메뉴 건너뛰기




Volumn 12, Issue 4, 2000, Pages 503-508

Connecting vesicle transport to the cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE; KINESIN; MYOSIN; RECEPTOR;

EID: 0033936009     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(00)00123-X     Document Type: Review
Times cited : (114)

References (48)
  • 1
    • 0032559708 scopus 로고    scopus 로고
    • Cruising along microtubule highways: How membranes move through the secretory pathway
    • Bloom G.S., Goldstein L.S.B. Cruising along microtubule highways: how membranes move through the secretory pathway. J Cell Biol. 140:1998;1277-1280.
    • (1998) J Cell Biol , vol.140 , pp. 1277-1280
    • Bloom, G.S.1    Goldstein, L.S.B.2
  • 2
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa N. Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science. 279:1998;519-526.
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 4
    • 0034614647 scopus 로고    scopus 로고
    • The road taken: Past and future foundations of membrane traffic
    • Mellman I., Warren G. The road taken: past and future foundations of membrane traffic. Cell. 100:2000;99-112.
    • (2000) Cell , vol.100 , pp. 99-112
    • Mellman, I.1    Warren, G.2
  • 5
    • 0033588989 scopus 로고    scopus 로고
    • Defective kinesin heavy chain behavior in mouse kinesin light chain mutants
    • Rahman A., Kamal A., Roberts E.A., Goldstein L.S.B. Defective kinesin heavy chain behavior in mouse kinesin light chain mutants. J Cell Biol. 146:1999;1277-1288.
    • (1999) J Cell Biol , vol.146 , pp. 1277-1288
    • Rahman, A.1    Kamal, A.2    Roberts, E.A.3    Goldstein, L.S.B.4
  • 6
    • 0033794484 scopus 로고    scopus 로고
    • Kinesin and dynamin are required for post-Golgi transport of a plasma membrane protein
    • Microtubule motors are required for Golgi to plasma membrane transport of a GFP-tagged apical membrane protein, p75. Antibody inhibition experiments reveal that a kinesin-I motor may be involved in the process but the identity of the motor remains unknown.
    • Kreitzer G., Marmorstein A., Okamoto P., Vallee R., Rodriguez-Boulan E. Kinesin and dynamin are required for post-Golgi transport of a plasma membrane protein. Nat Cell Biol. 2:2000;125-127. Microtubule motors are required for Golgi to plasma membrane transport of a GFP-tagged apical membrane protein, p75. Antibody inhibition experiments reveal that a kinesin-I motor may be involved in the process but the identity of the motor remains unknown.
    • (2000) Nat Cell Biol , vol.2 , pp. 125-127
    • Kreitzer, G.1    Marmorstein, A.2    Okamoto, P.3    Vallee, R.4    Rodriguez-Boulan, E.5
  • 7
    • 0033080404 scopus 로고    scopus 로고
    • Role of microtubules in organization of the Golgi complex
    • Thyberg J., Moskalewski S. Role of microtubules in organization of the Golgi complex. Exp Cell Res. 246:1999;263-279.
    • (1999) Exp Cell Res , vol.246 , pp. 263-279
    • Thyberg, J.1    Moskalewski, S.2
  • 8
    • 0030747463 scopus 로고    scopus 로고
    • Microtubule-dependent transport of secretory vesicles visualized in real time with a GFP-tagged secretory protein
    • Wacker I., Kaether C., Kromer A., Migala A., Almers W., Gerdes H.-H. Microtubule-dependent transport of secretory vesicles visualized in real time with a GFP-tagged secretory protein. J Cell Sci. 110:1997;1453-1463.
    • (1997) J Cell Sci , vol.110 , pp. 1453-1463
    • Wacker, I.1    Kaether, C.2    Kromer, A.3    Migala, A.4    Almers, W.5    Gerdes, H.-H.6
  • 9
    • 0025029828 scopus 로고
    • Microtubule- And motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells
    • Bomsel M., Parton R., Kuznetsov S.A., Schroer T.A., Gruenberg J. Microtubule- and motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells. Cell. 62:1990;719-731.
