol.267 , pp. 166-167
    • Esparis-Ogando, A.1    Zurzolo, C.2    Rodriguez-Boulan, E.3
  • 16
    • 0027393092 scopus 로고
    • Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein
    • Fath, K.R., and D.R. Burgess. 1993. Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess 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
  • 17
    • 0028026746 scopus 로고
    • Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells
    • Fath, K.R., G.M. Trimbur, and D.R. Burgess. 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    Trimbur, G.M.2    Burgess, D.R.3
  • 18
    • 0029923034 scopus 로고    scopus 로고
    • Role of type I myosins in receptor-mediated endocytosis in yeast
    • Geli, M.I., and H. Riezman. 1996. Role of type I myosins in receptor-mediated endocytosis in yeast. Science (Wash. DC). 272:533-535.
    • (1996) Science (Wash. DC) , vol.272 , pp. 533-535
    • Geli, M.I.1    Riezman, H.2
  • 19
    • 0023091173 scopus 로고
    • Possible role for fatty acyl-coenzyme a in intracellular protein transport
    • Glick, B.S., and J.E. Rothman. 1987. Possible role for fatty acyl-coenzyme A in intracellular protein transport. Nature (Lond.). 326:308-312.
    • (1987) Nature (Lond.) , vol.326 , pp. 308-312
    • Glick, B.S.1    Rothman, J.E.2
  • 20
    • 0027469161 scopus 로고
    • Actin filaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells
    • Gottlieb, T.A., I.E. Ivanov, M. Adesnik, and D.D. Sabatini. 1993. Actin filaments 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    Ivanov, I.E.2    Adesnik, M.3    Sabatini, D.D.4
  • 21
    • 0025612221 scopus 로고
    • Transport of influenza HA from the trans-Golgi network to the apical surface of MDCK cells permeabilized in their basolateral membranes: Energy dependence and involvement of GTP-binding proteins
    • Gravotta, D., M. Adesnik, and D.D. Sabatini. 1990. Transport of influenza HA from the trans-Golgi network to the apical surface of MDCK cells permeabilized in their basolateral membranes: energy dependence and involvement of GTP-binding proteins. J. Cell Biol. 111:2893-2908.
    • (1990) J. Cell Biol. , vol.111 , pp. 2893-2908
    • Gravotta, D.1    Adesnik, M.2    Sabatini, D.D.3
  • 22
    • 0022187987 scopus 로고
    • Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane
    • Griffiths, G., S. Pfeiffer, K. Simons, and K. Matlin. 1985. Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane. J. Cell Biol. 101:949-964.
    • (1985) J. Cell Biol. , vol.101 , pp. 949-964
    • Griffiths, G.1    Pfeiffer, S.2    Simons, K.3    Matlin, K.4
  • 23
    • 0028787438 scopus 로고
    • Parallel secretory pathways to the cell surface in yeast
    • Harsay, E., and A. Bretscher. 1995. Parallel secretory pathways to the cell surface in yeast. J. Cell Biol. 131:297-310.
    • (1995) J. Cell Biol. , vol.131 , pp. 297-310
    • Harsay, E.1    Bretscher, A.2
  • 24
    • 0029163054 scopus 로고
    • Molecular motors, membrane movements and physiology: Emerging roles for myosins
    • Hasson, T., and M.S. Mooseker. 1995. Molecular motors, membrane movements and physiology: emerging roles for myosins. Curr. Opin. Cell Biol. 7:587-594.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 587-594
    • Hasson, T.1    Mooseker, M.S.2
  • 25
    • 0026746713 scopus 로고
    • Inhibition by brefeldin a of a Golgi membrane enzyme that catalyzes exchange of guanine nucleotide bound to ARF
    • Helms, J.B., and J.E. Rothman. 1992. Inhibition by brefeldin A of a Golgi membrane enzyme that catalyzes exchange of guanine nucleotide bound to ARF. Nature (Lond.). 360:352-354.
