메뉴 건너뛰기




Volumn 9, Issue 10, 1998, Pages 2699-2714

In vitro reconstitution of microtubule plus end-directed, GTPγS- sensitive motility of Golgi membranes

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE; OKADAIC ACID; PHOSPHATASE; PROTEIN KINASE; STAUROSPORINE;

EID: 0031664962     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.10.2699     Document Type: Article
Times cited : (29)

References (83)
  • 1
    • 0029084786 scopus 로고
    • The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events
    • Acharya, U., Jacobs, R., Peters, J.-M., Watson, N., Farquhar, M.G., and Malhotra, V. (1995a). The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events. Cell 82, 895-904.
    • (1995) Cell , vol.82 , pp. 895-904
    • Acharya, U.1    Jacobs, R.2    Peters, J.-M.3    Watson, N.4    Farquhar, M.G.5    Malhotra, V.6
  • 2
    • 0028960491 scopus 로고
    • Reconstitution of vesiculated Golgi membranes into stacks of cisternae: Requirement of NSF in stack formation
    • Acharya, U., McCaffery, J.M., Jacobs, R., and Malhotra, V. (1995b). Reconstitution of vesiculated Golgi membranes into stacks of cisternae: requirement of NSF in stack formation. J. Cell Biol. 129, 577-590.
    • (1995) J. Cell Biol. , vol.129 , pp. 577-590
    • Acharya, U.1    McCaffery, J.M.2    Jacobs, R.3    Malhotra, V.4
  • 3
    • 0028943648 scopus 로고
    • Protein phosphatase 1 regulates the cytoplasmic dynein-driven formation of endoplasmic reticulum networks in vitro
    • Allan, V. (1995). Protein phosphatase 1 regulates the cytoplasmic dynein-driven formation of endoplasmic reticulum networks in vitro. J. Cell Biol. 128, 879-891.
    • (1995) J. Cell Biol. , vol.128 , pp. 879-891
    • Allan, V.1
  • 4
    • 0028284465 scopus 로고
    • Movement of membrane tubules along microtubules in vitro: Evidence for specialised sites of motor attachment
    • Allan, V., and Vale, R. (1994). Movement of membrane tubules along microtubules in vitro: evidence for specialised sites of motor attachment. J. Cell Sci. 107, 1885-1897.
    • (1994) J. Cell Sci. , vol.107 , pp. 1885-1897
    • Allan, V.1    Vale, R.2
  • 5
    • 0025829696 scopus 로고
    • Cell cycle control of microtubule-based membrane transport and tubule formation in vitro
    • Allan, V.J., and Vale, R.D. (1991). Cell cycle control of microtubule-based membrane transport and tubule formation in vitro. J. Cell Biol. 113, 347-359.
    • (1991) J. Cell Biol. , vol.113 , pp. 347-359
    • Allan, V.J.1    Vale, R.D.2
  • 6
    • 0019849712 scopus 로고
    • Video-enhanced contrast, differential interference contrast (AVEC-DIC) microscopy: A new method capable of analyzing microtubule-related motility in the reticulopodial network of Allogromia laticollaris
    • Allen, R.D., Allen, N.S., and Travis, J.L. (1981). Video-enhanced contrast, differential interference contrast (AVEC-DIC) microscopy: a new method capable of analyzing microtubule-related motility in the reticulopodial network of Allogromia laticollaris. Cell Motil. 1, 291-302.
    • (1981) Cell Motil. , vol.1 , pp. 291-302
    • Allen, R.D.1    Allen, N.S.2    Travis, J.L.3
  • 7
    • 0024811663 scopus 로고
    • The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium
    • Bacallao, R., Antony, C., Dotti, C., Karsenti, E., Stelzer, E.H.K., and Simons, K. (1989). The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium. J. Cell Biol. 109, 2817-2832.
    • (1989) J. Cell Biol. , vol.109 , pp. 2817-2832
    • Bacallao, R.1    Antony, C.2    Dotti, C.3    Karsenti, E.4    Stelzer, E.H.K.5    Simons, K.6
  • 9
    • 0032559708 scopus 로고    scopus 로고
    • Cruising along microtubule highways: How membranes move through the secretory pathway
    • Bloom, G.S., and Goldstein, L.S.B. (1998). Cruising along microtubule highways: how membranes move through the secretory pathway. J. Cell Biol. 140, 1277-1280.
