메뉴 건너뛰기




Volumn 57, Issue 4, 2014, Pages 372-377

Cytoplasmic dynein: A key player in neurodegenerative and neurodevelopmental diseases

Author keywords

dynein; neurodegenerative diseases; neurodevelopmental diseases; pathogenesis; retrograde transport

Indexed keywords

MUS;

EID: 84899932523     PISSN: 16747305     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11427-014-4639-9     Document Type: Review
Times cited : (35)

References (58)
  • 1
    • 0023608935 scopus 로고
    • MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
    • Paschal BM, Shpetner HS, Vallee RB. MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. J Cell Biol, 1987, 105: 1273-1282.
    • (1987) J Cell Biol , vol.105 , pp. 1273-1282
    • Paschal, B.M.1    Shpetner, H.S.2    Vallee, R.B.3
  • 2
    • 80052510244 scopus 로고    scopus 로고
    • Cytoplasmic dynein
    • Allan VJ. Cytoplasmic dynein. Biochem Soc Trans, 2011, 39: 1169-1178.
    • (2011) Biochem Soc Trans , vol.39 , pp. 1169-1178
    • Allan, V.J.1
  • 4
    • 13844275634 scopus 로고    scopus 로고
    • Dynein cargo gets its groove back
    • Pfister KK. Dynein cargo gets its groove back. Structure, 2005, 13: 172-173.
    • (2005) Structure , vol.13 , pp. 172-173
    • Pfister, K.K.1
  • 5
    • 84860272533 scopus 로고    scopus 로고
    • Dynactin is required for transport initiation from the distal axon
    • Moughamian AJ, Holzbaur EL. Dynactin is required for transport initiation from the distal axon. Neuron, 2012, 74: 331-343.
    • (2012) Neuron , vol.74 , pp. 331-343
    • Moughamian, A.J.1    Holzbaur, E.L.2
  • 6
    • 0029563632 scopus 로고
    • Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued
    • Vaughan KT, Vallee RB. Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued. J Cell Biol, 1995, 131: 1507-1516.
    • (1995) J Cell Biol , vol.131 , pp. 1507-1516
    • Vaughan, K.T.1    Vallee, R.B.2
  • 8
    • 33644747344 scopus 로고    scopus 로고
    • A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules
    • Culver-Hanlon TL, Lex SA, Stephens AD, Quintyne NJ, King SJ. A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules. Nat Cell Biol, 2006, 8: 264-270.
    • (2006) Nat Cell Biol , vol.8 , pp. 264-270
    • Culver-Hanlon, T.L.1    Lex, S.A.2    Stephens, A.D.3    Quintyne, N.J.4    King, S.J.5
  • 9
    • 0030751640 scopus 로고    scopus 로고
    • Spindle assembly in Xenopus egg extracts: respective roles of centrosomes and microtubule self-organization
    • Heald R, Tournebize R, Habermann A, Karsenti E, Hyman A. Spindle assembly in Xenopus egg extracts: respective roles of centrosomes and microtubule self-organization. J Cell Biol, 1997, 138: 615-628.
    • (1997) J Cell Biol , vol.138 , pp. 615-628
    • Heald, R.1    Tournebize, R.2    Habermann, A.3    Karsenti, E.4    Hyman, A.5
  • 10
    • 0033004145 scopus 로고    scopus 로고
    • Cytoplasmic dynein and dynactin in cell division and intracellular transport
    • Karki S, Holzbaur EL. Cytoplasmic dynein and dynactin in cell division and intracellular transport. Curr Opin Cell Biol, 1999, 11: 45-53.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 45-53
    • Karki, S.1    Holzbaur, E.L.2
  • 11
    • 0842333851 scopus 로고    scopus 로고
    • Dynein: an ancient motor protein involved in multiple modes of transport
    • Vallee RB, Williams JC, Varma D, Barnhart LE. Dynein: an ancient motor protein involved in multiple modes of transport. J Neurobiol, 2004, 58: 189-200.
