메뉴 건너뛰기




Volumn 147, Issue 2, 1999, Pages 307-319

Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the Arp1 minifilament pointed end

Author keywords

Dynein; Ultrastructure

Indexed keywords

ACTIN; DYNACTIN; DYNEIN ADENOSINE TRIPHOSPHATASE; GAG PROTEIN; POTASSIUM IODIDE; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; STRUCTURAL PROTEIN; UNCLASSIFIED DRUG;

EID: 0032728976     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.147.2.307     Document Type: Article
Times cited : (133)

References (75)
  • 1
    • 0030156513 scopus 로고    scopus 로고
    • Motor proteins: A dynamic duo
    • Allan, V. 1996. Motor proteins: a dynamic duo. Curr. Biol. 6:630-633.
    • (1996) Curr. Biol. , vol.6 , pp. 630-633
    • Allan, V.1
  • 2
    • 0031603961 scopus 로고    scopus 로고
    • Purification of dynein and dynactin from brain tissue
    • Bingham, J.B., S.J. King, and T.A. Schroer. 1998. Purification of dynein and dynactin from brain tissue. Methods Enzymol. 298:171-184.
    • (1998) Methods Enzymol. , vol.298 , pp. 171-184
    • Bingham, J.B.1    King, S.J.2    Schroer, T.A.3
  • 3
    • 0033602146 scopus 로고    scopus 로고
    • Self-regulated polymerization of the actin-related protein, Arp1
    • Bingham, J.B., and T.A. Schroer. 1999. Self-regulated polymerization of the actin-related protein, Arp1. Curr. Biol. 9:223-226.
    • (1999) Curr. Biol. , vol.9 , pp. 223-226
    • Bingham, J.B.1    Schroer, T.A.2
  • 5
    • 0023944514 scopus 로고
    • Native structure and physical properties of bovine brain kinesin and indentification of the ATP-binding subunit polypeptide
    • Bloom, G.S., M.C. Wagner, K.K. Pfister, and S.T. Brady. 1988. Native structure and physical properties of bovine brain kinesin and indentification 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
  • 6
    • 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., C.J. Echeverri, T. Nilsson, and R.B. Vallee. 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
  • 7
    • 0032560079 scopus 로고    scopus 로고
    • Dynein and dynactin are localized to astral microtubules and at cortical sites in mitolic epithelial cells
    • Busson, S., D. Dujardin, A. Moreau, J. Dompierre, and J.R. De Mey. 1998. Dynein and dynactin are localized to astral microtubules and at cortical sites in mitolic epithelial cells. Curr. Biol. 8:541-544.
    • (1998) Curr. Biol. , vol.8 , pp. 541-544
    • Busson, S.1    Dujardin, D.2    Moreau, A.3    Dompierre, J.4    De Mey, J.R.5
  • 8
    • 0024421755 scopus 로고
    • Effects of capz. An actin capping protein of muscle, on the polymerization of actin
    • Caldwell, J.E., S.G. Heiss, V. Mermall, and J.A. Cooper. 1989. Effects of CapZ. an actin capping protein of muscle, on the polymerization of actin. Biochemistry. 28:8506-8514.
    • (1989) Biochemistry , vol.28 , pp. 8506-8514
    • Caldwell, J.E.1    Heiss, S.G.2    Mermall, V.3    Cooper, J.A.4
  • 9
    • 0030750203 scopus 로고    scopus 로고
    • Microtubules orient the mitotic spindle in yeast through dynein-dependent interactions with the cell cortex
    • Carminati, J.L., and T. Stearns. 1997. Microtubules orient the mitotic spindle in yeast through dynein-dependent interactions with the cell cortex. J. Cell Biol. 138:629-641.