    • (1998) J. Cell Biol. , vol.140 , pp. 1277-1280
    • Bloom, G.S.1    Goldstein, L.S.B.2
  • 11
    • 0023944514 scopus 로고
    • Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptide
    • Bloom, G.S., Wagner, M.C., Pfister, K.K., and Brady, S.T. (1988). Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptide. Biochemistry 27, 3409-3416.
    • (1988) Biochemistry , vol.27 , pp. 3409-3416
    • Bloom, G.S.1    Wagner, M.C.2    Pfister, K.K.3    Brady, S.T.4
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0021894565 scopus 로고
    • Video microscopy of fast axonal transport in extruded axoplasm: A new model for study of molecular mechanisms
    • Brady, S.T., Lasek, R.J., and Allen, R.D. (1985). Video microscopy of fast axonal transport in extruded axoplasm: a new model for study of molecular mechanisms. Cell Motil. 5, 81-101.
    • (1985) Cell Motil. , vol.5 , pp. 81-101
    • Brady, S.T.1    Lasek, R.J.2    Allen, R.D.3
  • 14
    • 0025021497 scopus 로고
    • A monoclonal antibody against kinesin inhibits both anterograde and retrograde fast axonal transport in squid axoplasm
    • Brady, S.T., Pfister, K.K., and Bloom, G.S. (1990). A monoclonal antibody against kinesin inhibits both anterograde and retrograde fast axonal transport in squid axoplasm. Proc. Natl. Acad. Sci. USA 87, 1061-1065.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1061-1065
    • Brady, S.T.1    Pfister, K.K.2    Bloom, G.S.3
  • 15
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • Burkhardt, J.K., Echeverri, C.J., Nilsson, T., and Vallee, R.B. (1997). Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution. J. Cell Biol. 139, 469-484.
    • (1997) J. Cell Biol. , vol.139 , pp. 469-484
    • Burkhardt, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 16
    • 0024361302 scopus 로고
    • An improved procedure for identifying and quantifying protein phosphatases in mammalian tissues
    • Cohen, P., Klummp, S., and Schelling, D.L. (1989). An improved procedure for identifying and quantifying protein phosphatases in mammalian tissues. FEBS Lett. 250, 596-600.
    • (1989) FEBS Lett. , vol.250 , pp. 596-600
    • Cohen, P.1    Klummp, S.2    Schelling, D.L.3
  • 17
    • 0023194090 scopus 로고
    • Correlation between the ATPase and microtubule translocating activities of sea urchin egg kinesin
    • Cohn, S.A., Ingold, A.L., and Scholey, J.M. (1987). Correlation between the ATPase and microtubule translocating activities of sea urchin egg kinesin. Nature 328, 160-163.
    • (1987) Nature , vol.328 , pp. 160-163
    • Cohn, S.A.1    Ingold, A.L.2    Scholey, J.M.3
  • 18
    • 0024601079 scopus 로고
    • Quantitative analysis of sea urchin egg kinesin-driven microtubule motility
    • Cohn, S.A., Ingold, A.L., and Scholey, J.M. (1989). Quantitative analysis of sea urchin egg kinesin-driven microtubule motility. J. Biol. Chem. 264, 4290-4297.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4290-4297
    • Cohn, S.A.1    Ingold, A.L.2    Scholey, J.M.3
  • 19
    • 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., and Lippincott-Schwartz, J. (1996). Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites. Mol. Biol. Cell 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
  • 20
    • 0024041810 scopus 로고
    • The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cells
    • Dabora, S.L., and Sheetz, M.P. (1988). The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cells. Cell 54, 27-35.
    • (1988) Cell , vol.54 , pp. 27-35
    • Dabora, S.L.1    Sheetz, M.P.2
  • 21
    • 0029929903 scopus 로고    scopus 로고
    • Differential distribution of a subunits and βγ subunits of heterotrimeric G proteins on Golgi membranes of the exocrine pancreas
    • Denker, S.P., McCaffery, J.M., Palade, G.E., Insel, P.A., and Farquhar, M.G. (1996). Differential distribution of a subunits and βγ subunits of heterotrimeric G proteins on Golgi membranes of the exocrine pancreas. J. Cell Biol. 133, 1027-1040.