    • (1990) Cell , vol.62 , pp. 719-731
    • Bomsel, M.1    Parton, R.2    Kuznetsov, S.A.3    Schroer, T.A.4    Gruenberg, J.5
  • 10
    • 0027730175 scopus 로고
    • Cytoplasmic dynein-dependent vesicular transport from early to late endosomes
    • Aniento F., Emans N., Griffiths G., Gruenberg J. Cytoplasmic dynein-dependent vesicular transport from early to late endosomes. J Cell Biol. 123:1993;1373-1387.
    • (1993) J Cell Biol , vol.123 , pp. 1373-1387
    • Aniento, F.1    Emans, N.2    Griffiths, G.3    Gruenberg, J.4
  • 11
    • 0031947483 scopus 로고    scopus 로고
    • The role of the dynactin complex in intracellular motility
    • Holleran E.A., Karki S., Holzbaur E.L.F. The role of the dynactin complex in intracellular motility. Intl Rev Ctyology. 182:1998;69-109.
    • (1998) Intl Rev Ctyology , vol.182 , pp. 69-109
    • Holleran, E.A.1    Karki, S.2    Holzbaur, E.L.F.3
  • 12
    • 0032756658 scopus 로고    scopus 로고
    • Role of dynactin in endocytic traffic: Effects of dynamitin overexpression and colocalization with CLIP-170
    • Dynactin colocalizes with CLIP-170 at the plus ends of microtubules, and CLIP-170 recruits dynactin. This suggests that CLIP-170 binds microtubules and then recruits dynactin such that endosomes are linked to microtubules and then the motor, dynein.
    • Valetti C., Wetzel D.M., Schrader M., Hasbani M.J., Gill S.R., Kreis T.E., Schroer T.A. Role of dynactin in endocytic traffic: effects of dynamitin overexpression and colocalization with CLIP-170. Mol Biol Cell. 10:1999;4107-4120. Dynactin colocalizes with CLIP-170 at the plus ends of microtubules, and CLIP-170 recruits dynactin. This suggests that CLIP-170 binds microtubules and then recruits dynactin such that endosomes are linked to microtubules and then the motor, dynein.
    • (1999) Mol Biol Cell , vol.10 , pp. 4107-4120
    • Valetti, C.1    Wetzel, D.M.2    Schrader, M.3    Hasbani, M.J.4    Gill, S.R.5    Kreis, T.E.6    Schroer, T.A.7
  • 13
    • 0026793891 scopus 로고
    • CLIP-170 links endocytic vesicles to microtubules
    • Pierre P., Scheel J., Rickard J., Kreis T.E. CLIP-170 links endocytic vesicles to microtubules. Cell. 70:1992;887-900.
    • (1992) Cell , vol.70 , pp. 887-900
    • Pierre, P.1    Scheel, J.2    Rickard, J.3    Kreis, T.E.4
  • 14
    • 0032816013 scopus 로고    scopus 로고
    • Mapmodulin, cytoplasmic dynein, and microtubules enhance the transport of mannose 6-phosphate receptors from endosomes to the trans-Golgi network
    • Dynein and a novel cofactor, mapmodulin, stimulate microtuble-dependent transport of the mannose 6-phosphate receptor from late endosomes to the TGN in an in vitro assay. In addition, an interesting model is proposed where mapmodulin regulates the association of microtuble-associated proteins (MAPs) with microtubules and thus regulates organelle motility
    • Itin C, Ulitzur N, Muhlbauer, X., Pfeffer SR. Mapmodulin, cytoplasmic dynein, and microtubules enhance the transport of mannose 6-phosphate receptors from endosomes to the trans-Golgi network. Mol Biol Cell 1999, 10:2191-2197 Dynein and a novel cofactor, mapmodulin, stimulate microtuble-dependent transport of the mannose 6-phosphate receptor from late endosomes to the TGN in an in vitro assay. In addition, an interesting model is proposed where mapmodulin regulates the association of microtuble-associated proteins (MAPs) with microtubules and thus regulates organelle motility.
