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Volumn 12, Issue 6, 2006, Pages 469-476

Microtubule: A common target for Parkin and Parkinson's disease toxins

Author keywords

Dopamine; Microtubules; Parkin; Parkinson's disease; Rotenone; Tubulin

Indexed keywords

ANTIFUNGAL AGENT; ANTIPARASITIC AGENT; BENZIMIDAZOLE; NOCODAZOLE; PARKIN; ROTENONE; TIABENDAZOLE; TOXIN; TUBULIN; UBIQUITIN PROTEIN LIGASE E3;

EID: 33750466222     PISSN: 10738584     EISSN: 10894098     Source Type: Journal    
DOI: 10.1177/1073858406293853     Document Type: Review
Times cited : (82)

References (50)
  • 1
    • 76749158549 scopus 로고    scopus 로고
    • Tubulin and microtubules
    • Chichester (UK): Wiley
    • Amos LA. 2005. Tubulin and microtubules. In: Encyclopedia of life sciences. Chichester (UK): Wiley.
    • (2005) Encyclopedia of Life Sciences
    • Amos, L.A.1
  • 2
    • 0036140644 scopus 로고    scopus 로고
    • Microtubule transport in the axon
    • Baas PW. 2002. Microtubule transport in the axon. Int Rev Cytol 212:41-62.
    • (2002) Int Rev Cytol , vol.212 , pp. 41-62
    • Baas, P.W.1
  • 3
    • 33644976376 scopus 로고    scopus 로고
    • Continuing trials of GDNF in Parkinson's disease
    • Barker RA. 2006. Continuing trials of GDNF in Parkinson's disease. Lancet Neurol 5:285-6.
    • (2006) Lancet Neurol , vol.5 , pp. 285-286
    • Barker, R.A.1
  • 5
    • 0016367228 scopus 로고
    • Rotenone inhibition of spindle microtubule assembly in mammalian cells
    • Brinkley BR, Barham SS, Barranco SC, Fuller GM. 1974. Rotenone inhibition of spindle microtubule assembly in mammalian cells. Exp Cell Res 85:41-6.
    • (1974) Exp Cell Res , vol.85 , pp. 41-46
    • Brinkley, B.R.1    Barham, S.S.2    Barranco, S.C.3    Fuller, G.M.4
  • 6
    • 0024582786 scopus 로고
    • Dominant effects of tubulin overexpression in saccharomyces-cerevisiae
    • Burke D, Gasdaska P, Hartwell L. 1989. Dominant effects of tubulin overexpression in saccharomyces-cerevisiae. Mol Cell Biol 9:1049-59.
    • (1989) Mol Cell Biol , vol.9 , pp. 1049-1059
    • Burke, D.1    Gasdaska, P.2    Hartwell, L.3
  • 7
    • 0033118430 scopus 로고    scopus 로고
    • Influence of MPP+ on the state of tubulin polymerisation in NGF-differentiated PC12 cells
    • Cappelletti G, Maggioni MG, Maci R. 1999. Influence of MPP+ on the state of tubulin polymerisation in NGF-differentiated PC12 cells. J Neurosci Res 56:28-35.
    • (1999) J Neurosci Res , vol.56 , pp. 28-35
    • Cappelletti, G.1    Maggioni, M.G.2    Maci, R.3
  • 9
    • 0034826896 scopus 로고    scopus 로고
    • Regulation of microtubule-associated proteins
    • Cassimeris L, Spittle C. 2001. Regulation of microtubule-associated proteins. Int Rev Cytol 210:163-226.
    • (2001) Int Rev Cytol , vol.210 , pp. 163-226
    • Cassimeris, L.1    Spittle, C.2
  • 10
    • 0001717675 scopus 로고
    • Inhibition of electron and energy transfer in mitochondria. I. Effects of amytal, thiopental, rotenone, progesterone, and methylene glycol
    • Chance B, Williams GR, Hollunger G. 1963. Inhibition of electron and energy transfer in mitochondria. I. Effects of amytal, thiopental, rotenone, progesterone, and methylene glycol. J Biol Chem 238:418-31.
    • (1963) J Biol Chem , vol.238 , pp. 418-431
    • Chance, B.1    Williams, G.R.2    Hollunger, G.3
  • 11