    • (1996) J. Cell Biol. , vol.133 , pp. 1027-1040
    • Denker, S.P.1    McCaffery, J.M.2    Palade, G.E.3    Insel, P.A.4    Farquhar, M.G.5
  • 23
    • 0025325861 scopus 로고
    • Membrane localization of the pertussis toxin-sensitive G-protein subunits αi2 and αi3 and expression of a metallothionein-αi2 fusion gene in LLC-PK1 cells
    • Ercolani, L., Stow, J.L., Boyle, J.F., Holtzman, E.J., and Lin, H. (1990). Membrane localization of the pertussis toxin-sensitive G-protein subunits αi2 and αi3 and expression of a metallothionein-αi2 fusion gene in LLC-PK1 cells. Proc. Natl. Acad. Sci. USA 87, 4635-4639.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4635-4639
    • Ercolani, L.1    Stow, J.L.2    Boyle, J.F.3    Holtzman, E.J.4    Lin, H.5
  • 25
    • 0025887459 scopus 로고
    • Microtubule dynamics: Mechanism, regulation and function
    • Gelfand, V.I., and Bershadsky, A.D. (1991). Microtubule dynamics: mechanism, regulation and function. Annu. Rev. Cell Biol. 7, 93-116.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 93-116
    • Gelfand, V.I.1    Bershadsky, A.D.2
  • 26
    • 1842384421 scopus 로고
    • ADP-ribosylation of membrane proteins catalyzed by cholera toxin: Basis of the activation of adenylate cyclase
    • Gill, D.M., and Meren, R. (1978). ADP-ribosylation of membrane proteins catalyzed by cholera toxin: basis of the activation of adenylate cyclase. Proc. Natl. Acad. Sci. USA 75, 3050-3054.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3050-3054
    • Gill, D.M.1    Meren, R.2
  • 27
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman, A.G. (1987). G proteins: transducers of receptor-generated signals. Annu. Rev. Biochem. 56, 615-649.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 28
    • 0032559822 scopus 로고    scopus 로고
    • Processivity of the motor protein kinesin requires two heads
    • Hancock, W.O., and Howard, J. (1998). Processivity of the motor protein kinesin requires two heads. J. Cell Biol. 140, 1395-1405.
    • (1998) J. Cell Biol. , vol.140 , pp. 1395-1405
    • Hancock, W.O.1    Howard, J.2
  • 29
    • 0028965528 scopus 로고
    • In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum
    • Hendershot, L.M., Wei, J., Gaut, J.R., Lawson, B., Freiden, P.J., and Murti, K.G. (1995). In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum. Mol. Biol. Cell 6, 283-296.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 283-296
    • Hendershot, L.M.1    Wei, J.2    Gaut, J.R.3    Lawson, B.4    Freiden, P.J.5    Murti, K.G.6
  • 30
    • 0029942238 scopus 로고    scopus 로고
    • Association of a dynamin-like protein with the Golgi apparatus in mammalian cells
    • Henley, J.R., and McNiven, M.A. (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
  • 31
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa, N. (1998). Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279, 519-526.
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 32
    • 0024591237 scopus 로고
    • Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration
    • Hirokawa, N., Pfister, K.K., Yorifuji, H., Wagner, M.C., Brady, S.T., and Bloom, G.S. (1989). Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration. Cell 56, 867-878.
    • (1989) Cell , vol.56 , pp. 867-878
    • Hirokawa, N.1    Pfister, K.K.2    Yorifuji, H.3    Wagner, M.C.4    Brady, S.T.5    Bloom, G.S.6
  • 33
    • 0345420100 scopus 로고    scopus 로고
    • Golgi to plasma membrane trafficking in living cells: Characterization of post-Golgi intermediates
    • abstract
    • Hirschberg, K., Presley, J., Cole, N., and Lippincott-Schwartz, J. (1997). Golgi to plasma membrane trafficking in living cells: characterization of post-Golgi intermediates. Mol. Biol. Cell 8, 194a (abstract).
