메뉴 건너뛰기




Volumn 24, Issue 15, 2013, Pages 2362-2377

The yeast dynein Dyn2-Pac11 complex is a dynein dimerization/processivity factor: Structural and single-molecule characterization

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASMIC DYNEIN; DYN2 PROTEIN; FUNGAL PROTEIN; HOMODIMER; PAC11 PROTEIN; UNCLASSIFIED DRUG;

EID: 84881065338     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E13-03-0166     Document Type: Article
Times cited : (23)

References (71)
  • 1
    • 0034657914 scopus 로고    scopus 로고
    • Microtubule interactions with the cell cortex causing nuclear movements in Saccharomyces cerevisiae
    • Adames NR, Cooper JA (2000). Microtubule interactions with the cell cortex causing nuclear movements in Saccharomyces cerevisiae. J Cell Biol 149, 863-874.
    • (2000) J Cell Biol , vol.149 , pp. 863-874
    • Adames, N.R.1    Cooper, J.A.2
  • 2
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD et al. (2010). PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66, 213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 3
    • 77949486211 scopus 로고    scopus 로고
    • Dynein at the kinetochore: Timing, interactions and functions
    • Bader JR, Vaughan KT (2010). Dynein at the kinetochore: timing, interactions and functions. Semin Cell Dev Biol 21, 269-275.
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 269-275
    • Bader, J.R.1    Vaughan, K.T.2
  • 4
    • 56249132454 scopus 로고    scopus 로고
    • The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8
    • Benison G, Karplus PA, Barbar E (2008). The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8. J Mol Biol 384, 954-966.
    • (2008) J Mol Biol , vol.384 , pp. 954-966
    • Benison, G.1    Karplus, P.A.2    Barbar, E.3
  • 5
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger AT (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 7
    • 79952254224 scopus 로고    scopus 로고
    • Crystal structure of the dynein motor domain
    • Carter AP, Cho C, Jin L, Vale RD (2011). Crystal structure of the dynein motor domain. Science 331, 1159-1165.
    • (2011) Science , vol.331 , pp. 1159-1165
    • Carter, A.P.1    Cho, C.2    Jin, L.3    Vale, R.D.4
  • 9
    • 78650047411 scopus 로고    scopus 로고
    • Neurodegenerative mutation in cytoplasmic dynein alters its organization and dynein-dynactin and dynein-kinesin interactions
    • Deng W, Garrett C, Dombert B, Soura V, Banks G, Fisher EM, van der Brug MP, Hafezparast M (2010). Neurodegenerative mutation in cytoplasmic dynein alters its organization and dynein-dynactin and dynein-kinesin interactions. J Biol Chem 285, 39922-39934.
    • (2010) J Biol Chem , vol.285 , pp. 39922-39934
    • Deng, W.1    Garrett, C.2    Dombert, B.3    Soura, V.4    Banks, G.5    Fisher, E.M.6    Van Der Brug, M.P.7    Hafezparast, M.8
  • 12
    • 0035931754 scopus 로고    scopus 로고
    • Cortical Num1p interacts with the dynein intermediate chain Pac11p and cytoplasmic microtubules in budding yeast
    • Farkasovsky M, Küntzel H (2001). Cortical Num1p interacts with the dynein intermediate chain Pac11p and cytoplasmic microtubules in budding yeast. J Cell Biol 152, 251-262.
    • (2001) J Cell Biol , vol.152 , pp. 251-262
    • Farkasovsky, M.1    Küntzel, H.2
  • 13
    • 0030923317 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae genes required in the absence of the CIN8-encoded spindle motor act in functionally diverse mitotic pathways
    • Geiser JR, Schott EJ, Kingsbury TJ, Cole NB, Totis LJ, Bhattacharyya G, He L, Hoyt MA (1997). Saccharomyces cerevisiae genes required in the absence of the CIN8-encoded spindle motor act in functionally diverse mitotic pathways. Mol Biol Cell 8, 1035-1050.
    • (1997) Mol Biol Cell , vol.8 , pp. 1035-1050
    • Geiser, J.R.1    Schott, E.J.2    Kingsbury, T.J.3    Cole, N.B.4    Totis, L.J.5    Bhattacharyya, G.6    He, L.7    Hoyt, M.A.8
  • 14
    • 36249009069 scopus 로고    scopus 로고
    • Force-induced bidirectional stepping of cytoplasmic dynein
    • Gennerich A, Carter AP, Reck-Peterson SL, Vale RD (2007). Force-induced bidirectional stepping of cytoplasmic dynein. Cell 131, 952-965.