    • (2004) J Neurobiol , vol.58 , pp. 189-200
    • Vallee, R.B.1    Williams, J.C.2    Varma, D.3    Barnhart, L.E.4
  • 12
    • 70450228589 scopus 로고    scopus 로고
    • Regulators of the cytoplasmic dynein motor
    • Kardon JR, Vale RD. Regulators of the cytoplasmic dynein motor. Nat Rev Mol Cell Biol, 2009, 10: 854-865.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 854-865
    • Kardon, J.R.1    Vale, R.D.2
  • 13
    • 77951701022 scopus 로고    scopus 로고
    • LIS1 and NudE induce a persistent dynein force-producing state
    • McKenney RJ, Vershinin M, Kunwar A, Vallee RB, Gross SP. LIS1 and NudE induce a persistent dynein force-producing state. Cell, 2010, 141: 304-314.
    • (2010) Cell , vol.141 , pp. 304-314
    • McKenney, R.J.1    Vershinin, M.2    Kunwar, A.3    Vallee, R.B.4    Gross, S.P.5
  • 14
    • 33751020569 scopus 로고    scopus 로고
    • Axonal transport and neurodegenerative disease
    • Chevalier-Larsen E, Holzbaur EL. Axonal transport and neurodegenerative disease. Biochim Biophys Acta, 2006, 1762: 1094-1108.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 1094-1108
    • Chevalier-Larsen, E.1    Holzbaur, E.L.2
  • 15
    • 84055217271 scopus 로고    scopus 로고
    • Molecular motor proteins and amyotrophic lateral sclerosis
    • Soo KY, Farg M, Atkin JD. Molecular motor proteins and amyotrophic lateral sclerosis. Int J Mol Sci, 2011, 12: 9057-9082.
    • (2011) Int J Mol Sci , vol.12 , pp. 9057-9082
    • Soo, K.Y.1    Farg, M.2    Atkin, J.D.3
  • 16
    • 0027164824 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen DR. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature, 1993, 364: 362.
    • (1993) Nature , vol.364 , pp. 362
    • Rosen, D.R.1
  • 17
    • 0028960506 scopus 로고
    • Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice
    • Brown RJ. Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell, 1995, 80: 687-692.
    • (1995) Cell , vol.80 , pp. 687-692
    • Brown, R.J.1
  • 18
    • 12344278194 scopus 로고    scopus 로고
    • Inducible superoxide dismutase 1 aggregation in transgenic amyotrophic lateral sclerosis mouse fibroblasts
    • Turner BJ, Lopes EC, Cheema SS. Inducible superoxide dismutase 1 aggregation in transgenic amyotrophic lateral sclerosis mouse fibroblasts. J Cell Biochem, 2004, 91: 1074-1084.
    • (2004) J Cell Biochem , vol.91 , pp. 1074-1084
    • Turner, B.J.1    Lopes, E.C.2    Cheema, S.S.3
  • 21
    • 34447550238 scopus 로고    scopus 로고
    • Interaction between familial amyotrophic lateral sclerosis (ALS)-linked SOD1 mutants and the dynein complex
    • Zhang F, Strom AL, Fukada K, Lee S, Hayward LJ, Zhu H. Interaction between familial amyotrophic lateral sclerosis (ALS)-linked SOD1 mutants and the dynein complex. J Biol Chem, 2007, 282: 16691-16699.
    • (2007) J Biol Chem , vol.282 , pp. 16691-16699
    • Zhang, F.1    Strom, A.L.2    Fukada, K.3    Lee, S.4    Hayward, L.J.5    Zhu, H.6
  • 22
    • 34548299711 scopus 로고    scopus 로고
    • Defective axonal transport in motor neuron disease
    • El-Kadi AM, Soura V, Hafezparast M. Defective axonal transport in motor neuron disease. J Neurosci Res, 2007, 85: 2557-2566.
    • (2007) J Neurosci Res , vol.85 , pp. 2557-2566
    • El-Kadi, A.M.1    Soura, V.2    Hafezparast, M.3
  • 23
    • 45549084712 scopus 로고    scopus 로고
    • Cytoplasmic dynein could be key to understanding neurodegeneration
    • Banks GT, Fisher EM. Cytoplasmic dynein could be key to understanding neurodegeneration. Genome Biol, 2008, 9: 214.
    • (2008) Genome Biol , vol.9 , pp. 214
    • Banks, G.T.1    Fisher, E.M.2
  • 24
    • 37549068958 scopus 로고    scopus 로고
    • Proprioceptive sensory neuropathy in mice with a mutation in the cytoplasmic Dynein heavy chain 1 gene
    • Chen XJ, Levedakou EN, Millen KJ, Wollmann RL, Soliven B, Popko B. Proprioceptive sensory neuropathy in mice with a mutation in the cytoplasmic Dynein heavy chain 1 gene. J Neurosci, 2007, 27: 14515-14524.