    • (1997) Mol. Biol. Cell , vol.8
    • Hirschberg, K.1    Presley, J.2    Cole, N.3    Lippincott-Schwartz, J.4
  • 34
    • 0032548940 scopus 로고    scopus 로고
    • Fluoride activation of the rho family GTP-binding protein Cdc42Hs
    • Hoffman, G.R., Nassar, N., Oswald, R.E., and Cerione, R.A. (1998). Fluoride activation of the rho family GTP-binding protein Cdc42Hs. J. Biol. Chem. 273, 4392-4399.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4392-4399
    • Hoffman, G.R.1    Nassar, N.2    Oswald, R.E.3    Cerione, R.A.4
  • 35
    • 0030570801 scopus 로고    scopus 로고
    • Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor
    • Hotta, K., Tanaka, K., Mino, A., Kohno, H., and Takai, Y. (1996). Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor. Biochem. Biophys. Res. Commun. 225, 69-74.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 69-74
    • Hotta, K.1    Tanaka, K.2    Mino, A.3    Kohno, H.4    Takai, Y.5
  • 37
    • 0026452219 scopus 로고
    • G protein βγ subunits synthesized in Sf9 cells: Functional characterization and the significance of prenylation of γ
    • Iñiguez-Lluhi, J.A., Simon, M.I., Robishaw, J.D., and Gilman, A.G. (1992). G protein βγ subunits synthesized in Sf9 cells: functional characterization and the significance of prenylation of γ. J. Biol. Chem. 267, 23409-23417.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23409-23417
    • Iñiguez-Lluhi, J.A.1    Simon, M.I.2    Robishaw, J.D.3    Gilman, A.G.4
  • 39
    • 0032559342 scopus 로고    scopus 로고
    • Role of dynamin in the formation of transport vesicles from the trans-Golgi network
    • Jones, S.M., Howell, K.E., Henley, J.R., Cao, H., and McNiven, M.A. (1998). Role of dynamin in the formation of transport vesicles from the trans-Golgi network. Science 279, 573-577.
    • (1998) Science , vol.279 , pp. 573-577
    • Jones, S.M.1    Howell, K.E.2    Henley, J.R.3    Cao, H.4    McNiven, M.A.5
  • 40
    • 0025996803 scopus 로고
    • Fluoride is not an activator of the smaller (20-25 kDa) GTP-binding proteins
    • Kahn, R.A. (1991). Fluoride is not an activator of the smaller (20-25 kDa) GTP-binding proteins. J. Biol. Chem. 266, 15595-15597.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15595-15597
    • Kahn, R.A.1
  • 41
    • 0022961250 scopus 로고
    • Purification and characterization of Chlamydomonas flagellar dyneins
    • King, S.M., Otter, T., and Witman, G.B. (1986). Purification and characterization of Chlamydomonas flagellar dyneins. Methods Enzymol. 134, 291-306.
    • (1986) Methods Enzymol. , vol.134 , pp. 291-306
    • King, S.M.1    Otter, T.2    Witman, G.B.3
  • 42
    • 0025267442 scopus 로고
    • Role of microtubules in the organization of the Golgi apparatus
    • Kreis, T.E. (1990). Role of microtubules in the organization of the Golgi apparatus. Cell Motil. Cytoskel. 15, 67-70.
    • (1990) Cell Motil. Cytoskel. , vol.15 , pp. 67-70
    • Kreis, T.E.1
  • 44
    • 0022981422 scopus 로고
    • Bovine brain kinesin is a microtubule-activated ATPase
    • Kuznetsov, S.A., and Gelfand, V.I. (1986). Bovine brain kinesin is a microtubule-activated ATPase. Proc. Natl. Acad. Sci. USA 83, 8530-8534.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8530-8534
    • Kuznetsov, S.A.1    Gelfand, V.I.2
  • 45
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 46
    • 0028048171 scopus 로고
    • Expression of G-protein α subunits in Escherichia coli
    • Lee, E., Linder, M.L., and Gilman, A.G. (1994). Expression of G-protein α subunits in Escherichia coli. Methods Enzymol. 237, 146-164.
    • (1994) Methods Enzymol. , vol.237 , pp. 146-164
    • Lee, E.1    Linder, M.L.2    Gilman, A.G.3
  • 49
    • 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., and Klausner, R.D. (1990). Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 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    Klausner, R.D.7
  • 50
    • 0023441953 scopus 로고
    • Fragmentation and partitioning of the Golgi apparatus during mitosis in HeLa cells
    • Lucocq, J.M., and Warren, G. (1987). Fragmentation and partitioning of the Golgi apparatus during mitosis in HeLa cells. EMBO J. 6, 3239-3246.
    • (1987) EMBO J. , vol.6 , pp. 3239-3246
    • Lucocq, J.M.1    Warren, G.2
  • 51
    • 0023663075 scopus 로고
    • Identification of a microtubule-based cytoplasmic motor in the nematode C. elegans
    • Lye, R.J., Porter, M.E., Scholey, J.M., and McIntosh, J.R. (1987). Identification of a microtubule-based cytoplasmic motor in the nematode C. elegans. Cell 51, 309-318.