    • 0020967742 scopus 로고
    • The tubulins: From DNA to RNA to protein and back again
    • Cleveland DW. 1983. The tubulins: from DNA to RNA to protein and back again. Cell 34:330-2.
    • (1983) Cell , vol.34 , pp. 330-332
    • Cleveland, D.W.1
  • 12
    • 0024372769 scopus 로고
    • Autoregulated control of tubulin synthesis in animal cells
    • Cleveland DW. 1989. Autoregulated control of tubulin synthesis in animal cells. Curr Opin Cell Biol 1:10-14.
    • (1989) Curr Opin Cell Biol , vol.1 , pp. 10-14
    • Cleveland, D.W.1
  • 13
    • 0028950267 scopus 로고
    • Organization of organelles and membrane traffic by microtubules
    • Cole NB, Lippincott-Schwartz J. 1995. Organization of organelles and membrane traffic by microtubules. Curr Opin Cell Biol 7:55-64.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 55-64
    • Cole, N.B.1    Lippincott-Schwartz, J.2
  • 14
    • 27944470972 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors in the basal ganglia motor circuit
    • Conn PJ, Battaglia G, Marino MJ, Nicoletti F. 2005. Metabotropic glutamate receptors in the basal ganglia motor circuit. Nat Rev Neurosci 6:787-98.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 787-798
    • Conn, P.J.1    Battaglia, G.2    Marino, M.J.3    Nicoletti, F.4
  • 15
    • 0042521076 scopus 로고    scopus 로고
    • The environment and Parkinson's disease: Is the nigrostriatal system preferentially targeted by neurotoxins?
    • Di Monte DA. 2003. The environment and Parkinson's disease: is the nigrostriatal system preferentially targeted by neurotoxins? Lancet Neurol 2:531-8.
    • (2003) Lancet Neurol , vol.2 , pp. 531-538
    • Di Monte, D.A.1
  • 16
    • 0028850898 scopus 로고
    • Dynamic storage of dopamine in rat brain synaptic vesicles in vitro
    • Floor E, Leventhal PS, Wang Y, Meng L, Chen W. 1995. Dynamic storage of dopamine in rat brain synaptic vesicles in vitro. J Neurochem 64:689-99.
    • (1995) J Neurochem , vol.64 , pp. 689-699
    • Floor, E.1    Leventhal, P.S.2    Wang, Y.3    Meng, L.4    Chen, W.5
  • 17
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • Hampton RY. 2002. ER-associated degradation in protein quality control and cellular regulation. Curr Opin Cell Biol 14:476-82.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 18
    • 0029665268 scopus 로고    scopus 로고
    • [H-3]dihydrorotenone binding to NADH: Ubiquinone reductase (Complex I) of the electron transport chain: an autoradiographic study
    • Higgins DS, Greenamyre JT. 1996. [H-3]dihydrorotenone binding to NADH: ubiquinone reductase (Complex I) of the electron transport chain: an autoradiographic study. J Neurosci 16:3807-16.
    • (1996) J Neurosci , vol.16 , pp. 3807-3816
    • Higgins, D.S.1    Greenamyre, J.T.2
  • 19
    • 0028156230 scopus 로고
    • Mitotic disrupter herbicides act by a single mechanism but vary in efficacy
    • Hoffman JC, Vaughn KC. 1994. Mitotic disrupter herbicides act by a single mechanism but vary in efficacy. Protoplasma 179:16-25.
    • (1994) Protoplasma , vol.179 , pp. 16-25
    • Hoffman, J.C.1    Vaughn, K.C.2
  • 20
    • 0031655976 scopus 로고    scopus 로고
    • Chlorpropham [isopropyl N-(3-chlorophenyl) carbamate] disrupts microtubule organization, cell division, and early development of sea urchin embryos