    • (1997) J. Cell Biol. , vol.138 , pp. 629-641
    • Carminati, J.L.1    Stearns, T.2
  • 10
    • 0021007546 scopus 로고
    • Peptide mapping in one dimension by limited proteolysis of sodium dodecyl sulfate-solubilized proteins
    • Cleveland, D.W. 1983. Peptide mapping in one dimension by limited proteolysis of sodium dodecyl sulfate-solubilized proteins. Methods Enzymol. 96: 222-229.
    • (1983) Methods Enzymol. , vol.96 , pp. 222-229
    • Cleveland, D.W.1
  • 11
    • 0031809137 scopus 로고    scopus 로고
    • Focusing on spindle poles
    • Compton, D.A. 1998. Focusing on spindle poles. J. Cell Sci. 111:1477-1481.
    • (1998) J. Cell Sci. , vol.111 , pp. 1477-1481
    • Compton, D.A.1
  • 12
    • 0021259403 scopus 로고
    • Acanthamoeba castellanii capping protein: Properties, mechanism of action, immunologic cross-reactivity, and localization
    • Cooper, J.A., J.D. Blum, and T.D. Pollard. 1984. Acanthamoeba castellanii capping protein: properties, mechanism of action, immunologic cross-reactivity, and localization. J. Cell Biol. 99:217-225.
    • (1984) J. Cell Biol. , vol.99 , pp. 217-225
    • Cooper, J.A.1    Blum, J.D.2    Pollard, T.D.3
  • 13
    • 0029913484 scopus 로고    scopus 로고
    • Molecular characterization of 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis
    • Echeverri, C.J., B.M. Paschal, K.T. Vaughan, and R.B. Vallee. 1996. Molecular characterization of 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization 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
  • 14
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-spe-cific oligonucleotide primer
    • Frohman, M.A., M.K. Dush, and G.R. Martin. 1988. Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-spe-cific oligonucleotide primer. Proc. Nat. Acad. Sci. USA. 85:8998-9002.
    • (1988) Proc. Nat. Acad. Sci. USA , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 15
  • 16
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein
    • Gill, S. R., T.A. Schroer, I. Szilak, E.R. Steuer, M.P. Sheetz., and D.W. Cleveland. 1991. Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J. Cell Biol. 115:1639-1650.
    • (1991) J. Cell Biol. , vol.115 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steuer, E.R.4    Sheetz, M.P.5    Cleveland, D.W.6
  • 17
    • 0342265157 scopus 로고    scopus 로고
    • Cytoplasmic dynein is required for distinct aspects of MTOC positioning, including centrosome separation, in the one cell stage C elegant embryo
    • Gönczy, P., S. Pilcher, M. Kirkham, and A.A. Hyman. 1999. Cytoplasmic dynein is required for distinct aspects of MTOC positioning, including centrosome separation, in the one cell stage C elegant embryo. J. Cell Biol. 147: 135-150.
    • (1999) J. Cell Biol. , vol.147 , pp. 135-150
    • Gönczy, P.1    Pilcher, S.2    Kirkham, M.3    Hyman, A.A.4
  • 18
    • 0032489870 scopus 로고    scopus 로고
    • Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein
    • Harada, A., Y. Takei, Y. Kanai, Y. Tanaka, S. Nonaka, and N. Hirokawa. 1998. Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein. J. Cell Biol. 141:51-59.
    • (1998) J. Cell Biol. , vol.141 , pp. 51-59
    • Harada, A.1    Takei, Y.2    Kanai, Y.3    Tanaka, Y.4    Nonaka, S.5    Hirokawa, N.6
  • 19
    • 0029836330 scopus 로고    scopus 로고
    • Self-organization of microtubules into bipolar spindles around artificial chromosomes in Xenopus egg extracts
    • Heald, R., R. Tournebize, T. Blank, R. Sandaltzopoulos, P. Becker, A. Hyman, and E. Karsenti. 1996. Self-organization of microtubules into bipolar spindles around artificial chromosomes in Xenopus egg extracts. Nature. 382: 420-425.