    • (1992) Nature (Lond.) , vol.360 , pp. 352-354
    • Helms, J.B.1    Rothman, J.E.2
  • 26
    • 0029942238 scopus 로고    scopus 로고
    • Association of a dynamin-like protein with the Golgi apparatus in mammalian cells
    • Henley, J.R. and M.A. McNiven. 1996. Association of a dynamin-like protein with the Golgi apparatus in mammalian cells. J. Cell Biol. 133:761-775.
    • (1996) J. Cell Biol. , vol.133 , pp. 761-775
    • Henley, J.R.1    McNiven, M.A.2
  • 27
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw, J.E., and S.L. Schmid. 1995. Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature (Lond.). 274:190-192.
    • (1995) Nature (Lond.) , vol.274 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2
  • 28
    • 0030479303 scopus 로고    scopus 로고
    • Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles
    • Holleran, E.A., M.K. Tokito, S. Karki, and E.L.F. Holzbaur. 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.K.2    Karki, S.3    Holzbaur, E.L.F.4
  • 29
    • 0027517448 scopus 로고
    • Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane
    • Huber, L.A., S. Pimplikar, R. Parton, H. Virta, M. Zerial, and K. Simons. 1993. Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane. J. Cell Biol. 123:35-46.
    • (1993) J. Cell Biol. , vol.123 , pp. 35-46
    • Huber, L.A.1    Pimplikar, S.2    Parton, R.3    Virta, H.4    Zerial, M.5    Simons, K.6
  • 30
    • 0023623227 scopus 로고
    • Movement of myosin fragments in vitro: Domains involved in force production
    • Hynes, T.R., S.M. Block, B.T. White, and J.A. Spudich. 1987. Movement of myosin fragments in vitro: domains involved in force production. Cell. 48:953-963.
    • (1987) Cell , vol.48 , pp. 953-963
    • Hynes, T.R.1    Block, S.M.2    White, B.T.3    Spudich, J.A.4
  • 31
    • 0029062772 scopus 로고
    • Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells
    • Ikonen, E., M. Tagaya, O. Ulrich, C. Montecuco, and K. Simons. 1995. Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells. Cell. 81:571-580.
    • (1995) Cell , vol.81 , pp. 571-580
    • Ikonen, E.1    Tagaya, M.2    Ulrich, O.3    Montecuco, C.4    Simons, K.5
  • 32
    • 0029894049 scopus 로고    scopus 로고
    • Analysis of the role of p200-containing vesicles in post-Golgi traffic
    • Ikonen, E., R.G. Parton, F. Lafont, and K. Simons. 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
  • 34
    • 0029925627 scopus 로고    scopus 로고
    • Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions
    • Jung, G., X. Wu, and J.A. Hammer III. 1996. Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions. J. Cell Biol. 133:305-323.
    • (1996) J. Cell Biol. , vol.133 , pp. 305-323
    • Jung, G.1    Wu, X.2    Hammer III., J.A.3
  • 35
    • 0023919181 scopus 로고
    • Force measurements by micromanipulation of a single actin filament by glass needles
    • Kishino, A., and T. Yanagida. 1988. Force measurements by micromanipulation of a single actin filament by glass needles. Nature (Lond.). 334:74-76.
    • (1988) Nature (Lond.) , vol.334 , pp. 74-76
    • Kishino, A.1    Yanagida, T.2
  • 36
    • 0027260748 scopus 로고
    • Actin and fimbrin are required for the internalization step of endocytosis in yeast
    • Kuebler, E., and H. Riezman. 1993. Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO (Eur. Mol. Biol. Organ.) J. 12:2855-2862.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 2855-2862
    • Kuebler, E.1    Riezman, H.2
  • 37
    • 0028136433 scopus 로고
    • HVEM tomography of the trans-Golgi network: Structural insights and identification of a lace-like vesicle coat
    • Ladinsky, M.S., J.R. Kremer, P.S. Furcinitti, J.R. McIntosh, and K.E. Howell. 1994. HVEM tomography of the trans-Golgi network: structural insights and identification of a lace-like vesicle coat. J. Cell Biol. 127:29-38.