    • (2007) J Neurosci , vol.27 , pp. 14515-14524
    • Chen, X.J.1    Levedakou, E.N.2    Millen, K.J.3    Wollmann, R.L.4    Soliven, B.5    Popko, B.6
  • 25
    • 41649086378 scopus 로고    scopus 로고
    • Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria
    • Vande VC, Miller TM, Cashman NR, Cleveland DW. Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria. Proc Natl Acad Sci USA, 2008, 105: 4022-4027.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 4022-4027
    • Vande, V.C.1    Miller, T.M.2    Cashman, N.R.3    Cleveland, D.W.4
  • 27
    • 0016266593 scopus 로고
    • Genetic and clinical aspects of Charcot-Marie-Tooth's disease
    • Skre H. Genetic and clinical aspects of Charcot-Marie-Tooth's disease. Clin Genet, 1974, 6: 98-118.
    • (1974) Clin Genet , vol.6 , pp. 98-118
    • Skre, H.1
  • 28
    • 33745278558 scopus 로고    scopus 로고
    • Clinical and electrophysiological aspects of Charcot-Marie-Tooth disease
    • Pareyson D, Scaioli V, Laura M. Clinical and electrophysiological aspects of Charcot-Marie-Tooth disease. Neuromolecular Med, 2006, 8: 3-22.
    • (2006) Neuromolecular Med , vol.8 , pp. 3-22
    • Pareyson, D.1    Scaioli, V.2    Laura, M.3
  • 29
    • 67349116532 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease
    • Szigeti K, Lupski JR. Charcot-Marie-Tooth disease. Eur J Hum Genet, 2009, 17: 703-710.
    • (2009) Eur J Hum Genet , vol.17 , pp. 703-710
    • Szigeti, K.1    Lupski, J.R.2
  • 33
    • 5444267945 scopus 로고    scopus 로고
    • Phenotypic analysis of neurofilament light gene mutations linked to Charcot-Marie-Tooth disease in cell culture models
    • Perez-Olle R, Jones ST, Liem RK. Phenotypic analysis of neurofilament light gene mutations linked to Charcot-Marie-Tooth disease in cell culture models. Hum Mol Genet, 2004, 13: 2207-2220.
    • (2004) Hum Mol Genet , vol.13 , pp. 2207-2220
    • Perez-Olle, R.1    Jones, S.T.2    Liem, R.K.3
  • 34
    • 77949801029 scopus 로고    scopus 로고
    • Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex
    • Misko A, Jiang S, Wegorzewska I, Milbrandt J, Baloh RH. Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/Milton complex. J Neurosci, 2010, 30: 4232-4240.
    • (2010) J Neurosci , vol.30 , pp. 4232-4240
    • Misko, A.1    Jiang, S.2    Wegorzewska, I.3    Milbrandt, J.4    Baloh, R.H.5
  • 37
    • 84862141618 scopus 로고    scopus 로고
    • A novel phenotype for the dynein heavy chain mutation Loa: altered dendritic morphology, organelle density, and reduced numbers of trigeminal motoneurons
    • Wiggins LM, Kuta A, Stevens JC, Fisher EM, von Bartheld CS. A novel phenotype for the dynein heavy chain mutation Loa: altered dendritic morphology, organelle density, and reduced numbers of trigeminal motoneurons. J Comp Neurol, 2012, 520: 2757-2773.
    • (2012) J Comp Neurol , vol.520 , pp. 2757-2773
    • Wiggins, L.M.1    Kuta, A.2    Stevens, J.C.3    Fisher, E.M.4    von Bartheld, C.S.5
  • 38
    • 0037047506 scopus 로고    scopus 로고
    • Normal dendritic arborization in spinal motoneurons requires neurofilament subunit L
    • Zhang Z, Casey DM, Julien JP, Xu Z. Normal dendritic arborization in spinal motoneurons requires neurofilament subunit L. J Comp Neurol, 2002, 450: 144-152.