    • (1996) Nature , vol.382 , pp. 420-425
    • Heald, R.1    Tournebize, R.2    Blank, T.3    Sandaltzopoulos, R.4    Becker, P.5    Hyman, A.6    Karsenti, E.7
  • 20
    • 0021095633 scopus 로고
    • Procedure for freeze-drying molecules adsorbed to mica flakes
    • Heuser, J.E. 1983. Procedure for freeze-drying molecules adsorbed to mica flakes. J. Mol. Biol. 169:155-195.
    • (1983) J. Mol. Biol. , vol.169 , pp. 155-195
    • Heuser, J.E.1
  • 21
    • 0345647172 scopus 로고    scopus 로고
    • Centractin (actin-related protein 1) binds directly to spectrin
    • Abstr.
    • Holleran, E.A., and E.L.F. Holzbaur. 1998. Centractin (actin-related protein 1) binds directly to spectrin. Mol. Biol. Cell. 9:274a. ( Abstr.)
    • (1998) Mol. Biol. Cell. , vol.9
    • Holleran, E.A.1    Holzbaur, E.L.F.2
  • 22
    • 0031947483 scopus 로고    scopus 로고
    • The role of the dynactin complex in intracellular motility
    • Holleran, E.A., S. Karki, and E.L. Holzbaur. 1998. The role of the dynactin complex in intracellular motility. Int. Rev. Cytol. 182:69-109.
    • (1998) Int. Rev. Cytol. , vol.182 , pp. 69-109
    • Holleran, E.A.1    Karki, S.2    Holzbaur, E.L.3
  • 23
    • 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
  • 24
  • 25
    • 0028170819 scopus 로고
    • Dyneins: Molecular structure and cellular function
    • Holzbaur, E.L., and R.B. Vallee. 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
  • 27
    • 0028944687 scopus 로고
    • The actin fold
    • Kabsch, W., and K.C. Holmes. 1995. The actin fold. FASEB J. 9:167-174.
    • (1995) FASEB J. , vol.9 , pp. 167-174
    • Kabsch, W.1    Holmes, K.C.2
  • 29
    • 0028806377 scopus 로고
    • Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex
    • Karki, S., and E.L.F. Holzbaur. 1995. Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex. J. Biol. Chem. 270:28806-28811.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28806-28811
    • Karki, S.1    Holzbaur, E.L.F.2
  • 30
    • 0032563618 scopus 로고    scopus 로고
    • Characterization of the p22 subunit of dynactin reveals the localization of cytoplasmic dynein and dynactin to the midbody of dividing cells
    • Karki, S., B. LaMonte, and E.L.F. Holzbaur. 1998. Characterization of the p22 subunit of dynactin reveals the localization of cytoplasmic dynein and dynactin to the midbody of dividing cells. J. Cell Biol. 142:1023-1034.
    • (1998) J. Cell Biol. , vol.142 , pp. 1023-1034
    • Karki, S.1    LaMonte, B.2    Holzbaur, E.L.F.3
  • 31
    • 0026630055 scopus 로고
    • Cytoplasmic dynein is a vesicle protein
    • Lacey, M.L., and L.T. Haimo. 1992. Cytoplasmic dynein is a vesicle protein. J. Biol. Chem. 267:4793-4798.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4793-4798
    • Lacey, M.L.1    Haimo, L.T.2
  • 32
    • 0028238805 scopus 로고
    • Cytoplasmic dynein binds to phospholipid vesicles
    • Lacey, M.L., and L.T. Haimo. 1994. Cytoplasmic dynein binds to phospholipid vesicles. Cell Motil. Cytoskelet. 28:205-212.
    • (1994) Cell Motil. Cytoskelet. , vol.28 , pp. 205-212
    • Lacey, M.L.1    Haimo, L.T.2
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0023803882 scopus 로고
    • Two monoclonal antibodies to actin: One muscle selective and one generally reactive
    • Lessard, J.L. 1988. Two monoclonal antibodies to actin: one muscle selective and one generally reactive. Cell Motil. Cytoskelet. 10:349-362.