    • (1987) Cell , vol.51 , pp. 309-318
    • Lye, R.J.1    Porter, M.E.2    Scholey, J.M.3    McIntosh, J.R.4
  • 52
    • 0028104096 scopus 로고
    • Association of kinesin with the Golgi apparatus in rat hepatocytes
    • Marks, D.L., Larkin, J.M., and McNiven, M.A. (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    Larkin, J.M.2    McNiven, M.A.3
  • 53
    • 0028327124 scopus 로고
    • COP-coated vesicles are involved in the mitotic fragmentation of Golgi stacks in a cell-free system
    • Misteli, T., and Warren, G. (1994). COP-coated vesicles are involved in the mitotic fragmentation of Golgi stacks in a cell-free system. J. Cell Biol. 125, 269-282.
    • (1994) J. Cell Biol. , vol.125 , pp. 269-282
    • Misteli, T.1    Warren, G.2
  • 54
    • 0030036699 scopus 로고    scopus 로고
    • Formation of a transition-state analog of the Ras GTPase reaction by Ras-GDP, tetrafluoroaluminate, and GTPase-activating proteins
    • Mittal, R., Ahmadian, M.R., Goody, R.S., and Wittinghofer, A. (1996). Formation of a transition-state analog of the Ras GTPase reaction by Ras-GDP, tetrafluoroaluminate, and GTPase-activating proteins. Science 273, 115-117.
    • (1996) Science , vol.273 , pp. 115-117
    • Mittal, R.1    Ahmadian, M.R.2    Goody, R.S.3    Wittinghofer, A.4
  • 55
    • 0028177082 scopus 로고
    • αi2 to the Golgi by alternative spliced carboxyl-terminal region
    • αi2 to the Golgi by alternative spliced carboxyl-terminal region. Science 263, 95-98.
    • (1994) Science , vol.263 , pp. 95-98
    • Montmayeur, J.-P.1    Borrelli, E.2
  • 56
    • 0021100134 scopus 로고
    • Actiavation by thiol of the latent NAD glycohydrolase and ADP-ribosyltransferase activities of Bordetella pertussis toxin (islet activating protein)
    • Moss, J., Stanley, S.J., Burns, D.L., Hsia, J.A., Yost, D.A., Myers, G.A., and Hewlett, E.L. (1983). Actiavation by thiol of the latent NAD glycohydrolase and ADP-ribosyltransferase activities of Bordetella pertussis toxin (islet activating protein). J. Biol. Chem. 258, 11879-11882.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11879-11882
    • Moss, J.1    Stanley, S.J.2    Burns, D.L.3    Hsia, J.A.4    Yost, D.A.5    Myers, G.A.6    Hewlett, E.L.7
  • 57
    • 0032472369 scopus 로고    scopus 로고
    • The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3
    • Nagata, K., Puls, A., Futter, C., Aspenstrom, P., Schaefer, E., Nakata, T., Hirokawa, N., and Hall, A. (1998). The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3. EMBO J. 27, 149-158.
    • (1998) EMBO J. , vol.27 , pp. 149-158
    • Nagata, K.1    Puls, A.2    Futter, C.3    Aspenstrom, P.4    Schaefer, E.5    Nakata, T.6    Hirokawa, N.7    Hall, A.8
  • 58
    • 0029954709 scopus 로고    scopus 로고
    • Cell cycle regulation of dynein association with membranes modulates microtubule-based organelle transport
    • Niclas, J., Allan, V.J., and Vale, R.D. (1996). Cell cycle regulation of dynein association with membranes modulates microtubule-based organelle transport. J. Cell Biol. 133, 585-593.
    • (1996) J. Cell Biol. , vol.133 , pp. 585-593
    • Niclas, J.1    Allan, V.J.2    Vale, R.D.3
  • 59
    • 0025729050 scopus 로고
    • Biosynthesis of lysosomal enzymes in cells of the End3 complementation group conditionally defective in endosomal acidification
    • Park, J.E., Draper, R.K., and Brown, W.J. (1991). Biosynthesis of lysosomal enzymes in cells of the End3 complementation group conditionally defective in endosomal acidification. Somat. Cell Mol. Genet. 17, 137-150.