    • Holy J. 1998. Chlorpropham [isopropyl N-(3-chlorophenyl) carbamate] disrupts microtubule organization, cell division, and early development of sea urchin embryos. J Toxicol Environ Health A 54:319-33.
    • (1998) J Toxicol Environ Health A , vol.54 , pp. 319-333
    • Holy, J.1
  • 21
    • 33646833056 scopus 로고    scopus 로고
    • Basic fibroblast growth factor protects against rotenone-induced dopaminergic cell death through activation of extracellular signal-regulated kinases 1/2 and phosphatidylinositol-3 kinase pathways
    • Hsuan SL, Klintworth HM, Xia Z. 2006. Basic fibroblast growth factor protects against rotenone-induced dopaminergic cell death through activation of extracellular signal-regulated kinases 1/2 and phosphatidylinositol-3 kinase pathways. J Neurosci 26:4481-91.
    • (2006) J Neurosci , vol.26 , pp. 4481-4491
    • Hsuan, S.L.1    Klintworth, H.M.2    Xia, Z.3
  • 22
    • 0141995596 scopus 로고    scopus 로고
    • The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI
    • Huynh DP, Scoles DR, Nguyen D, Pulst SM. 2003. The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI. Hum Mol Genet 12:2587-97.
    • (2003) Hum Mol Genet , vol.12 , pp. 2587-2597
    • Huynh, D.P.1    Scoles, D.R.2    Nguyen, D.3    Pulst, S.M.4
  • 23
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai Y, Soda M, Inoue H, Hattori N, Mizuno Y, Takahashi R. 2001. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin Cell 105:891-902.
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 24
    • 11144232015 scopus 로고    scopus 로고
    • Parkin increases dopamine uptake by enhancing the cell surface expression of dopamine transporter
    • Jiang H, Jiang Q, Feng J. 2004. Parkin increases dopamine uptake by enhancing the cell surface expression of dopamine transporter. J Biol Chem 279:54380-6.
    • (2004) J Biol Chem , vol.279 , pp. 54380-54386
    • Jiang, H.1    Jiang, Q.2    Feng, J.3
  • 25
    • 33749410628 scopus 로고    scopus 로고
    • Neurotrophic factors stabilize microtubules and protect against rotenone toxicity on dopaminergic neurons
    • Jiang Q, Yan Z, Feng J. 2006a. Neurotrophic factors stabilize microtubules and protect against rotenone toxicity on dopaminergic neurons. J Biol Chem 281:29391-400.
    • (2006) J Biol Chem , vol.281 , pp. 29391-29400
    • Jiang, Q.1    Yan, Z.2    Feng, J.3
  • 26
    • 33646446045 scopus 로고    scopus 로고
    • Activation of group III metabotropic glutamate receptors attenuates rotenone toxicity on dopaminergic neurons through a microtubule-dependent mechanism
    • Jiang Q, Yan Z, Feng J. 2006b. Activation of group III metabotropic glutamate receptors attenuates rotenone toxicity on dopaminergic neurons through a microtubule-dependent mechanism. J Neurosci 26:4318-28.
    • (2006) J Neurosci , vol.26 , pp. 4318-4328
    • Jiang, Q.1    Yan, Z.2    Feng, J.3
  • 27
    • 1942438028 scopus 로고    scopus 로고
    • Microtubules as a target for anticancer drugs
    • Jordan MA, Wilson L. 2004. Microtubules as a target for anticancer drugs. Nat Rev Cancer 4:253-65.
    • (2004) Nat Rev Cancer , vol.4 , pp. 253-265
    • Jordan, M.A.1    Wilson, L.2
  • 28
    • 1642499508 scopus 로고    scopus 로고
    • Localized striatal delivery of GDNF as a treatment for Parkinson disease
