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Volumn 17, Issue 21, 1998, Pages 6168-6177

A novel direct interaction of endoplasmic reticulum with microtubules

Author keywords

Cytoskeleton; Endoplasmic reticulum; Linker protein; Microtubules; p63

Indexed keywords

MEMBRANE PROTEIN; MUTANT PROTEIN;

EID: 0032476663     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.21.6168     Document Type: Article
Times cited : (161)

References (59)
  • 1
    • 0028943648 scopus 로고
    • Protein phosphatase 1 regulates the cytoplasmic dyneindriven formation of endoplasmic reticulum networks in vitro
    • Allan,V. (1995a) Protein phosphatase 1 regulates the cytoplasmic dyneindriven 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
  • 2
    • 0029127631 scopus 로고
    • Membrane traffic motors
    • Allan,V. (1995b) Membrane traffic motors. FEES Lett., 369, 101-106.
    • (1995) FEES Lett. , vol.369 , pp. 101-106
    • Allan, V.1
  • 3
    • 0025182686 scopus 로고
    • Molecular biology of circulatory shock. Part II. Expression of four groups of hepatic genes is enhanced after resuscitation from cardiogenic shock
    • Buchman,T.G., Cabin,D.E., Vickers,S., Deutschman,C.S., Delgado,E., Sussman,M.M. and Bulkley,G.B. (1990) Molecular biology of circulatory shock. Part II. Expression of four groups of hepatic genes is enhanced after resuscitation from cardiogenic shock. Surgery, 108, 559-566.
    • (1990) Surgery , vol.108 , pp. 559-566
    • Buchman, T.G.1    Cabin, D.E.2    Vickers, S.3    Deutschman, C.S.4    Delgado, E.5    Sussman, M.M.6    Bulkley, G.B.7
  • 4
    • 0029670547 scopus 로고    scopus 로고
    • In search of membrane receptors for microtubule-based motors - Is kinectin a kinesin receptor?
    • Burkhardt,J.K. (1996) In search of membrane receptors for microtubule-based motors - Is kinectin a kinesin receptor? Trends Cell Biol., 6, 127-131.
    • (1996) Trends Cell Biol. , vol.6 , pp. 127-131
    • Burkhardt, J.K.1
  • 5
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • Burkhard,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
    • Burkhard, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 6
    • 0025959396 scopus 로고
    • Non-neuronal 210×10(3) Mr microtubule-associated protein (MAP4) contains a domain homologous to the microtubule-binding domain of neuronal MAP2 and tau
    • Chapin,S.J. and Bulinski,J.C. (1991) Non-neuronal 210×10(3) Mr microtubule-associated protein (MAP4) contains a domain homologous to the microtubule-binding domain of neuronal MAP2 and tau. J. Cell Sci., 98, 27-36.
    • (1991) J. Cell Sci. , vol.98 , pp. 27-36
    • Chapin, S.J.1    Bulinski, J.C.2
  • 7
    • 0028950267 scopus 로고
    • Organization of organelles and membrane traffic by microtubules
    • Cole,N.B. and 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
  • 8
    • 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
  • 9
    • 0025228404 scopus 로고
    • Tubulovesicular processes emerge from the trans-Golgi cisternae, extend along microtubules, and interlink adjacent trans-Golgi elements into a reticulum
    • Cooper,M.S., Cornell-Bell,A.H., Chernjavsky,A., Dani,J.W. and Smith,S.J. (1990) Tubulovesicular processes emerge from the trans-Golgi cisternae, extend along microtubules, and interlink adjacent trans-Golgi elements into a reticulum. Cell, 61, 135-145.
    • (1990) Cell , vol.61 , pp. 135-145
    • Cooper, M.S.1    Cornell-Bell, A.H.2    Chernjavsky, A.3    Dani, J.W.4    Smith, S.J.5
  • 10
    • 0023084134 scopus 로고
    • Use of eukaryotic expression technology in the functional analysis of cloned genes
    • Cullen,B.R. (1987) Use of eukaryotic expression technology in the functional analysis of cloned genes. Methods Enzymol., 152, 684-704.
    • (1987) Methods Enzymol. , vol.152 , pp. 684-704
    • Cullen, B.R.1
  • 11
    • 0024041810 scopus 로고
    • The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cell extracts
    • Dabora,S.L. and Sheetz,M.P. (1988) The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cell extracts. Cell, 54, 27-35.