    • (2007) Cell , vol.131 , pp. 952-965
    • Gennerich, A.1    Carter, A.P.2    Reck-Peterson, S.L.3    Vale, R.D.4
  • 15
    • 0028334031 scopus 로고
    • Characterization of DLC-A and DLC-B, two families of cytoplasmic dynein light chain subunits
    • Gill SR, Cleveland DW, Schroer TA (1994). Characterization of DLC-A and DLC-B, two families of cytoplasmic dynein light chain subunits. Mol Biol Cell 5, 645-654.
    • (1994) Mol Biol Cell , vol.5 , pp. 645-654
    • Gill, S.R.1    Cleveland, D.W.2    Schroer, T.A.3
  • 16
    • 0032873415 scopus 로고    scopus 로고
    • Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae
    • Goldstein AL, McCusker JH (1999). Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae. Yeast 15, 1541-1553.
    • (1999) Yeast , vol.15 , pp. 1541-1553
    • Goldstein, A.L.1    McCusker, J.H.2
  • 17
    • 0037734370 scopus 로고    scopus 로고
    • Mutations in dynein link motor neuron degeneration to defects in retrograde transport
    • Hafezparast M et al. (2003). Mutations in dynein link motor neuron degeneration to defects in retrograde transport. Science 300, 808-812.
    • (2003) Science , vol.300 , pp. 808-812
    • Hafezparast, M.1
  • 18
    • 77954568867 scopus 로고    scopus 로고
    • The crystal structure of dynein intermediate chain-light chain roadblock complex gives new insights into dynein assembly
    • Hall J, Song Y, Karplus PA, Barbar E (2010). The crystal structure of dynein intermediate chain-light chain roadblock complex gives new insights into dynein assembly. J Biol Chem 285, 22566-22575.
    • (2010) J Biol Chem , vol.285 , pp. 22566-22575
    • Hall, J.1    Song, Y.2    Karplus, P.A.3    Barbar, E.4
  • 19
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y et al. (2002). Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415, 180-183.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1
  • 20
    • 33750054653 scopus 로고    scopus 로고
    • Alternatively spliced exon B of myosin Va is essential for binding the tail-associated light chain shared by dynein
    • Hódi Z, Nemeth AL, Radnai L, Hetenyi C, Schlett K, Bodor A, Perczel A, Nyitray L (2006). Alternatively spliced exon B of myosin Va is essential for binding the tail-associated light chain shared by dynein. Biochemistry 45, 12582-12595.
    • (2006) Biochemistry , vol.45 , pp. 12582-12595
    • Hódi, Z.1    Nemeth, A.L.2    Radnai, L.3    Hetenyi, C.4    Schlett, K.5    Bodor, A.6    Perczel, A.7    Nyitray, L.8
  • 21
    • 0034425715 scopus 로고    scopus 로고
    • Genome-wide, large-scale production of mutant mice by ENU mutagenesis
    • Hrabé de Angelis MH et al. (2000). Genome-wide, large-scale production of mutant mice by ENU mutagenesis. Nat Genet 25, 444-447.
    • (2000) Nat Genet , vol.25 , pp. 444-447
    • Hrabé De Angelis, M.H.1
  • 22
    • 36049016163 scopus 로고    scopus 로고
    • The coordination of cyclic microtubule association/dissociation and tail swing of cytoplasmic dynein
    • Imamula K, Kon T, Ohkura R, Sutoh K (2007). The coordination of cyclic microtubule association/dissociation and tail swing of cytoplasmic dynein. Proc Natl Acad Sci USA 104, 16134-16139.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 16134-16139
    • Imamula, K.1    Kon, T.2    Ohkura, R.3    Sutoh, K.4
  • 23
    • 65249170094 scopus 로고    scopus 로고
    • Regulation of the processivity and intracellular localization of Saccharomyces cerevisiae dynein by dynactin
    • Kardon JR, Reck-Peterson SL, Vale RD (2009). Regulation of the processivity and intracellular localization of Saccharomyces cerevisiae dynein by dynactin. Proc Natl Acad Sci USA 106, 5669-5674.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5669-5674
    • Kardon, J.R.1    Reck-Peterson, S.L.2    Vale, R.D.3
  • 24
    • 0028806377 scopus 로고
    • Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex
    • Karki S, Holzbaur EL (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.2
  • 25
    • 0036227869 scopus 로고    scopus 로고
    • Subunit organization in cytoplasmic dynein subcomplexes
    • King SJ, Bonilla M, Rodgers ME, Schroer TA (2002). Subunit organization in cytoplasmic dynein subcomplexes. Protein Sci 11, 1239-1250.