    • (1994) J. Cell Biol. , vol.127 , pp. 29-38
    • Ladinsky, M.S.1    Kremer, J.R.2    Furcinitti, P.S.3    McIntosh, J.R.4    Howell, K.E.5
  • 39
    • 0024424368 scopus 로고
    • Steady state distribution and biogenesis of endogenous MDCK glycoproteins: Evidence for intracellular sorting and polarized cell surface delivery
    • Lisanti, M., A. Le Bivic, M. Sargiacomo, and E. Rodriguez-Boulan. 1989. Steady state distribution and biogenesis of endogenous MDCK glycoproteins: evidence for intracellular sorting and polarized cell surface delivery. J. Cell Biol. 109:2117-2128.
    • (1989) J. Cell Biol. , vol.109 , pp. 2117-2128
    • Lisanti, M.1    Le Bivic, A.2    Sargiacomo, M.3    Rodriguez-Boulan, E.4
  • 40
    • 0029583095 scopus 로고
    • Coronin involved in phagocytosis: Dynamics of particle-induced relocalization visualized by a green fluorescent protein Tag
    • Maniak, M., R. Rauchenberger, R. Albrecht, J. Murphy, and G. Gerisch. 1995. Coronin involved in phagocytosis: dynamics of particle-induced relocalization visualized by a green fluorescent protein Tag. Cell. 83:915-924.
    • (1995) Cell , vol.83 , pp. 915-924
    • Maniak, M.1    Rauchenberger, R.2    Albrecht, R.3    Murphy, J.4    Gerisch, G.5
  • 41
    • 0005002873 scopus 로고
    • Changes in cell function due to inorganic fluoride
    • F.A. Smith, editor. Springer-Verlag, New York
    • Mathews, J. 1970. Changes in cell function due to inorganic fluoride. In Handbook of Experimental Pharmacology. Vol. 20, part 2. F.A. Smith, editor. Springer-Verlag, New York. 98-143.
    • (1970) Handbook of Experimental Pharmacology. , vol.20 , Issue.2 PART , pp. 98-143
    • Mathews, J.1
  • 42
    • 0020804564 scopus 로고
    • Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation
    • Matlin, K.S., and K. Simons. 1983. Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation. Cell. 34:233-243.
    • (1983) Cell , vol.34 , pp. 233-243
    • Matlin, K.S.1    Simons, K.2
  • 43
    • 0027983926 scopus 로고
    • Myosin II is involved in transmitter release at synapses formed between rat sympathetic neurons in culture
    • Mochida, S., Y. Kobayashi, Y. Yuda, K. Muramoto, and N. Nonomura. 1994. Myosin II is involved in transmitter release at synapses formed between rat sympathetic neurons in culture. Neuron. 13:1131-1142.
    • (1994) Neuron. , vol.13 , pp. 1131-1142
    • Mochida, S.1    Kobayashi, Y.2    Yuda, Y.3    Muramoto, K.4    Nonomura, N.5
  • 45
    • 0028889137 scopus 로고
    • Actin filament dissassembly is a sufficient final trigger for exocytosis in nonexitable cells
    • Muallem, S., K. Kwiatkowska, X. Xu, and H.L. Yin. 1995. Actin filament dissassembly is a sufficient final trigger for exocytosis in nonexitable 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
  • 46
    • 0029943503 scopus 로고    scopus 로고
    • Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells
    • Müsch, A., H. Xu, D. Shields, and E. Rodriguez-Boulan. 1996. Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells. J. Cell Biol. 133:543-558.