    • (1988) Cell , vol.54 , pp. 27-35
    • Dabora, S.L.1    Sheetz, M.P.2
  • 12
    • 0026034581 scopus 로고
    • The endoplasmic reticulum retention signal of the E3/19K protein of adenovirus-2 is microtubule binding
    • Dahllöf,B., Wallin,M. and Kvist,S. (1991) The endoplasmic reticulum retention signal of the E3/19K protein of adenovirus-2 is microtubule binding. J. Biol. Chew., 266, 1804-1808.
    • (1991) J. Biol. Chew. , vol.266 , pp. 1804-1808
    • Dahllöf, B.1    Wallin, M.2    Kvist, S.3
  • 13
    • 0031459588 scopus 로고    scopus 로고
    • CLIP-115, a novel brain-specific cytoplasmic linker protein, mediates the localization of dendritic lamellar bodies
    • De Zeeuw,C.I., Hoogenraad,C.C., Goedknegt,E., Hertzberg,E., Neubauer,A., Grosveld,F. and Galjart,N. (1997) CLIP-115, a novel brain-specific cytoplasmic linker protein, mediates the localization of dendritic lamellar bodies. Neuron, 19, 1187-1199.
    • (1997) Neuron , vol.19 , pp. 1187-1199
    • De Zeeuw, C.I.1    Hoogenraad, C.C.2    Goedknegt, E.3    Hertzberg, E.4    Neubauer, A.5    Grosveld, F.6    Galjart, N.7
  • 14
    • 0029913484 scopus 로고    scopus 로고
    • Molecular characterization of the 50-kD-subunit of dynactin reveals function for the complex in chromosome alignment and spindle orientation during mitosis
    • Echeverri,C.J., Paschal,B.M., Vaughan,K.T. and Vallee,R.B. (1996) Molecular characterization of the 50-kD-subunit of dynactin reveals function for the complex in chromosome alignment and spindle orientation during mitosis. J. Cell Biol., 132, 617-633.
    • (1996) J. Cell Biol. , vol.132 , pp. 617-633
    • Echeverri, C.J.1    Paschal, B.M.2    Vaughan, K.T.3    Vallee, R.B.4
  • 15
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan,G.I., Lewis,G.K., Ramsay,G. and Bishop,J.M. (1985) Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol., 5, 3610-3616.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 16
    • 0031444202 scopus 로고    scopus 로고
    • An extended microtubule-binding structure within the dynein motor domain
    • Gee,M.A., Heuser,J.E. and Vallee,R.B. (1997) An extended microtubule-binding structure within the dynein motor domain. Nature, 390, 636-639.
    • (1997) Nature , vol.390 , pp. 636-639
    • Gee, M.A.1    Heuser, J.E.2    Vallee, R.B.3
  • 18
    • 0022181709 scopus 로고
    • Expression and intracellular transport of microvillus membrane hydrolases in human intestinal epithelial cells
    • Hauri,H.-P., Sterchi,E.E., Bienz,D., Fransen,J.A. and Marxer,A. (1985) Expression and intracellular transport of microvillus membrane hydrolases in human intestinal epithelial cells. J. Cell Biol., 101, 838-851.
    • (1985) J. Cell Biol. , vol.101 , pp. 838-851
    • Hauri, H.-P.1    Sterchi, E.E.2    Bienz, D.3    Fransen, J.A.4    Marxer, A.5
  • 19
    • 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
  • 20
    • 0028170819 scopus 로고
    • Dyneins: Molecular structure and cellular function
    • Holzbaur,E.L. and Vallee,R.B. (1994) Dyneins: molecular structure and cellular function. Annu. Rev. Cell Biol., 10, 339-372.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 339-372
    • Holzbaur, E.L.1    Vallee, R.B.2
  • 21
    • 0029861916 scopus 로고    scopus 로고
    • Beta-tubulin binds Src homology 2 domains through a region different from the tyrosine-phosphorylated protein-recognizing site
    • Itoh,T., Miura,K., Miki,H. and Takenawa,T. (1996) Beta-tubulin binds Src homology 2 domains through a region different from the tyrosine-phosphorylated protein-recognizing site. J. Biol. Chem., 271, 27931-27935.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27931-27935
    • Itoh, T.1    Miura, K.2    Miki, H.3    Takenawa, T.4
  • 22
    • 0016184723 scopus 로고
    • Purification and characterization of Na-K-ATPase. III. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulfate
    • Jorgensen,P.L. (1974) Purification and characterization of Na-K-ATPase. III. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulfate. Biochim. Biophys. Acta, 356, 36-52.