    • (2002) J Comp Neurol , vol.450 , pp. 144-152
    • Zhang, Z.1    Casey, D.M.2    Julien, J.P.3    Xu, Z.4
  • 42
    • 2942561028 scopus 로고    scopus 로고
    • The importance of neuritic plaques and tangles to the development and evolution of AD
    • Tiraboschi P, Hansen LA, Thal LJ, Corey-Bloom J. The importance of neuritic plaques and tangles to the development and evolution of AD. Neurology, 2004, 62: 1984-1989.
    • (2004) Neurology , vol.62 , pp. 1984-1989
    • Tiraboschi, P.1    Hansen, L.A.2    Thal, L.J.3    Corey-Bloom, J.4
  • 45
    • 79955641945 scopus 로고    scopus 로고
    • Cytoplasmic dynein in neurodegeneration
    • Eschbach J, Dupuis L. Cytoplasmic dynein in neurodegeneration. Pharmacol Ther, 2011, 130: 348-363.
    • (2011) Pharmacol Ther , vol.130 , pp. 348-363
    • Eschbach, J.1    Dupuis, L.2
  • 46
    • 34948859426 scopus 로고    scopus 로고
    • Aging attenuates dynactindynein interaction: down-regulation of dynein causes accumulation of endogenous tau and amyloid precursor protein in human neuroblastoma cells
    • Kimura N, Imamura O, Ono F, Terao K. Aging attenuates dynactindynein interaction: down-regulation of dynein causes accumulation of endogenous tau and amyloid precursor protein in human neuroblastoma cells. J Neurosci Res, 2007, 85: 2909-2916.
    • (2007) J Neurosci Res , vol.85 , pp. 2909-2916
    • Kimura, N.1    Imamura, O.2    Ono, F.3    Terao, K.4
  • 47
    • 0042733013 scopus 로고    scopus 로고
    • Rab5-stimulated up-regulation of the endocytic pathway increases intracellular betacleaved amyloid precursor protein carboxyl-terminal fragment levels and Abeta production
    • Grbovic OM, Mathews PM, Jiang Y, Schmidt SD, Dinakar R, Summers-Terio NB, Ceresa BP, Nixon RA, Cataldo AM. Rab5-stimulated up-regulation of the endocytic pathway increases intracellular betacleaved amyloid precursor protein carboxyl-terminal fragment levels and Abeta production. J Biol Chem, 2003, 278: 31261-31268.
    • (2003) J Biol Chem , vol.278 , pp. 31261-31268
    • Grbovic, O.M.1    Mathews, P.M.2    Jiang, Y.3    Schmidt, S.D.4    Dinakar, R.5    Summers-Terio, N.B.6    Ceresa, B.P.7    Nixon, R.A.8    Cataldo, A.M.9
  • 48
    • 84882284105 scopus 로고    scopus 로고
    • Hyperphosphorylation of tau protein by calpain regulation in retina of Alzheimer's disease transgenic mouse
    • Zhao H, Chang R, Che H, Wang J, Yang L, Fang W, Xia Y, Li N, Ma Q, Wang X. Hyperphosphorylation of tau protein by calpain regulation in retina of Alzheimer's disease transgenic mouse. Neurosci Lett, 2013, 551: 12-16.
    • (2013) Neurosci Lett , vol.551 , pp. 12-16
    • Zhao, H.1    Chang, R.2    Che, H.3    Wang, J.4    Yang, L.5    Fang, W.6    Xia, Y.7    Li, N.8    Ma, Q.9    Wang, X.10
  • 49
    • 84877633354 scopus 로고    scopus 로고
    • Inhibition of serine palmitoyltransferase reduces Abeta and tau hyperphosphorylation in a murine model: a safe therapeutic strategy for Alzheimer's disease
    • Geekiyanage H, Upadhye A, Chan C. Inhibition of serine palmitoyltransferase reduces Abeta and tau hyperphosphorylation in a murine model: a safe therapeutic strategy for Alzheimer's disease. Neurobiol Aging, 2013, 34: 2037-2051.
    • (2013) Neurobiol Aging , vol.34 , pp. 2037-2051
    • Geekiyanage, H.1    Upadhye, A.2    Chan, C.3
  • 50
    • 25144517127 scopus 로고    scopus 로고
    • Altered cellular distribution of phospho-tau proteins coincides with impaired retrograde axonal transport in neurons of aged rats
    • Niewiadomska G, Baksalerska-Pazera M, Riedel G. Altered cellular distribution of phospho-tau proteins coincides with impaired retrograde axonal transport in neurons of aged rats. Ann N Y Acad Sci, 2005, 1048: 287-295.