    • (1996) J. Cell Biol. , vol.133 , pp. 543-558
    • Müsch, A.1    Xu, H.2    Shields, D.3    Rodriguez-Boulan, E.4
  • 47
    • 0028920639 scopus 로고
    • Distinct coated vesicles labeled for p200 bud from trans-Golgi network membranes
    • Narula, N., and J.L. Stow. 1995. Distinct coated vesicles labeled for p200 bud from trans-Golgi network membranes. Proc. Natl. Acad. Sci. USA. 92:2874-2878.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2874-2878
    • Narula, N.1    Stow, J.L.2
  • 49
    • 0028981591 scopus 로고
    • β-NAP, a cerebrellar degeneration antigen, is a neuron-specific vesicle coat protein
    • Newman, L.S., M.O. McKeever, O.J. Hirotaka, and R.B. Darnell. 1995. β-NAP, a cerebrellar degeneration antigen, is a neuron-specific vesicle coat protein. Cell. 82:773-783.
    • (1995) Cell , vol.82 , pp. 773-783
    • Newman, L.S.1    McKeever, M.O.2    Hirotaka, O.J.3    Darnell, R.B.4
  • 50
    • 0027291429 scopus 로고
    • Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol
    • Orci, L., D.J. Palmer, M. Amherdt, and J.E. Rothman. 1993a. Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol. Nature (Lond.). 364:732-734.
    • (1993) Nature (Lond.) , vol.364 , pp. 732-734
    • Orci, L.1    Palmer, D.J.2    Amherdt, M.3    Rothman, J.E.4
  • 51
    • 0027467275 scopus 로고
    • Budding from Golgi membranes requires coatomer complex of non-clathrin coated vesicles
    • Orci, L., D.J. Palmer, M. Ravazzola, A. Perrelet, M. Amherd, and J.E. Rothman. 1993b. Budding from Golgi membranes requires coatomer complex of non-clathrin coated vesicles. Nature (Lond.). 362:648-652.
    • (1993) Nature (Lond.) , vol.362 , pp. 648-652
    • Orci, L.1    Palmer, D.J.2    Ravazzola, M.3    Perrelet, A.4    Amherd, M.5    Rothman, J.E.6
  • 52
    • 0029987840 scopus 로고    scopus 로고
    • Overlapping functions of myosin-I isoforms?
    • Ostap, E.M., and T.D. Pollard. 1996. Overlapping functions of myosin-I isoforms? J. Cell Biol. 133:221-224.
    • (1996) J. Cell Biol. , vol.133 , pp. 221-224
    • Ostap, E.M.1    Pollard, T.D.2
  • 53
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein secretion
    • Palade, G.E. 1975. Intracellular aspects of the process of protein secretion. Science (Wash. DC). 189:374-358.
    • (1975) Science (Wash. DC) , vol.189 , pp. 374-1358
    • Palade, G.E.1
  • 55
    • 0028364351 scopus 로고
    • Basolateral protein transport in streptolysin O-permeabilized MDCK cells
    • Pimplikar, S.W., E. Ikonen, and K. Simons. 1994. Basolateral protein transport in streptolysin O-permeabilized MDCK cells. J. Cell Biol. 125:1025-1035.
    • (1994) J. Cell Biol. , vol.125 , pp. 1025-1035
    • Pimplikar, S.W.1    Ikonen, E.2    Simons, K.3
  • 56
    • 0020023992 scopus 로고
    • Purifications of nonmuscle myosins
    • Pollard, T.D. 1982. Purifications of nonmuscle myosins. Methods Enzymol. 85:331-356.
    • (1982) Methods Enzymol. , vol.85 , pp. 331-356
    • Pollard, T.D.1
  • 57
    • 0026627966 scopus 로고
    • Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: Effects of brefeldin A and G protein activators
    • Robinson, M.S., and T.E. Kreis. 1992. Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: effects of brefeldin A and G protein activators. Cell. 69:129-138.
    • (1992) Cell , vol.69 , pp. 129-138
    • Robinson, M.S.1    Kreis, T.E.2
  • 58
    • 0000747079 scopus 로고
    • Asymmetric budding of viruses in epithelial monolayers: A model system for study of epithelial polarity
    • Rodriguez-Boulan, E., and D.D. Sabatini. 1978. Asymmetric budding of viruses in epithelial monolayers: a model system for study of epithelial polarity Proc. Natl. Acad. Sci. USA. 75:5071-5075.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5071-5075
    • Rodriguez-Boulan, E.1    Sabatini, D.D.2
  • 59
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J.E. 1994. Mechanisms of intracellular protein transport. Nature (Lond.). 372:55-63.