    • (1988) Cell Motil. Cytoskelet. , vol.10 , pp. 349-362
    • Lessard, J.L.1
  • 35
    • 0030298137 scopus 로고    scopus 로고
    • A complex of NuMA and cytoplasmic dynein is essential for mitotic spindle assembly
    • Merdes, A., K. Ramyar, J.D. Vechio, and D.W. Cleveland. 1996. A complex of NuMA and cytoplasmic dynein is essential for mitotic spindle assembly. Cell. 87:447-458.
    • (1996) Cell , vol.87 , pp. 447-458
    • Merdes, A.1    Ramyar, K.2    Vechio, J.D.3    Cleveland, D.W.4
  • 36
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins, R.D., J.A. Heuser, and T.D. Pollard. 1998. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA. 95: 6181-6186.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 37
    • 0031051993 scopus 로고    scopus 로고
    • Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba
    • Mullins, R.D.,. W.F. Stafford, and T.D. Pollard. 1997. Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba. J. Cell Biol. 136:331-343.
    • (1997) J. Cell Biol. , vol.136 , pp. 331-343
    • Mullins, R.D.1    Stafford, W.F.2    Pollard, T.D.3
  • 40
    • 0033582659 scopus 로고    scopus 로고
    • CLIP-170 highlights growing microtubule ends in vivo
    • Perez, F., G.S. Diamantopoulos, R. Stalder, and T.E. Kreis. 1999. CLIP-170 highlights growing microtubule ends in vivo. Cell. 96:517-527.
    • (1999) Cell , vol.96 , pp. 517-527
    • Perez, F.1    Diamantopoulos, G.S.2    Stalder, R.3    Kreis, T.E.4
  • 42
    • 0026793891 scopus 로고
    • CLIP-170 links endocytic vesicles to microtubules
    • Pierre, P., J. Scheel, J. Rickard, and T.E. Kreis. 1992. CLIP-170 links endocytic vesicles to microtubules. Cell. 70:887-900.
    • (1992) Cell , vol.70 , pp. 887-900
    • Pierre, P.1    Scheel, J.2    Rickard, J.3    Kreis, T.E.4
  • 43
    • 0028067033 scopus 로고
    • Cytoplasmic dynein and actin-related protein Arp1 are required for normal nuclear distribution in filamentous fungi
    • Plamann, M., P.F. Minke, J.H. Tinsley, and K.S. Bruno. 1994. Cytoplasmic dynein and actin-related protein Arp1 are required for normal nuclear distribution in filamentous fungi. J. Cell Biol. 127:139-149.
    • (1994) J. Cell Biol. , vol.127 , pp. 139-149
    • Plamann, M.1    Minke, P.F.2    Tinsley, J.H.3    Bruno, K.S.4
  • 44
    • 0030754347 scopus 로고    scopus 로고
    • Who's who among the Saccharomyces cerevisiae actin-related proteins? A classification and nomenclature proposal for a large family
    • Poch, O., and B. Winsor. 1997. Who's who among the Saccharomyces cerevisiae actin-related proteins? A classification and nomenclature proposal for a large family. Yeast. 13:1053-1058.
    • (1997) Yeast , vol.13 , pp. 1053-1058
    • Poch, O.1    Winsor, B.2
  • 47
    • 0033538842 scopus 로고    scopus 로고
    • Cytoplasmic dynein is required for the nuclear attachment and migration of centrosome during mitosis in Drosophila
    • Robinson, J.T., E.J. Wojcik, M.A. Sander, M. McGrail, and T.S. Hays. 1999. Cytoplasmic dynein is required for the nuclear attachment and migration of centrosome during mitosis in Drosophila. J. Cell Biol. 146:597-608.