    • (1974) Biochim. Biophys. Acta , vol.356 , pp. 36-52
    • Jorgensen, P.L.1
  • 23
    • 0022399724 scopus 로고
    • Monoclonal antibody to Na,K-ATPase: Immunocytochemical localization along nephron segments
    • Kashgarian,M., Biemesderfer,D., Caplan,M. and Forbush,B. (1985) Monoclonal antibody to Na,K-ATPase: immunocytochemical localization along nephron segments. Kidney Int., 28, 899-913.
    • (1985) Kidney Int. , vol.28 , pp. 899-913
    • Kashgarian, M.1    Biemesderfer, D.2    Caplan, M.3    Forbush, B.4
  • 24
    • 0030877444 scopus 로고    scopus 로고
    • Identification of a microtubule-binding domain in a cytoplasmic dynein heavy chain
    • Koonce,M.P. (1997) Identification of a microtubule-binding domain in a cytoplasmic dynein heavy chain. J. Biol. Chem., 272, 19714-19718.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19714-19718
    • Koonce, M.P.1
  • 25
    • 0023403268 scopus 로고
    • Microtubules containing detyrosinated tubulin are less dynamic
    • Kreis,T.E. (1987) Microtubules containing detyrosinated tubulin are less dynamic. EMBO J., 6, 2597-2606.
    • (1987) EMBO J. , vol.6 , pp. 2597-2606
    • Kreis, T.E.1
  • 26
    • 0023693945 scopus 로고
    • Dynamic behavior of endoplasmic reticulum in living cells
    • Lee,C. and Chen,L.B. (1988) Dynamic behavior of endoplasmic reticulum in living cells. Cell, 54, 37-46.
    • (1988) Cell , vol.54 , pp. 37-46
    • Lee, C.1    Chen, L.B.2
  • 27
    • 0023905288 scopus 로고
    • The primary structure and heterogeneity of tau protein from mouse brain
    • Lee,G., Cowan,N. and Kirschner,M. (1988) The primary structure and heterogeneity of tau protein from mouse brain. Science, 239, 285-288.
    • (1988) Science , vol.239 , pp. 285-288
    • Lee, G.1    Cowan, N.2    Kirschner, M.3
  • 28
    • 0024268202 scopus 로고
    • Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein
    • Lewis,S.A., Wang,D.H. and Cowan,N.J. (1988) Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein. Science, 242, 936-939.
    • (1988) Science , vol.242 , pp. 936-939
    • Lewis, S.A.1    Wang, D.H.2    Cowan, N.J.3
  • 29
    • 0027244942 scopus 로고
    • Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa
    • Linstedt,A.D. and Hauri,H.-P. (1993) Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa. Mol. Biol. Cell, 4, 679-693.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 679-693
    • Linstedt, A.D.1    Hauri, H.-P.2
  • 30
    • 3643104885 scopus 로고
    • Cell-cycle dependent phosphorylation of giantin, a cytoskeletal-like Golgi membrane protein
    • Linstedt,A.D. and Hauri,H.-P. (1994) Cell-cycle dependent phosphorylation of giantin, a cytoskeletal-like Golgi membrane protein. Mol. Biol. Cell, 5, 240a.
    • (1994) Mol. Biol. Cell , vol.5
    • Linstedt, A.D.1    Hauri, H.-P.2
  • 32
    • 0029149264 scopus 로고
    • Protein palmitoylation in membrane trafficking
    • Mundy,D.I. (1995) Protein palmitoylation in membrane trafficking. Biochem. Soc. Trans., 23, 572-576.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 572-576
    • Mundy, D.I.1
  • 33
    • 0026543668 scopus 로고
    • Mitosis and inhibition of intracellular transport stimulate palmitoylation of a 62-kD protein
    • Mundy,D.I. and Warren,G. (1992) Mitosis and inhibition of intracellular transport stimulate palmitoylation of a 62-kD protein. J. Cell Biol., 116, 135-146.
    • (1992) J. Cell Biol. , vol.116 , pp. 135-146
    • Mundy, D.I.1    Warren, G.2
  • 35
    • 0024801639 scopus 로고
    • The microtubule binding domain of microtubule-associated protein MAP1B contains a repeated sequence motif unrelated to that of MAP2 and tau
    • Noble,M, Lewis,S.A. and Cowan,N.J. (1989) The microtubule binding domain of microtubule-associated protein MAP1B contains a repeated sequence motif unrelated to that of MAP2 and tau. J. Cell Biol., 109, 3367-3376.
    • (1989) J. Cell Biol. , vol.109 , pp. 3367-3376
    • Noble, M.1    Lewis, S.A.2    Cowan, N.J.3
  • 36
    • 0026793891 scopus 로고
    • CLIP-170 links endocytic vesicles 10 microtubules
    • Pierre,P., Scheel,J., Rickard,J.E. and Kreis,T.E. (1992) CLIP-170 links endocytic vesicles 10 microtubules. Cell, 70, 887-900.