    • (1991) Somat. Cell Mol. Genet. , vol.17 , pp. 137-150
    • Park, J.E.1    Draper, R.K.2    Brown, W.J.3
  • 60
    • 0023205148 scopus 로고
    • Retrograde transport by the microtubule-associated protein MAP 1C
    • Paschal, B.M., and Vallee, R.B. (1987). Retrograde transport by the microtubule-associated protein MAP 1C. Nature 330, 181-183.
    • (1987) Nature , vol.330 , pp. 181-183
    • Paschal, B.M.1    Vallee, R.B.2
  • 61
    • 0027720243 scopus 로고
    • Microtubule and axoneme gliding assays for force production by microtubule motor proteins
    • Paschal, B.M., and Vallee, R.B. (1993). Microtubule and axoneme gliding assays for force production by microtubule motor proteins. Methods Cell Biol. 39, 65-74.
    • (1993) Methods Cell Biol. , vol.39 , pp. 65-74
    • Paschal, B.M.1    Vallee, R.B.2
  • 62
    • 0024512960 scopus 로고
    • Monoclonal antibodies to kinesin heavy and light chains stain vesicle-like structures, but not microtubules, in cultured cells
    • Pfister, K.K., Wagner, M.C., Stenoien, D.A., Brady, S.T., and Bloom, G.S. (1989). Monoclonal antibodies to kinesin heavy and light chains stain vesicle-like structures, but not microtubules, in cultured cells. J. Cell Biol. 108, 1453-1463.
    • (1989) J. Cell Biol. , vol.108 , pp. 1453-1463
    • Pfister, K.K.1    Wagner, M.C.2    Stenoien, D.A.3    Brady, S.T.4    Bloom, G.S.5
  • 66
    • 0032489499 scopus 로고    scopus 로고
    • Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro
    • Rabouille, C., Kondo, H., Newman, R., Hui, N., Freemont, P., and Warren, G. (1998). Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro. Cell 92, 603-610.
    • (1998) Cell , vol.92 , pp. 603-610
    • Rabouille, C.1    Kondo, H.2    Newman, R.3    Hui, N.4    Freemont, P.5    Warren, G.6
  • 67
    • 0029089959 scopus 로고
    • An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments
    • Rabouille, C., Levine, T.P., Peters, J.-M., and Warren, G. (1995). An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments. Cell 82, 905-914.
    • (1995) Cell , vol.82 , pp. 905-914
    • Rabouille, C.1    Levine, T.P.2    Peters, J.-M.3    Warren, G.4
  • 68
    • 0028930157 scopus 로고
    • Reassembly of Golgi stacks from mitotic Golgi fragments in a cell-free system
    • Rabouille, C., Misteli, T., Watson, R., and Warren, G. (1995). Reassembly of Golgi stacks from mitotic Golgi fragments in a cell-free system. J. Cell Biol. 129, 605-618.
    • (1995) J. Cell Biol. , vol.129 , pp. 605-618
    • Rabouille, C.1    Misteli, T.2    Watson, R.3    Warren, G.4
  • 69
    • 0028584420 scopus 로고
    • Microtubules are oriented with their minus-ends directed apically before tight junction formation in rat Sertoli cells
    • Redenbach, D.M., and Boekelheide, K. (1994). Microtubules are oriented with their minus-ends directed apically before tight junction formation in rat Sertoli cells. Eur. J. Cell Biol. 65, 246-257.
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 246-257
    • Redenbach, D.M.1    Boekelheide, K.2
  • 70
    • 0031586946 scopus 로고    scopus 로고
    • Aluminum fluoride associates with the small guanine nucleotide binding proteins
    • Reza, M., Mittal, R., Hall, A., and Wittinghofer, A. (1997). Aluminum fluoride associates with the small guanine nucleotide binding proteins. FEBS Lett. 408, 315-318.
    • (1997) FEBS Lett. , vol.408 , pp. 315-318
    • Reza, M.1    Mittal, R.2    Hall, A.3    Wittinghofer, A.4
  • 71
    • 0024078184 scopus 로고
    • Characterization of the microtubule-activated ATPase of brain cytoplasmic dynein (MAP 1C)
    • Shpetner, H.S., Paschal, B.M., and Vallee, R.B. (1988). Characterization of the microtubule-activated ATPase of brain cytoplasmic dynein (MAP 1C). J. Cell Biol. 107, 1001-1009.