    • (1999) J. Cell Biol. , vol.146 , pp. 597-608
    • Robinson, J.T.1    Wojcik, E.J.2    Sander, M.A.3    McGrail, M.4    Hays, T.S.5
  • 49
    • 0028304474 scopus 로고
    • Ultrastructural analysis of the dynaclin complex: An actin-related protein is a component of a filament that resembles f-actin
    • Schafer, D.A., S.R. Gill, J.A. Cooper, J.E. Heuser, and T.A. Schroer. 1994a. Ultrastructural analysis of the dynaclin complex: An actin-related protein is a component of a filament that resembles f-actin. J. Cell Biol. 126:403-412.
    • (1994) J. Cell Biol. , vol.126 , pp. 403-412
    • Schafer, D.A.1    Gill, S.R.2    Cooper, J.A.3    Heuser, J.E.4    Schroer, T.A.5
  • 50
    • 0027959864 scopus 로고
    • Differential localization and sequence analysis of capping protein β-suhunit isoforms of vertebrates
    • Schafer, D.A., Y.O. Korshunova, T.A. Schroer, and J.A. Cooper. 1994b. Differential localization and sequence analysis of capping protein β-suhunit isoforms of vertebrates. J. Cell Biol. 127:453-465.
    • (1994) J. Cell Biol. , vol.127 , pp. 453-465
    • Schafer, D.A.1    Korshunova, Y.O.2    Schroer, T.A.3    Cooper, J.A.4
  • 52
    • 0001147917 scopus 로고    scopus 로고
    • Structure and function of dynactin. Semin
    • Schroer, T.A. 1996. Structure and function of dynactin. Semin. Cell Biol. 7:321-328.
    • (1996) Cell Biol. , vol.7 , pp. 321-328
    • Schroer, T.A.1
  • 53
    • 0029891913 scopus 로고    scopus 로고
    • Actin-related protein 1 and cytoplasmic dynein-based motility - What's the connection?
    • Schroer, T.A., J.B. Bingham, and S.R. Gill. 1996. Actin-related protein 1 and cytoplasmic dynein-based motility - what's the connection? Trends Cell Biol. 6:212-215.
    • (1996) Trends Cell Biol. , vol.6 , pp. 212-215
    • Schroer, T.A.1    Bingham, J.B.2    Gill, S.R.3
  • 55
    • 0025789647 scopus 로고
    • Two activators of microtubule-based vesicle transport
    • Schroer, T.A., and M.P. Sheetz. 1991. Two activators of microtubule-based vesicle transport. J. Cell Biol. 115:1309-1318.
    • (1991) J. Cell Biol. , vol.115 , pp. 1309-1318
    • Schroer, T.A.1    Sheetz, M.P.2
  • 56
    • 0032497694 scopus 로고    scopus 로고
    • The dynactin complex is required for cleavage plane specification in early Caenorhabditis elegans embryos
    • Skop, A., and J. While. 1998. The dynactin complex is required for cleavage plane specification in early Caenorhabditis elegans embryos. Curr. Biol. 8:1110-1116.
    • (1998) Curr. Biol. , vol.8 , pp. 1110-1116
    • Skop, A.1    While, J.2
  • 57
    • 0030896925 scopus 로고    scopus 로고
    • Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus
    • Sodeik, B., M.W. Ebersold, and A. Helenius. 1997. Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J. Cell Biol. 136:1007-1021.
    • (1997) J. Cell Biol. , vol.136 , pp. 1007-1021
    • Sodeik, B.1    Ebersold, M.W.2    Helenius, A.3
  • 58
    • 0031852650 scopus 로고    scopus 로고
    • ZW10 helps recruit dynactin and dynein to the kinetochore
    • Starr, D.A., B.C. Williams, T.S. Hays, and M.L. Goldberg. 1998. ZW10 helps recruit dynactin and dynein to the kinetochore. J. Cell Biol. 142:763-774.