    • (1999) Mol Biol Cell , vol.10 , pp. 2191-2197
    • Itin, C.1    Ulitzur, N.2    Muhlbauer, X.3    Pfeffer, S.R.4
  • 15
    • 0033202945 scopus 로고    scopus 로고
    • Rab5 regulates motility of early endosomes on microtubules
    • A new role for Rab5 in endosomal trafficking is revealed: Rab5 regulates the association of endosomes with microtubules and also regulates early endosome motility on microtubules in vitro.
    • Nielsen E., Severin F., Backer J.M., Hyman A.A., Zerial M. Rab5 regulates motility of early endosomes on microtubules. Nat Cell Biol. 1:1999;376-388. A new role for Rab5 in endosomal trafficking is revealed: Rab5 regulates the association of endosomes with microtubules and also regulates early endosome motility on microtubules in vitro.
    • (1999) Nat Cell Biol , vol.1 , pp. 376-388
    • Nielsen, E.1    Severin, F.2    Backer, J.M.3    Hyman, A.A.4    Zerial, M.5
  • 16
    • 0033280225 scopus 로고    scopus 로고
    • Cooperation between microtubule and actin-based motor proteins
    • Brown S.S. Cooperation between microtubule and actin-based motor proteins. Annu Rev Cell Dev Biol. 15:1999;63-80.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 63-80
    • Brown, S.S.1
  • 18
    • 0033571411 scopus 로고    scopus 로고
    • The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting
    • The tail of yeast myosin V, myo2p, is important for targeting of secretory vesicles and genetically interacts with Smy1p, a kinesin homologue and Sec4p, a vesicle-associated Rab protein.
    • Schott D., Ho J., Pruyne D., Bretscher A. The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting. J Cell Biol. 147:1999;791-808. The tail of yeast myosin V, myo2p, is important for targeting of secretory vesicles and genetically interacts with Smy1p, a kinesin homologue and Sec4p, a vesicle-associated Rab protein.
    • (1999) J Cell Biol , vol.147 , pp. 791-808
    • Schott, D.1    Ho, J.2    Pruyne, D.3    Bretscher, A.4
  • 19
    • 0034004749 scopus 로고    scopus 로고
    • The yeast kinesin-related protein Smy1p exerts its effects on the class V myosin Myo2p via a physical interaction
    • This study shows a direct interaction between yeast myosin V (Myo2p) and the kinesin-related protein Smy1p, suggesting that different motors may be present on the same cargo.
    • Beningo K.A., Lillie S.H., Brown S.S. The yeast kinesin-related protein Smy1p exerts its effects on the class V myosin Myo2p via a physical interaction. Mol Biol Cell. 11:2000;691-702. This study shows a direct interaction between yeast myosin V (Myo2p) and the kinesin-related protein Smy1p, suggesting that different motors may be present on the same cargo.
    • (2000) Mol Biol Cell , vol.11 , pp. 691-702
    • Beningo, K.A.1    Lillie, S.H.2    Brown, S.S.3
  • 20
    • 0033590558 scopus 로고    scopus 로고
    • Direct interaction of microtubule- And actin-based transport motors
    • This paper provides evidence for a direct interaction between myosin Va and mouse ubiquitous kinesin heavy chain (KIF5B), suggesting that the microtubule- and actin-based membrane transport systems could be linked.
    • Huang J.D., Brady S.T., Richards B.W., Stenoien D., Resau J.H., Copeland N.G., Jenkins N.A. Direct interaction of microtubule- and actin-based transport motors. Nature. 397:1999;267-270. This paper provides evidence for a direct interaction between myosin Va and mouse ubiquitous kinesin heavy chain (KIF5B), suggesting that the microtubule- and actin-based membrane transport systems could be linked.
    • (1999) Nature , vol.397 , pp. 267-270
    • Huang, J.D.1    Brady, S.T.2    Richards, B.W.3    Stenoien, D.4    Resau, J.H.5    Copeland, N.G.6    Jenkins, N.A.7
  • 21
    • 0034078008 scopus 로고    scopus 로고
    • Microtubule-based transport system in neurons: The roles of kinesins and dyneins
    • Goldstein L.S.B., Yang Z. Microtubule-based transport system in neurons: the roles of kinesins and dyneins. Annu Rev Neurosci. 23:2000;39-72.