    • (2002) Protein Sci , vol.11 , pp. 1239-1250
    • King, S.J.1    Bonilla, M.2    Rodgers, M.E.3    Schroer, T.A.4
  • 27
    • 0035159410 scopus 로고    scopus 로고
    • Modulation of cytoplasmic dynein ATPase activity by the accessory subunits
    • Kini AR, Collins CA (2001). Modulation of cytoplasmic dynein ATPase activity by the accessory subunits. Cell Motil Cytoskeleton 48, 52-60.
    • (2001) Cell Motil Cytoskeleton , vol.48 , pp. 52-60
    • Kini, A.R.1    Collins, C.A.2
  • 28
  • 29
    • 4444330119 scopus 로고    scopus 로고
    • Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein
    • Kon T, Nishiura M, Ohkura R, Toyoshima YY, Sutoh K (2004). Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein. Biochemistry 43, 11266-11274.
    • (2004) Biochemistry , vol.43 , pp. 11266-11274
    • Kon, T.1    Nishiura, M.2    Ohkura, R.3    Toyoshima, Y.Y.4    Sutoh, K.5
  • 31
    • 13844250546 scopus 로고    scopus 로고
    • The offloading model for dynein function: Differential function of motor subunits
    • Lee WL, Kaiser MA, Cooper JA (2005). The offloading model for dynein function: differential function of motor subunits. J Cell Biol 168, 201-207.
    • (2005) J Cell Biol , vol.168 , pp. 201-207
    • Lee, W.L.1    Kaiser, M.A.2    Cooper, J.A.3
  • 32
    • 0037415644 scopus 로고    scopus 로고
    • The role of the lissencephaly protein Pac1 during nuclear migration in budding yeast
    • Lee WL, Oberle JR, Cooper JA (2003). The role of the lissencephaly protein Pac1 during nuclear migration in budding yeast. J Cell Biol 160, 355-364.
    • (2003) J Cell Biol , vol.160 , pp. 355-364
    • Lee, W.L.1    Oberle, J.R.2    Cooper, J.A.3
  • 33
    • 22144491144 scopus 로고    scopus 로고
    • NudEL targets dynein to microtubule ends through LIS1
    • Li J, Lee WL, Cooper JA (2005). NudEL targets dynein to microtubule ends through LIS1. Nat Cell Biol 7, 686-690.
    • (2005) Nat Cell Biol , vol.7 , pp. 686-690
    • Li, J.1    Lee, W.L.2    Cooper, J.A.3
  • 34
    • 0027453547 scopus 로고
    • Disruption of mitotic spindle orientation in a yeast dynein mutant
    • Li YY, Yeh E, Bloom K (1993). Disruption of mitotic spindle orientation in a yeast dynein mutant. Proc Natl Acad Sci USA 90, 10096-10100.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10096-10100
    • Li, Y.Y.1    Yeh, E.2    Bloom, K.3
  • 36
    • 0037006969 scopus 로고    scopus 로고
    • Interactions of cytoplasmic dynein light chains Tctex-1 and LC8 with the intermediate chain IC74
    • Makokha M, Hare M, Li M, Hays T, Barbar E (2002). Interactions of cytoplasmic dynein light chains Tctex-1 and LC8 with the intermediate chain IC74. Biochemistry 41, 4302-4311.
    • (2002) Biochemistry , vol.41 , pp. 4302-4311
    • Makokha, M.1    Hare, M.2    Li, M.3    Hays, T.4    Barbar, E.5
  • 37
    • 0035957959 scopus 로고    scopus 로고
    • Structure of Tctex-1 and its interaction with cytoplasmic dynein intermediate chain
    • Mok YK, Lo KW, Zhang M (2001). Structure of Tctex-1 and its interaction with cytoplasmic dynein intermediate chain. J Biol Chem 276, 14067-14074.
    • (2001) J Biol Chem , vol.276 , pp. 14067-14074
    • Mok, Y.K.1    Lo, K.W.2    Zhang, M.3
  • 38
    • 40449130757 scopus 로고    scopus 로고
    • Dynactin function in mitotic spindle positioning
    • Moore JK, Li J, Cooper JA (2008). Dynactin function in mitotic spindle positioning. Traffic 9, 510-527.