    • (1998) J. Cell Biol. , vol.142 , pp. 763-774
    • Starr, D.A.1    Williams, B.C.2    Hays, T.S.3    Goldberg, M.L.4
  • 59
    • 0030803260 scopus 로고    scopus 로고
    • The involvement of the intermediate chain of cytoplasmic dynein in binding the motor complex to membranous organelles of Xenopus oocytes
    • Steffen, W., S. Karki, K.T. Vaughan, R.B. Vallee, E.L. Holzbaur, D.G. Weiss. and S.A. Kuznetsov. 1997. The involvement of the intermediate chain of cytoplasmic dynein in binding the motor complex to membranous organelles of Xenopus oocytes. Mol. Biol. Cell. 8:2077-2088.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 2077-2088
    • Steffen, W.1    Karki, S.2    Vaughan, K.T.3    Vallee, R.B.4    Holzbaur, E.L.5    Weiss, D.G.6    Kuznetsov, S.A.7
  • 60
    • 0033593811 scopus 로고    scopus 로고
    • Microtubule-dependent plus-and minus end-directed motilities are competing processes for nuclear targeting of adenovirus
    • Suomalainen, M., M.Y. Nakano, S. Keller. K. Boucke, R.P. Stidwill, and U.F. Greber. 1999. Microtubule-dependent plus-and minus end-directed motilities are competing processes for nuclear targeting of adenovirus. J. Cell Biol. 144:657-672.
    • (1999) J. Cell Biol. , vol.144 , pp. 657-672
    • Suomalainen, M.1    Nakano, M.Y.2    Keller, S.3    Boucke, K.4    Stidwill, R.P.5    Greber, U.F.6
  • 61
    • 0345378408 scopus 로고
    • The reversible depolymerization of actin by potassium iodide
    • Szent-Gyorgi, A. 1951. The reversible depolymerization of actin by potassium iodide. Arch. Biochem. Biophys. 31:97-103.
    • (1951) Arch. Biochem. Biophys. , vol.31 , pp. 97-103
    • Szent-Gyorgi, A.1
  • 62
    • 0033603239 scopus 로고    scopus 로고
    • Rhodopsin's carhoxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1
    • Tai, A.W., J.-Z. Chuang, C. Bode, U. Wolfrum, and C.-H. Sung. 1999. Rhodopsin's carhoxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1. Cell. 97:877-887.
    • (1999) Cell , vol.97 , pp. 877-887
    • Tai, A.W.1    Chuang, J.-Z.2    Bode, C.3    Wolfrum, U.4    Sung, C.-H.5
  • 63
    • 0029658940 scopus 로고    scopus 로고
    • P150Glued, the largest subunit of the dynactin complex, is nonessential in Neurospora hut required for nuclear distribution
    • Tinsley, J.H., P.F. Minke, K.S. Bruno, and M. Plamann. 1996. p150Glued, the largest subunit of the dynactin complex, is nonessential in Neurospora hut required for nuclear distribution. Mol. Biol. Cell 7:731-742.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 731-742
    • Tinsley, J.H.1    Minke, P.F.2    Bruno, K.S.3    Plamann, M.4
  • 64
    • 0032497796 scopus 로고    scopus 로고
    • The genomic structure of DCTN1, a candidate gene for limb-girdle muscular dystrophy (LGMD2B)
    • Tokito, M.K., and E.L. Holzbaur. 1998. The genomic structure of DCTN1, a candidate gene for limb-girdle muscular dystrophy (LGMD2B). Biochim. Biophys. Acta. 1442:432-436.
    • (1998) Biochim. Biophys. Acta. , vol.1442 , pp. 432-436
    • Tokito, M.K.1    Holzbaur, E.L.2
  • 65
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Grodon. 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    Grodon, J.3
  • 66
    • 0027420391 scopus 로고
    • Cytoplasmic dynein plays a role in mammalian mitotic spindle formation
    • Vaisberg, E.A., M.P. Koonce, and J.R. McIntosh. 1993. Cytoplasmic dynein plays a role in mammalian mitotic spindle formation. J. Cell Biol. 123:849-858.