    • (2000) Annu Rev Neurosci , vol.23 , pp. 39-72
    • Goldstein, L.S.B.1    Yang, Z.2
  • 22
    • 0032741064 scopus 로고    scopus 로고
    • Cytoplasmic dynein, the dynactin complex, and kinesin are interdependent and essential for fast axonal transport
    • Martin M., Iyadurai S.J., Gassman A., Gindhart J.G., Hays T.S., Saxton W.M. Cytoplasmic dynein, the dynactin complex, and kinesin are interdependent and essential for fast axonal transport. Mol Cell Biol. 10:1999;3717-3728.
    • (1999) Mol Cell Biol , vol.10 , pp. 3717-3728
    • Martin, M.1    Iyadurai, S.J.2    Gassman, A.3    Gindhart, J.G.4    Hays, T.S.5    Saxton, W.M.6
  • 23
    • 0033549485 scopus 로고    scopus 로고
    • Drosophila roadblock and Chlamydomonas LC7: A conserved family of dynein-associated proteins involved in axonal transport, flagellar motility, and mitosis
    • •] provide the first genetic evidence for the role of dynein in fast retrograde axonal transport.
    • •] provide the first genetic evidence for the role of dynein in fast retrograde axonal transport.
    • (1999) J Cell Biol , vol.146 , pp. 165-179
    • Bowman, A.B.1    Patel-King, R.S.2    Benashski, S.E.3    McCaffery, J.M.4    Goldstein, L.S.B.5    King, S.M.6
  • 24
    • 0026534466 scopus 로고
    • Actin-dependent organelle movement in squid axoplasm
    • Kuznetsov S.A., Langford G.M., Weiss D.G. Actin-dependent organelle movement in squid axoplasm. Nature. 356:1992;722-725.
    • (1992) Nature , vol.356 , pp. 722-725
    • Kuznetsov, S.A.1    Langford, G.M.2    Weiss, D.G.3
  • 25
    • 0032872611 scopus 로고    scopus 로고
    • Myosin Va movements in normal and dilute-lethal axons provide support for a dual filament motor complex
    • Bridgman P.C. Myosin Va movements in normal and dilute-lethal axons provide support for a dual filament motor complex. J Cell Biol. 146:1999;1045-1060.
    • (1999) J Cell Biol , vol.146 , pp. 1045-1060
    • Bridgman, P.C.1
  • 26
    • 0024514875 scopus 로고    scopus 로고
    • The basis of polarity in neurons
    • Black M.M., Bass P.W. The basis of polarity in neurons. Trends Neurosci. 12:2000;211-214.
    • (2000) Trends Neurosci , vol.12 , pp. 211-214
    • Black, M.M.1    Bass, P.W.2
  • 27
    • 0342419162 scopus 로고
    • Polarity orientation of microtubules in hippocampal neurons: Uniformity in the axon and non-uniformity in the dendrite
    • Bass P.W., Deitch J.S., Black M.M., Banker G.A. Polarity orientation of microtubules in hippocampal neurons: uniformity in the axon and non-uniformity in the dendrite. Proc Natl Acad Sci USA. 85:1988;8335-8339.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8335-8339
    • Bass, P.W.1    Deitch, J.S.2    Black, M.M.3    Banker, G.A.4
  • 28
    • 0030888785 scopus 로고    scopus 로고
    • Characterization of KIFC2, a neuronal kinesin superfamily member in mouse
    • Hanlon D.W., Yang Z., Goldstein L.S. Characterization of KIFC2, a neuronal kinesin superfamily member in mouse. Neuron. 18:1997;439-451.
    • (1997) Neuron , vol.18 , pp. 439-451
    • Hanlon, D.W.1    Yang, Z.2    Goldstein, L.S.3
  • 29
    • 0030939131 scopus 로고    scopus 로고
    • KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor for dendritic transport of multi-vesicular body-like organelles
    • Saito N., Okada Y., Noda Y., Kinoshita Y., Kondo S., Hirokawa N. KIFC2 is a novel neuron-specific C-terminal type kinesin superfamily motor for dendritic transport of multi-vesicular body-like organelles. Neuron. 18:1997;425-438.