    • (1994) Nature (Lond.) , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 60
    • 0028385277 scopus 로고
    • Implications of the SNARE hypothesis for intracellular membrane topology and dynamics
    • Rothman, J.E., and G. Warren. 1994. Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr. Biol. 4:220-233.
    • (1994) Curr. Biol. , vol.4 , pp. 220-233
    • Rothman, J.E.1    Warren, G.2
  • 61
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman, J.E., and F.T. Wieland. 1996. Protein sorting by transport vesicles Science (Wash. DC). 272:227-234.
    • (1996) Science (Wash. DC) , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 62
    • 0022479585 scopus 로고
    • Microtubules and actin filaments are not critically involved in the biogenesis of epithelial cell surface polarity
    • Salas, P.J., D.E. Misek, D.E. Vega Salas, D. Gundersen, M. Cereijido, and E. Rodriguez-Boulan. 1986. Microtubules and actin filaments are not critically involved in the biogenesis of epithelial cell surface polarity. J. Cell Biol. 102: 1853-1867.
    • (1986) J. Cell Biol. , vol.102 , pp. 1853-1867
    • Salas, P.J.1    Misek, D.E.2    Vega Salas, D.E.3    Gundersen, D.4    Cereijido, M.5    Rodriguez-Boulan, E.6
  • 63
    • 0025259884 scopus 로고
    • Selective modulation of the endocytic uptake of ricin and fluid phase markers without alteration in transferrin endocytosis
    • Sandvig, K., and B. van Deurs. 1990. Selective modulation of the endocytic uptake of ricin and fluid phase markers without alteration in transferrin endocytosis. J. Biol. Chem. 265:6382-6388.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6382-6388
    • Sandvig, K.1    Van Deurs, B.2
  • 64
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., and L. Orci. 1996. Coat proteins and vesicle budding. Science (Wash. DC). 271:1526-1533.
    • (1996) Science (Wash. DC) , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 65
    • 0030001418 scopus 로고    scopus 로고
    • The in vitro generation of post-Golgi vesicles carrying viral envelope glycoproteins requires an ARF-like GTP-binding protein and a protein kinase C associated with the Golgi apparatus
    • Simon, J.-P., I.E. Ivanov, B. Shopsin, D. Hersh, M. Adesnik, and D.D. Sabatini. 1996. The in vitro generation of post-Golgi vesicles carrying viral envelope glycoproteins requires an ARF-like GTP-binding protein and a protein kinase C associated with the Golgi apparatus. J. Biol. Chem. 271:16952-16961.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16952-16961
    • Simon, J.-P.1    Ivanov, I.E.2    Shopsin, B.3    Hersh, D.4    Adesnik, M.5    Sabatini, D.D.6
  • 67
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP ribosylation factor, a small GTP binding protein
    • Stamnes, M.A., and J.E. Rothman. 1993. The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP ribosylation factor, a small GTP binding protein. Cell. 73:999-1005.
    • (1993) Cell , vol.73 , pp. 999-1005
    • Stamnes, M.A.1    Rothman, J.E.2
  • 68
    • 0030047961 scopus 로고    scopus 로고
    • A novel class of clathrin-coated vesicles budding from endosomes
    • Stoorvogel, W., V. Oorschot, and H.J. Geuze. 1996. A novel class of clathrin-coated vesicles budding from endosomes. J. Cell Biol. 132:21-33.
    • (1996) J. Cell Biol. , vol.132 , pp. 21-33
    • Stoorvogel, W.1    Oorschot, V.2    Geuze, H.J.3
  • 69
    • 0025239273 scopus 로고
    • Isolation of subcellular organelles
    • Storrie, B., and E. Madden. 1990. Isolation of subcellular organelles. Methods Enzymol. 182:203-225.