    • (2008) Traffic , vol.9 , pp. 510-527
    • Moore, J.K.1    Li, J.2    Cooper, J.A.3
  • 39
    • 0028871742 scopus 로고
    • Point mutation of adenosine triphosphate-binding motif generated rigor kinesin that selectively blocks anterograde lysosome membrane transport
    • Nakata T, Hirokawa N (1995). Point mutation of adenosine triphosphate-binding motif generated rigor kinesin that selectively blocks anterograde lysosome membrane transport. J Cell Biol 131, 1039-1053.
    • (1995) J Cell Biol , vol.131 , pp. 1039-1053
    • Nakata, T.1    Hirokawa, N.2
  • 40
    • 79954448219 scopus 로고    scopus 로고
    • C-sequence of the Dictyostelium cytoplasmic dynein participates in processivity modulation
    • Numata N, Shima T, Ohkura R, Kon T, Sutoh K (2011). C-sequence of the Dictyostelium cytoplasmic dynein participates in processivity modulation. FEBS Lett 585, 1185-1190.
    • (2011) FEBS Lett , vol.585 , pp. 1185-1190
    • Numata, N.1    Shima, T.2    Ohkura, R.3    Kon, T.4    Sutoh, K.5
  • 41
    • 27444442808 scopus 로고    scopus 로고
    • Ionization of His 55 at the dimer interface of dynein light-chain LC8 is coupled to dimer dissociation
    • Nyarko A, Cochrun L, Norwood S, Pursifull N, Voth A, Barbar E (2005). Ionization of His 55 at the dimer interface of dynein light-chain LC8 is coupled to dimer dissociation. Biochemistry 44, 14248-14255.
    • (2005) Biochemistry , vol.44 , pp. 14248-14255
    • Nyarko, A.1    Cochrun, L.2    Norwood, S.3    Pursifull, N.4    Voth, A.5    Barbar, E.6
  • 42
    • 80052327148 scopus 로고    scopus 로고
    • Conformational dynamics promote binding diversity of dynein light chain LC8
    • Nyarko A, Hall J, Hall A, Hare M, Kremerskothen J, Barbar E (2011). Conformational dynamics promote binding diversity of dynein light chain LC8. Biophys Chem 159, 41-47.
    • (2011) Biophys Chem , vol.159 , pp. 41-47
    • Nyarko, A.1    Hall, J.2    Hall, A.3    Hare, M.4    Kremerskothen, J.5    Barbar, E.6
  • 43
    • 78649842747 scopus 로고    scopus 로고
    • A cytoplasmic dynein tail mutation impairs motor processivity
    • Ori-McKenney KM, Xu J, Gross SP, Vallee RB (2010). A cytoplasmic dynein tail mutation impairs motor processivity. Nat Cell Biol 12, 1228-1234.
    • (2010) Nat Cell Biol , vol.12 , pp. 1228-1234
    • Ori-Mckenney, K.M.1    Xu, J.2    Gross, S.P.3    Vallee, R.B.4
  • 44
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997). Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 45
    • 23644443050 scopus 로고    scopus 로고
    • Conjugation of fluorophores to tubulin
    • Peloquin J, Komarova Y, Borisy G (2005). Conjugation of fluorophores to tubulin. Nat Methods 2, 299-303.
    • (2005) Nat Methods , vol.2 , pp. 299-303
    • Peloquin, J.1    Komarova, Y.2    Borisy, G.3
  • 47
    • 84873829562 scopus 로고    scopus 로고
    • Identification of a novel site in the tail of dynein heavy chain important for dynein function in vivo
    • Qiu R, Zhang J, Xiang X (2013). Identification of a novel site in the tail of dynein heavy chain important for dynein function in vivo. J Biol Chem 288, 2271-2280.
    • (2013) J Biol Chem , vol.288 , pp. 2271-2280
    • Qiu, R.1    Zhang, J.2    Xiang, X.3
  • 48
    • 78649646795 scopus 로고    scopus 로고
    • Affinity, avidity, and kinetics of target sequence binding to LC8 dynein light chain isoforms
    • Radnai L et al. (2010). Affinity, avidity, and kinetics of target sequence binding to LC8 dynein light chain isoforms. J Biol Chem 285, 38649-38657.