    • (1997) Neuron , vol.18 , pp. 425-438
    • Saito, N.1    Okada, Y.2    Noda, Y.3    Kinoshita, Y.4    Kondo, S.5    Hirokawa, N.6
  • 30
    • 0033519294 scopus 로고    scopus 로고
    • Novel dendritic kinesin sorting identified by different process targeting of two related kinesins: KIF21A and KIF21B
    • This paper identifies two novel kinesin-like proteins, one of which is enriched in dendrites (KIF21B) and is a likely candidate for a dendritic motor.
    • Marszalek J.R., Weiner J.A., Farlow S.J., Chun J., Goldstein L.S.B. Novel dendritic kinesin sorting identified by different process targeting of two related kinesins: KIF21A and KIF21B. J Cell Biol. 145:1999;469-479. This paper identifies two novel kinesin-like proteins, one of which is enriched in dendrites (KIF21B) and is a likely candidate for a dendritic motor.
    • (1999) J Cell Biol , vol.145 , pp. 469-479
    • Marszalek, J.R.1    Weiner, J.A.2    Farlow, S.J.3    Chun, J.4    Goldstein, L.S.B.5
  • 31
    • 0033535057 scopus 로고    scopus 로고
    • Intraflagellar transport: The eyes have it
    • Rosenbaum J.L., Cole D.G., Diener D.R. Intraflagellar transport: the eyes have it. J Cell Biol. 144:1999;385-388.
    • (1999) J Cell Biol , vol.144 , pp. 385-388
    • Rosenbaum, J.L.1    Cole, D.G.2    Diener, D.R.3
  • 33
    • 0033577894 scopus 로고    scopus 로고
    • Left-right asymmetry and kinesin superfamily protein KIF3A: New insights in determination of laterality and mesoderm induction by kif3A -/- mice analysis
    • •,34], show that mouse mutants of kinesin-II subunits KIF3A and KIF3B lack cilia on early cells of the embryonic cells perhaps as a result of defective transport within the cilum itself. The work also establishes that cilia are important for the determination of left-right body axes.
    • •,34], show that mouse mutants of kinesin-II subunits KIF3A and KIF3B lack cilia on early cells of the embryonic cells perhaps as a result of defective transport within the cilum itself. The work also establishes that cilia are important for the determination of left-right body axes.
    • (1999) J Cell Biol , vol.145 , pp. 825-836
    • Takeda, S.1    Yonekawa, Y.2    Tanaka, Y.3    Okada, Y.4    Nonaka, S.5    Hirokawa, N.6
  • 34
    • 0032428685 scopus 로고    scopus 로고
    • Randomization of left-right asymmetry due to loss of nodal cilia generating leftward flow of extraembryonic fluid in mice lacking KIF3B motor protein
    • Nonaka S., Tanaka Y., Okada Y., Takeda S., Harada A., Kanai Y., Kido M., Hirokawa N. Randomization of left-right asymmetry due to loss of nodal cilia generating leftward flow of extraembryonic fluid in mice lacking KIF3B motor protein. Cell. 95:1998;829-837.
    • (1998) Cell , vol.95 , pp. 829-837
    • Nonaka, S.1    Tanaka, Y.2    Okada, Y.3    Takeda, S.4    Harada, A.5    Kanai, Y.6    Kido, M.7    Hirokawa, N.8
  • 35
  • 37
    • 0033231086 scopus 로고    scopus 로고
    • Role of Class DHC1b dynein in retrograde transport of IFT motors and IFT raft particles along cilia, but not dendrites, in chemosensory neurons of living Caenorhabditis elegans
    • •] use fluoresence microscopy to monitor the intraflagellar transport (IFT) of GFP-tagged kinesin II (KAP subunit) and its putative cargoes (OSM-1 and OSM-6) in living C. elegans.
    • •] use fluoresence microscopy to monitor the intraflagellar transport (IFT) of GFP-tagged kinesin II (KAP subunit) and its putative cargoes (OSM-1 and OSM-6) in living C. elegans.