    • (1992) Cell , vol.70 , pp. 887-900
    • Pierre, P.1    Scheel, J.2    Rickard, J.E.3    Kreis, T.E.4
  • 37
    • 0028283041 scopus 로고
    • Molecular characterization of two functional domains of CLIP-170 in vivo
    • Pierre,P., Pepperkok,R. and Kreis,T.E. (1994) Molecular characterization of two functional domains of CLIP-170 in vivo. J. Cell Sci., 107, 1909-1920.
    • (1994) J. Cell Sci. , vol.107 , pp. 1909-1920
    • Pierre, P.1    Pepperkok, R.2    Kreis, T.E.3
  • 39
    • 0029929297 scopus 로고    scopus 로고
    • CLIPs for organelle-microtubule interactions
    • Rickard,J.E. and Kreis,T.E. (1996) CLIPs for organelle-microtubule interactions. Trends Cell Biol., 6, 178-183.
    • (1996) Trends Cell Biol. , vol.6 , pp. 178-183
    • Rickard, J.E.1    Kreis, T.E.2
  • 40
    • 0026001747 scopus 로고
    • Motor protein independent binding of endocytic carrier vesicles to microtubules in vitro
    • Scheel,J. and Kreis,T.E. (1991) Motor protein independent binding of endocytic carrier vesicles to microtubules in vitro. J. Biol. Chem., 266, 18141-18148.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18141-18148
    • Scheel, J.1    Kreis, T.E.2
  • 41
    • 0030903317 scopus 로고    scopus 로고
    • Retroactive motors
    • Schnapp,B.J. (1997) Retroactive motors. Neuron, 18, 523-526.
    • (1997) Neuron , vol.18 , pp. 523-526
    • Schnapp, B.J.1
  • 42
    • 0344649735 scopus 로고    scopus 로고
    • Interactions between microtubules and intracellular membranes: The role of microtubule-based motors and accessory proteins
    • Schroer,T.A. and Gill,S.R. (1996) Interactions between microtubules and intracellular membranes: the role of microtubule-based motors and accessory proteins. Curr. Top. Membr., 43, 27-52.
    • (1996) Curr. Top. Membr. , vol.43 , pp. 27-52
    • Schroer, T.A.1    Gill, S.R.2
  • 43
    • 0028349810 scopus 로고
    • An N-terminal double-arginine motif maintains type II membrane proteins in the endoplasmic reticulum
    • Schutze,M.-P., Peterson,P.A. and Jackson,M.R. (1994) An N-terminal double-arginine motif maintains type II membrane proteins in the endoplasmic reticulum, EMBO J., 13, 1696-1705
    • (1994) EMBO J. , vol.13 , pp. 1696-1705
    • Schutze, M.-P.1    Peterson, P.A.2    Jackson, M.R.3
  • 44
    • 0025760015 scopus 로고
    • The isolated ER-Golgi intermediate compartment exhibits properties that are different from ER and cis-Golgi
    • Schweizer,A., Matter,K., Ketcham,C.M. and Hauri,H.-P. (1991) The isolated ER-Golgi intermediate compartment exhibits properties that are different from ER and cis-Golgi. J. Cell Biol., 113, 45-54.
    • (1991) J. Cell Biol. , vol.113 , pp. 45-54
    • Schweizer, A.1    Matter, K.2    Ketcham, C.M.3    Hauri, H.-P.4
  • 45
    • 0027284699 scopus 로고
    • Characterization of a novel 63 kDa membrane protein. Implications for the organization of the ER-to-Golgi pathway
    • Schweizer,A., Ericsson,M., Bächi,T., Griffiths,G. and Hauri,H.-P. (1993a) Characterization of a novel 63 kDa membrane protein. Implications for the organization of the ER-to-Golgi pathway. J. Cell Sci., 104, 671-683.
    • (1993) J. Cell Sci. , vol.104 , pp. 671-683
    • Schweizer, A.1    Ericsson, M.2    Bächi, T.3    Griffiths, G.4    Hauri, H.-P.5
  • 46
    • 0027238044 scopus 로고
    • A reversibly palmitoylated resident protein (p63) of an ER-Golgi intermediate compartment is related to a circulatory shock resuscitation protein
    • Schweizer,A., Rohrer,J., Jeno,P., DeMaio,A., Buchman,T.G. and Hauri,H.P. (1993b) A reversibly palmitoylated resident protein (p63) of an ER-Golgi intermediate compartment is related to a circulatory shock resuscitation protein. J. Cell Sci., 104, 685-694.