    • (2010) J Biol Chem , vol.285 , pp. 38649-38657
    • Radnai, L.1
  • 49
    • 84860389388 scopus 로고    scopus 로고
    • DYNLL/LC8: A light chain subunit of the dynein motor complex and beyond
    • Rapali P, Szenes A, Radnai L, Bakos A, Pal G, Nyitray L (2011). DYNLL/LC8: a light chain subunit of the dynein motor complex and beyond. FEBS J 278, 2980-2996.
    • (2011) FEBS J , vol.278 , pp. 2980-2996
    • Rapali, P.1    Szenes, A.2    Radnai, L.3    Bakos, A.4    Pal, G.5    Nyitray, L.6
  • 51
    • 59049095230 scopus 로고    scopus 로고
    • AAA+ Ring and linker swing mechanism in the dynein motor
    • Roberts AJ et al. (2009). AAA+ Ring and linker swing mechanism in the dynein motor. Cell 136, 485-495.
    • (2009) Cell , vol.136 , pp. 485-495
    • Roberts, A.J.1
  • 52
    • 84860848799 scopus 로고    scopus 로고
    • Structure of a yeast Dyn2-Nup159 complex and molecular basis for dynein light chain-nuclear pore interaction
    • Romes EM, Tripathy A, Slep KC (2012). Structure of a yeast Dyn2-Nup159 complex and molecular basis for dynein light chain-nuclear pore interaction. J Biol Chem 287, 15862-15873.
    • (2012) J Biol Chem , vol.287 , pp. 15862-15873
    • Romes, E.M.1    Tripathy, A.2    Slep, K.C.3
  • 54
    • 0028890381 scopus 로고
    • Saccharomyces cerevisiae kinesin-and dynein-related proteins required for anaphase chromosome segregation
    • Saunders WS, Koshland D, Eshel D, Gibbons IR, Hoyt MA (1995). Saccharomyces cerevisiae kinesin-and dynein-related proteins required for anaphase chromosome segregation. J Cell Biol 128, 617-624.
    • (1995) J Cell Biol , vol.128 , pp. 617-624
    • Saunders, W.S.1    Koshland, D.2    Eshel, D.3    Gibbons, I.R.4    Hoyt, M.A.5
  • 55
    • 84860721580 scopus 로고    scopus 로고
    • Insights into dynein motor domain function from a 3.3-A crystal structure
    • S491
    • Schmidt H, Gleave ES, Carter AP (2012). Insights into dynein motor domain function from a 3.3-A crystal structure. Nat Struct Mol Biol 19, 492-497, S491.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 492-497
    • Schmidt, H.1    Gleave, E.S.2    Carter, A.P.3
  • 56
    • 77954639410 scopus 로고    scopus 로고
    • Acidification of the oxygen scavenging system in single-molecule fluorescence studies: In situ sensing with a ratiometric dual-emission probe
    • Shi X, Lim J, Ha T (2010). Acidification of the oxygen scavenging system in single-molecule fluorescence studies: in situ sensing with a ratiometric dual-emission probe. Anal Chem 82, 6132-6138.
    • (2010) Anal Chem , vol.82 , pp. 6132-6138
    • Shi, X.1    Lim, J.2    Ha, T.3
  • 57
    • 0033231086 scopus 로고    scopus 로고
    • Role of a 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
    • Signor D, Wedaman KP, Orozco JT, Dwyer ND, Bargmann CI, Rose LS, Scholey JM (1999). Role of a 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. J Cell Biol 147, 519-530.
    • (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
  • 58
    • 84866490577 scopus 로고    scopus 로고
    • A mouse neurodegenerative dynein heavy chain mutation alters dynein motility and localization in Neurospora crassa
    • Sivagurunathan S, Schnittker RR, Nandini S, Plamann MD, King SJ (2012). A mouse neurodegenerative dynein heavy chain mutation alters dynein motility and localization in Neurospora crassa. Cytoskeleton (Hoboken) 69, 613-624.
    • (2012) Cytoskeleton (Hoboken) , vol.69 , pp. 613-624
    • Sivagurunathan, S.1    Schnittker, R.R.2    Nandini, S.3    Plamann, M.D.4    King, S.J.5
  • 60
    • 0025320820 scopus 로고
    • Localization of cytoplasmic dynein to mitotic spindles and kinetochores
    • Steuer ER, Wordeman L, Schroer TA, Sheetz MP (1990). Localization of cytoplasmic dynein to mitotic spindles and kinetochores. Nature 345, 266-268.