    • (1988) J. Cell Biol. , vol.107 , pp. 1001-1009
    • Shpetner, H.S.1    Paschal, B.M.2    Vallee, R.B.3
  • 72
    • 0019921514 scopus 로고
    • Aluminum: A requirement for activation of the regulatory component of adenylate cyclase by fluoride
    • Sternweiss, P.C., and Gilman, A.G. (1982). Aluminum: a requirement for activation of the regulatory component of adenylate cyclase by fluoride. Proc. Natl. Acad. Sci. USA 79, 4888-4891.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4888-4891
    • Sternweiss, P.C.1    Gilman, A.G.2
  • 73
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • Svoboda, K., Schmidt, C.F., Schnapp, B.J., and Block, S.M. (1993). Direct observation of kinesin stepping by optical trapping interferometry. Nature 365, 721-727.
    • (1993) Nature , vol.365 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 74
    • 0026517912 scopus 로고
    • Evidence for kinesin-related proteins in the mitotic apparatus using peptide antibodies
    • Swain, K.E., Mitchison, T.J., and Wordeman, L.G. (1992). Evidence for kinesin-related proteins in the mitotic apparatus using peptide antibodies. J. Cell Sci. 101, 303-313.
    • (1992) J. Cell Sci. , vol.101 , pp. 303-313
    • Swain, K.E.1    Mitchison, T.J.2    Wordeman, L.G.3
  • 76
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 77
    • 0026775359 scopus 로고
    • Kinectin, a major kinesin-binding protein on ER
    • Toyoshima, I., Yu, H., Steuer, E.R., and Sheetz, M.P. (1992). Kinectin, a major kinesin-binding protein on ER. J. Cell Biol. 118, 1121-1131.
    • (1992) J. Cell Biol. , vol.118 , pp. 1121-1131
    • Toyoshima, I.1    Yu, H.2    Steuer, E.R.3    Sheetz, M.P.4
  • 78
    • 0024211157 scopus 로고
    • Formation of membrane networks in vitro by kinesin-driven microtubule movement
    • Vale, R.D., and Hotani, H. (1988). Formation of membrane networks in vitro by kinesin-driven microtubule movement. J. Cell Biol. 107, 2233-2241.
    • (1988) J. Cell Biol. , vol.107 , pp. 2233-2241
    • Vale, R.D.1    Hotani, H.2
  • 79
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
    • Vale, R.D., Reese, T.S., and Sheetz, M.P. (1985). Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell 42, 39-50.
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 80
    • 0024506317 scopus 로고
    • Copurification of kinesin polypeptides with microtubule-stimulated Mg-ATPase activity and kinetic analysis of enzymatic processes
    • Wagner, M.C., Pfister, K.K., Bloom, G.S., and Brady, S.T. (1989). Copurification of kinesin polypeptides with microtubule-stimulated Mg-ATPase activity and kinetic analysis of enzymatic processes. Cell Motil. Cytoskel. 12, 195-215.
    • (1989) Cell Motil. Cytoskel. , vol.12 , pp. 195-215
    • Wagner, M.C.1    Pfister, K.K.2    Bloom, G.S.3    Brady, S.T.4
  • 81
    • 0026014164 scopus 로고
    • A mutated transferrin receptor lacking asparagine-linked glycosylation sites shows reduced functionality and an association with binding immunoglobulin protein
    • Williams, A.M., and Enns, C.A. (1991). A mutated transferrin receptor lacking asparagine-linked glycosylation sites shows reduced functionality and an association with binding immunoglobulin protein. J. Biol. Chem. 266, 17648-17654.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17648-17654
    • Williams, A.M.1    Enns, C.A.2
  • 82
    • 0028079674 scopus 로고
    • Cellular variations in heterotrimeric G protein localization and expression in rat pituitary
    • Wilson, B.S., Komuro, M., and Farquhar, M.G. (1994). Cellular variations in heterotrimeric G protein localization and expression in rat pituitary. Endocrinology 134, 233-244.
    • (1994) Endocrinology , vol.134 , pp. 233-244
    • Wilson, B.S.1    Komuro, M.2    Farquhar, M.G.3
  • 83
    • 0022962478 scopus 로고
    • Isolation of Chlamydomonas flagella and flagellar axonemes
    • Witman, G.B. (1986). Isolation of Chlamydomonas flagella and flagellar axonemes. Methods Enzymol. 134, 280-290.
    • (1986) Methods Enzymol. , vol.134 , pp. 280-290
    • Witman, G.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.