    • (1993) J. Cell Sci. , vol.104 , pp. 685-694
    • Schweizer, A.1    Rohrer, J.2    Jeno, P.3    DeMaio, A.4    Buchman, T.G.5    Hauri, H.P.6
  • 47
    • 0028228060 scopus 로고
    • Retention of p63 in an ER-Golgi intermediate compartment depends on the presence of all three of its domains and on its ability to form oligomers
    • Schweizer,A., Rohrer,J., Hauri,H.-P. and Kornfeld,S. (1994) Retention of p63 in an ER-Golgi intermediate compartment depends on the presence of all three of its domains and on its ability to form oligomers. J. Cell Biol., 126, 25-39.
    • (1994) J. Cell Biol. , vol.126 , pp. 25-39
    • Schweizer, A.1    Rohrer, J.2    Hauri, H.-P.3    Kornfeld, S.4
  • 49
    • 0023025842 scopus 로고
    • Microtubules and the endoplasmic reticulum are highly interdependent structures
    • Terasaki,M., Chen, L.B. and Fujiwara,K. (1986) Microtubules and the endoplasmic reticulum are highly interdependent structures. J. Cell Biol., 103, 1557-1568.
    • (1986) J. Cell Biol. , vol.103 , pp. 1557-1568
    • Terasaki, M.1    Chen, L.B.2    Fujiwara, K.3
  • 50
    • 0022412716 scopus 로고
    • Microtubules and the organization of the Golgi complex
    • Thyberg,J. and 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
  • 51
    • 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
  • 52
    • 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
  • 53
    • 0023016138 scopus 로고
    • Purification of brain microtubules and microtubule-associated protein 1 using taxol
    • VaHee,R.B. (1986) Purification of brain microtubules and microtubule-associated protein 1 using taxol. Methods Enzymol., 134, 104-115.
    • (1986) Methods Enzymol. , vol.134 , pp. 104-115
    • VaHee, R.B.1
  • 54
    • 0029932027 scopus 로고    scopus 로고
    • Targeting of motor proteins
    • Vallee,R.B. and Sheetz,M.P. (1996) Targeting of motor proteins. Science, 271, 1539-1544.
    • (1996) Science , vol.271 , pp. 1539-1544
    • Vallee, R.B.1    Sheetz, M.P.2
  • 55
    • 0027267694 scopus 로고
    • Cytoplasmic microtubule-associated motors
    • Walker,R.A. and Sheetz,M.P. (1993) Cytoplasmic microtubule-associated motors. Annu. Rev. Biochem., 62, 429-451.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 429-451
    • Walker, R.A.1    Sheetz, M.P.2
  • 56
    • 0030728492 scopus 로고    scopus 로고
    • Stu2p: A microtubule-binding protein that is an essential component of the yeast spindle pole body
    • Wang,P.J. and Huffaker,T.C. (1997) Stu2p: a microtubule-binding protein that is an essential component of the yeast spindle pole body. J. Cell Biol., 139, 1271-1280.
    • (1997) J. Cell Biol. , vol.139 , pp. 1271-1280
    • Wang, P.J.1    Huffaker, T.C.2
  • 57
    • 0029128472 scopus 로고
    • Membrane/microtubule tip attachment complexes (TACs) allow the assembly dynamics of plus ends to push and pull membranes into tubulovesicular networks in interphase Xenopus egg extracts
    • Waterman-Storer,C.M., Gregory,J., Parsons,S.F. and Salmon,E.D. (1995) Membrane/microtubule tip attachment complexes (TACs) allow the assembly dynamics of plus ends to push and pull membranes into tubulovesicular networks in interphase Xenopus egg extracts. J. Cell Biol., 130, 1161-1169.
    • (1995) J. Cell Biol. , vol.130 , pp. 1161-1169
    • Waterman-Storer, C.M.1    Gregory, J.2    Parsons, S.F.3    Salmon, E.D.4
  • 58
    • 0016344063 scopus 로고
    • Properties of the depolymerization products of microtubules from mammalian brain
    • Weingarten,M.D., Suter,M.M., Littman,D.R. and Kirschner,M.W. (1974) Properties of the depolymerization products of microtubules from mammalian brain. Biochemistry, 13, 5529-5537.
    • (1974) Biochemistry , vol.13 , pp. 5529-5537
    • Weingarten, M.D.1    Suter, M.M.2    Littman, D.R.3    Kirschner, M.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.