    • (2005) Ann N Y Acad Sci , vol.1048 , pp. 287-295
    • Niewiadomska, G.1    Baksalerska-Pazera, M.2    Riedel, G.3
  • 51
    • 0035364748 scopus 로고    scopus 로고
    • Expanded CAG repeats in exon 1 of the Huntington's disease gene stimulate dopamine-mediated striatal neuron autophagy and degeneration
    • Petersen A, Larsen KE, Behr GG, Romero N, Przedborski S, Brundin P, Sulzer D. Expanded CAG repeats in exon 1 of the Huntington's disease gene stimulate dopamine-mediated striatal neuron autophagy and degeneration. Hum Mol Genet, 2001, 10: 1243-1254.
    • (2001) Hum Mol Genet , vol.10 , pp. 1243-1254
    • Petersen, A.1    Larsen, K.E.2    Behr, G.G.3    Romero, N.4    Przedborski, S.5    Brundin, P.6    Sulzer, D.7
  • 53
    • 77951701022 scopus 로고    scopus 로고
    • LIS1 and NudE induce a persistent dynein force-producing state
    • McKenney RJ, Vershinin M, Kunwar A, Vallee RB, Gross SP. LIS1 and NudE induce a persistent dynein force-producing state. Cell, 2010, 141: 304-314.
    • (2010) Cell , vol.141 , pp. 304-314
    • McKenney, R.J.1    Vershinin, M.2    Kunwar, A.3    Vallee, R.B.4    Gross, S.P.5
  • 54
    • 34250677626 scopus 로고    scopus 로고
    • Cytoplasmic dynein and LIS1 are required for microtubule advance during growth cone remodeling and fast axonal outgrowth
    • Grabham PW, Seale GE, Bennecib M, Goldberg DJ, Vallee RB. Cytoplasmic dynein and LIS1 are required for microtubule advance during growth cone remodeling and fast axonal outgrowth. J Neurosci, 2007, 27: 5823-5834.
    • (2007) J Neurosci , vol.27 , pp. 5823-5834
    • Grabham, P.W.1    Seale, G.E.2    Bennecib, M.3    Goldberg, D.J.4    Vallee, R.B.5
  • 56
    • 5144228139 scopus 로고    scopus 로고
    • Ndel1 operates in a common pathway with LIS1 and cytoplasmic dynein to regulate cortical neuronal positioning
    • Shu T, Ayala R, Nguyen MD, Xie Z, Gleeson JG, Tsai LH. Ndel1 operates in a common pathway with LIS1 and cytoplasmic dynein to regulate cortical neuronal positioning. Neuron, 2004, 44: 263-277.
    • (2004) Neuron , vol.44 , pp. 263-277
    • Shu, T.1    Ayala, R.2    Nguyen, M.D.3    Xie, Z.4    Gleeson, J.G.5    Tsai, L.H.6
  • 57
    • 5144228139 scopus 로고    scopus 로고
    • Ndel1 operates in a common pathway with LIS1 and cytoplasmic dynein to regulate cortical neuronal positioning
    • Shu T, Ayala R, Nguyen MD, Xie Z, Gleeson JG, Tsai LH. Ndel1 operates in a common pathway with LIS1 and cytoplasmic dynein to regulate cortical neuronal positioning. Neuron, 2004, 44: 263-277.
    • (2004) Neuron , vol.44 , pp. 263-277
    • Shu, T.1    Ayala, R.2    Nguyen, M.D.3    Xie, Z.4    Gleeson, J.G.5    Tsai, L.H.6
  • 58
    • 84886253792 scopus 로고    scopus 로고
    • Cytoskeleton in action: lissencephaly, a neuronal migration disorder
    • Moon HM, Wynshaw-Boris A. Cytoskeleton in action: lissencephaly, a neuronal migration disorder. Wiley Interdiscip Rev Dev Biol, 2013, 2: 229-245.
    • (2013) Wiley Interdiscip Rev Dev Biol , vol.2 , pp. 229-245
    • Moon, H.M.1    Wynshaw-Boris, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.