    • (1999) J Cell Biol , vol.147 , pp. 519-530
    • Signor, D.1    Wedaman, K.P.2    Orozco, J.T.3    Dwyer, N.D.4    Bargmann, C.I.5    Rose, L.S.6    Scholey, J.M.7
  • 38
    • 0033603239 scopus 로고    scopus 로고
    • Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1
    • Rhodopsin is identified as the first membrane cargo receptor for dynein by directly interacting with Tctex-1, a dynein light chain. This interaction is necessary for dynein to translocate rhodopsin-bearing vesicles along microtubules in vitro.
    • Tai A.W., Chuang J-Z., Bode C., Wolfrum U., Sung C-H. Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1. Cell. 97:1999;877-887. Rhodopsin is identified as the first membrane cargo receptor for dynein by directly interacting with Tctex-1, a dynein light chain. This interaction is necessary for dynein to translocate rhodopsin-bearing vesicles along microtubules in vitro.
    • (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
  • 39
    • 0033280668 scopus 로고    scopus 로고
    • The road less traveled: Emerging principles: Emerging principles of kinesin motor utilization
    • Goldstein L.S.B., Philip A.V. The road less traveled: emerging principles: emerging principles of kinesin motor utilization. Annu Rev Cell Dev Biol. 15:1999;141-183.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 141-183
    • Goldstein, L.S.B.1    Philip, A.V.2
  • 41
    • 0033195492 scopus 로고    scopus 로고
    • Single-molecule analysis of kinesin motility reveals regulation by the cargo-binding tail domain
    • ••].
    • ••].
    • (1999) Nat Cell Biol , vol.1 , pp. 293-297
    • Friedman, D.S.1    Vale, R.D.2
  • 42
    • 0033591331 scopus 로고    scopus 로고
    • Formation of the compact confomer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity
    • ••] suggest that in the absence of bound cargo, kinesin-1 folds into a compact conformation and is inhibited from moving along microtubules by its cargo-binding tail.
    • ••] suggest that in the absence of bound cargo, kinesin-1 folds into a compact conformation and is inhibited from moving along microtubules by its cargo-binding tail.
    • (1999) J Biol Chem , vol.274 , pp. 14617-14623
    • Stock, M.F.1    Guerrero, J.2    Cobb, B.3    Eggers, C.T.4    Huang, T.-G.5    Li, X.6    Hackney, D.7
  • 44
    • 0030911916 scopus 로고    scopus 로고
    • Immnochemical analysis of kinesin light chain function
    • Stenoinen D.L., Brady S.T. Immnochemical analysis of kinesin light chain function. Mol Biol Cell. 8:1997;675-689.
    • (1997) Mol Biol Cell , vol.8 , pp. 675-689
    • Stenoinen, D.L.1    Brady, S.T.2
  • 46
    • 0033004145 scopus 로고    scopus 로고
    • Cytoplasmic dynein and dynactin in cell division and intracellular transport
    • Karki S., Holzbaur E.L. Cytoplasmic dynein and dynactin in cell division and intracellular transport. Curr Opin Cell Biol. 11:1999;45-53.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 45-53
    • Karki, S.1    Holzbaur, E.L.2
  • 47
    • 0033789351 scopus 로고    scopus 로고
    • Dynactin increases the processivity of the cytoplasmic dynein motor
    • Dynactin binds microtubules and increases the processivity of the cytoplasmic dynein motor in an in vitro bead-motility assay.
    • King S.J., Schroer T.A. Dynactin increases the processivity of the cytoplasmic dynein motor. Nat Cell Biol. 2:2000;20-24. Dynactin binds microtubules and increases the processivity of the cytoplasmic dynein motor in an in vitro bead-motility assay.
    • (2000) Nat Cell Biol , vol.2 , pp. 20-24
    • King, S.J.1    Schroer, T.A.2
  • 48
    • 0032728976 scopus 로고    scopus 로고
    • Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the Arp1 minifilament pointed end
    • Eckley D.M., Gill S.R., Melkonian K.A., Bingham J.B., Goodson H.V., Heuser J.E., Schroer T.A. Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the Arp1 minifilament pointed end. J Cell Biol. 147:1999;307-319.
    • (1999) J Cell Biol , vol.147 , pp. 307-319
    • Eckley, D.M.1    Gill, S.R.2    Melkonian, K.A.3    Bingham, J.B.4    Goodson, H.V.5    Heuser, J.E.6    Schroer, T.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.