    • (1990) Methods Enzymol. , vol.182 , pp. 203-225
    • Storrie, B.1    Madden, E.2
  • 70
    • 0025785552 scopus 로고
    • Control of actin polymerization in live and permeabilized fibroblasts
    • Symons, M.H., and T.J. Mitchison. 1991. Control of actin polymerization in live and permeabilized fibroblasts. J. Cell Biol. 114:503-513.
    • (1991) J. Cell Biol. , vol.114 , pp. 503-513
    • Symons, M.H.1    Mitchison, T.J.2
  • 71
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals
    • Takel, K., P.S. McPherson, S.L. Schmid, and P. De Camilli. 1995. Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals. Nature (Lond.). 374:186-190.
    • (1995) Nature (Lond.) , vol.374 , pp. 186-190
    • Takel, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 72
    • 0027423161 scopus 로고
    • Biochemical dissection of AP-1 recruitment onto Golgi membranes
    • Traub, L.M., J.A. Ostrom, and S. Kornfeld. 1993. Biochemical dissection of AP-1 recruitment onto Golgi membranes. J. Cell Biol. 123:561-573.
    • (1993) J. Cell Biol. , vol.123 , pp. 561-573
    • Traub, L.M.1    Ostrom, J.A.2    Kornfeld, S.3
  • 74
    • 0027302723 scopus 로고
    • Characterization of a caldesmon fragment that competes with myosin-ATP binding to actin
    • Velaz, L., Y.-d. Chen, and J. Chalovich. 1993. Characterization of a caldesmon fragment that competes with myosin-ATP binding to actin. Biophys. J. 65:892-898.
    • (1993) Biophys. J. , vol.65 , pp. 892-898
    • Velaz, L.1    Chen, Y.-D.2    Chalovich, J.3
  • 75
    • 0028301797 scopus 로고
    • Brefeldin a causes structural and functional alterations of the trans-Golgi network of MDCK cells
    • Wagner, M., A.K. Rajasekaran, D.K. Hanzel, S. Mayor, and E. Rodriguez-Boulan. 1994. Brefeldin A causes structural and functional alterations of the trans-Golgi network of MDCK cells. J. Cell Sci. 107:933-943.
    • (1994) J. Cell Sci. , vol.107 , pp. 933-943
    • Wagner, M.1    Rajasekaran, A.K.2    Hanzel, D.K.3    Mayor, S.4    Rodriguez-Boulan, E.5
  • 76
    • 0348028030 scopus 로고
    • Effect of inorganic fluoride on enzymes
    • F.A. Smith, editor. Springer-Verlag, New York
    • Wiseman, A. 1970. Effect of inorganic fluoride on enzymes. In Handbook of Experimental Pharmacology. Vol. 20, part 2. F.A. Smith, editor. Springer-Verlag, New York. 48-97.
    • (1970) Handbook of Experimental Pharmacology , vol.20 , Issue.2 PART , pp. 48-97
    • Wiseman, A.1
  • 77
    • 0028875216 scopus 로고
    • Cytoplasmic coat proteins involved in endosome fusion
    • Whitney, J.A., M. Gomez, D. Sheff, T.E. Kreis, and I. Mellman. 1995. Cytoplasmic coat proteins involved in endosome fusion. Cell. 83:703-713.
    • (1995) Cell , vol.83 , pp. 703-713
    • Whitney, J.A.1    Gomez, M.2    Sheff, D.3    Kreis, T.E.4    Mellman, I.5
  • 79
    • 0029879919 scopus 로고    scopus 로고
    • Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells
    • Yoshimori, T., P. Keller, M.G. Roth, and K. Simons. 1996. Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells. J. Cell Biol. 133:247-256.
    • (1996) J. Cell Biol. , vol.133 , pp. 247-256
    • Yoshimori, T.1    Keller, P.2    Roth, M.G.3    Simons, K.4


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