    • (1993) J. Cell Biol. , vol.123 , pp. 849-858
    • Vaisberg, E.A.1    Koonce, M.P.2    McIntosh, J.R.3
  • 68
    • 0029932027 scopus 로고    scopus 로고
    • Targeting of motor proteins
    • Vallee, R.B., and M.P. Sheetz. 1996. Targeting of motor proteins. Science. 271: 1539-1544.
    • (1996) Science , vol.271 , pp. 1539-1544
    • Vallee, R.B.1    Sheetz, M.P.2
  • 69
    • 0029550849 scopus 로고    scopus 로고
    • Targeting of cytoplasmic dynein to membranous organelles and kinetochores via dynactin
    • Vallee, R.B., K.T. Vaughan, and C.J. Echeverri. 1996. Targeting of cytoplasmic dynein to membranous organelles and kinetochores via dynactin. Cold Spring Harb. Symp. Qiunt. Biol. 60:803-811.
    • (1996) Cold Spring Harb. Symp. Qiunt. Biol. , vol.60 , pp. 803-811
    • Vallee, R.B.1    Vaughan, K.T.2    Echeverri, C.J.3
  • 70
    • 0033051741 scopus 로고    scopus 로고
    • Colocalization of cytoplasmic dynein with dynactin and CLIP-170 at microtubule distal ends
    • Vaughan, K.T., S.H. Tynan, N.E. Faulkner, C.J. Echeverri, and R.B. Vallee. 1999. Colocalization of cytoplasmic dynein with dynactin and CLIP-170 at microtubule distal ends. J. Cell Sci. 112:1437-1447.
    • (1999) J. Cell Sci. , vol.112 , pp. 1437-1447
    • Vaughan, K.T.1    Tynan, S.H.2    Faulkner, N.E.3    Echeverri, C.J.4    Vallee, R.B.5
  • 72
    • 0026071835 scopus 로고
    • Taxol-induced microtubule asters in mitotic extracts of Xenopus eggs: Requirement for phosphorylated factors and cytoplasmic dynein
    • Verde, F., J.-M. Berrez, C. Antony, and E. Karsenti. 1991. Taxol-induced microtubule asters in mitotic extracts of Xenopus eggs: requirement for phosphorylated factors and cytoplasmic dynein. J. Cell Biol. 112:1177-1187.
    • (1991) J. Cell Biol. , vol.112 , pp. 1177-1187
    • Verde, F.1    Berrez, J.-M.2    Antony, C.3    Karsenti, E.4
  • 73
    • 0030943888 scopus 로고    scopus 로고
    • A gene required for nuclear migration in Neurospara crassa codes for a protein with cysteine-rich, LIM/RING-like domains
    • Vierula, P.J., and J.M. Mais. 1997. A gene required for nuclear migration in Neurospara crassa codes for a protein with cysteine-rich, LIM/RING-like domains. Mol. Microbiol. 24:331-340.
    • (1997) Mol. Microbiol. , vol.24 , pp. 331-340
    • Vierula, P.J.1    Mais, J.M.2
  • 74
    • 0028986631 scopus 로고
    • The p150 component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1)
    • Waterman-Storer, CM., S. Karki, and E.L. Holzbaur. 1995. The p150 component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1). Proc. Natl. Acad. Sci. USA. 92:1634-1638.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1634-1638
    • Waterman-Storer, C.M.1    Karki, S.2    Holzbaur, E.L.3
  • 75
    • 0032622374 scopus 로고    scopus 로고
    • Recombinant p50/dynamitin as a tool to examine the role of dynactin in intracellutar processes
    • Academic Press. Inc., San Diego. CA
    • Wittman, T., and A. Hyman. 1999. Recombinant p50/dynamitin as a tool to examine the role of dynactin in intracellutar processes. In Methods in Cell Biol. Academic Press. Inc., San Diego. CA.
    • (1999) Methods in Cell Biol.
    • Wittman, T.1    Hyman, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.