    • (1990) Nature , vol.345 , pp. 266-268
    • Steuer, E.R.1    Wordeman, L.2    Schroer, T.A.3    Sheetz, M.P.4
  • 61
    • 79961036305 scopus 로고    scopus 로고
    • Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning
    • Stuchell-Brereton MD, Siglin A, Li J, Moore JK, Ahmed S, Williams JC, Cooper JA (2011). Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning. Mol Biol Cell 22, 2690-2701.
    • (2011) Mol Biol Cell , vol.22 , pp. 2690-2701
    • Stuchell-Brereton, M.D.1    Siglin, A.2    Li, J.3    Moore, J.K.4    Ahmed, S.5    Williams, J.C.6    Cooper, J.A.7
  • 63
    • 84860281806 scopus 로고    scopus 로고
    • A novel patch assembly domain in Num1 mediates dynein anchoring at the cortex during spindle positioning
    • Tang X, Germain BS, Lee WL (2012). A novel patch assembly domain in Num1 mediates dynein anchoring at the cortex during spindle positioning. J Cell Biol 196, 743-756.
    • (2012) J Cell Biol , vol.196 , pp. 743-756
    • Tang, X.1    Germain, B.S.2    Lee, W.L.3
  • 64
    • 84871387592 scopus 로고    scopus 로고
    • Reconstitution of the human cytoplasmic dynein complex
    • Trokter M, Mücke N, Surrey T (2012). Reconstitution of the human cytoplasmic dynein complex. Proc Natl Acad Sci USA 109, 20895-20900.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 20895-20900
    • Trokter, M.1    Mücke, N.2    Surrey, T.3
  • 65
    • 33644746123 scopus 로고    scopus 로고
    • Molecular requirements for kinetochore-associated microtubule formation in mammalian cells
    • Tulu US, Fagerstrom C, Ferenz NP, Wadsworth P (2006). Molecular requirements for kinetochore-associated microtubule formation in mammalian cells. Curr Biol 16, 536-541.
    • (2006) Curr Biol , vol.16 , pp. 536-541
    • Tulu, U.S.1    Fagerstrom, C.2    Ferenz, N.P.3    Wadsworth, P.4
  • 66
    • 0034693043 scopus 로고    scopus 로고
    • Distinct but overlapping sites within the cytoplasmic dynein heavy chain for dimerization and for intermediate chain and light intermediate chain binding
    • Tynan SH, Gee MA, Vallee RB (2000). Distinct but overlapping sites within the cytoplasmic dynein heavy chain for dimerization and for intermediate chain and light intermediate chain binding. J Biol Chem 275, 32769-32774.
    • (2000) J Biol Chem , vol.275 , pp. 32769-32774
    • Tynan, S.H.1    Gee, M.A.2    Vallee, R.B.3
  • 67
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • Vale RD (2003). The molecular motor toolbox for intracellular transport. Cell 112, 467-480.
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 68
    • 33749012287 scopus 로고    scopus 로고
    • The binding of DYNLL2 to myosin Va requires alternatively spliced exon B and stabilizes a portion of the myosin's coiled-coil domain
    • Wagner W, Fodor E, Ginsburg A, Hammer JA 3rd (2006). The binding of DYNLL2 to myosin Va requires alternatively spliced exon B and stabilizes a portion of the myosin's coiled-coil domain. Biochemistry 45, 11564-11577.
    • (2006) Biochemistry , vol.45 , pp. 11564-11577
    • Wagner, W.1    Fodor, E.2    Ginsburg, A.3    Hammer III, J.A.4
  • 69
    • 35948979262 scopus 로고    scopus 로고
    • Dyneins across eukaryotes: A comparative genomic analysis
    • Wickstead B, Gull K (2007). Dyneins across eukaryotes: a comparative genomic analysis. Traffic 8, 1708-1721.
    • (2007) Traffic , vol.8 , pp. 1708-1721
    • Wickstead, B.1    Gull, K.2
  • 71
    • 20444488809 scopus 로고    scopus 로고
    • Crystal structure of dynein light chain TcTex-1
    • Williams JC, Xie H, Hendrickson WA (2005). Crystal structure of dynein light chain TcTex-1. J Biol Chem 280, 21981-21986.
    • (2005) J Biol Chem , vol.280 , pp. 21981-21986
    • Williams, J.C.1    Xie, H.2    Hendrickson, W.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.