    • Kirik D, Georgievska B, Bjorklund A. 2004. Localized striatal delivery of GDNF as a treatment for Parkinson disease. Nat Neurosci 7:105-10.
    • (2004) Nat Neurosci , vol.7 , pp. 105-110
    • Kirik, D.1    Georgievska, B.2    Bjorklund, A.3
  • 29
    • 2142760084 scopus 로고    scopus 로고
    • Screening for microtubule-disrupting antifungal agents by using a mitotic-arrest mutant of Aspergillus nidulans and novel action of phenylalanine derivatives accompanying tubulin loss
    • Kiso T, Fujita K, Ping X, Tanaka T, Taniguchi M. 2004. Screening for microtubule-disrupting antifungal agents by using a mitotic-arrest mutant of Aspergillus nidulans and novel action of phenylalanine derivatives accompanying tubulin loss. Antimicrob Agents Chemother 48:1739-48.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 1739-1748
    • Kiso, T.1    Fujita, K.2    Ping, X.3    Tanaka, T.4    Taniguchi, M.5
  • 30
    • 0028215382 scopus 로고
    • Biochemistry of benzimidazole resistance
    • Lacey E, Gill JH. 1994. Biochemistry of benzimidazole resistance. Acta Trop 56:245-62.
    • (1994) Acta Trop , vol.56 , pp. 245-262
    • Lacey, E.1    Gill, J.H.2
  • 31
    • 0036776975 scopus 로고    scopus 로고
    • Parkinson's disease: Current and future challenges
    • Langston JW. 2002. Parkinson's disease: current and future challenges. Neurotoxicology 23:443-50.
    • (2002) Neurotoxicology , vol.23 , pp. 443-450
    • Langston, J.W.1
  • 32
    • 0030687570 scopus 로고    scopus 로고
    • The alpha- and beta-tubulin folding pathways
    • Lewis SA, Tian GL, Cowan NJ. 1997. The alpha- and beta-tubulin folding pathways. Trends Cell Biol 7:479-84.
    • (1997) Trends Cell Biol , vol.7 , pp. 479-484
    • Lewis, S.A.1    Tian, G.L.2    Cowan, N.J.3
  • 34
    • 0031044233 scopus 로고    scopus 로고
    • The role of vesicular transport proteins in synaptic transmission and neural degeneration
    • Liu Y, Edwards RH. 1997. The role of vesicular transport proteins in synaptic transmission and neural degeneration. Annu Rev Neurosci 20:125-56.
    • (1997) Annu Rev Neurosci , vol.20 , pp. 125-156
    • Liu, Y.1    Edwards, R.H.2
  • 35
    • 1242341372 scopus 로고    scopus 로고
    • Activation of group III metabotropic glutamate receptors in selected regions of the basal ganglia alleviates akinesia in the reserpine-treated rat
    • Macinnes N, Messenger MJ, Duty S. 2004. Activation of group III metabotropic glutamate receptors in selected regions of the basal ganglia alleviates akinesia in the reserpine-treated rat. Br J Pharmacol 141:15-22.
    • (2004) Br J Pharmacol , vol.141 , pp. 15-22
    • Macinnes, N.1    Messenger, M.J.2    Duty, S.3
  • 36
    • 0018176775 scopus 로고
    • Rotenone inhibition of tubulin self-assembly
    • Marshall LE, Himes RH. 1978. Rotenone inhibition of tubulin self-assembly. Biochim Biophys Acta 543:590-4.
    • (1978) Biochim Biophys Acta , vol.543 , pp. 590-594
    • Marshall, L.E.1    Himes, R.H.2
  • 37
    • 0036842251 scopus 로고    scopus 로고
    • A missense mutation in Tbce causes progressive motor neuronopathy in mice
    • Martin N, Jaubert J, Gounon P, Salido E, Haase G, Szatanik M, and others. 2002. A missense mutation in Tbce causes progressive motor neuronopathy in mice. Nat Genet 32:443-7.
    • (2002) Nat Genet , vol.32 , pp. 443-447
    • Martin, N.1    Jaubert, J.2    Gounon, P.3    Salido, E.4    Haase, G.5    Szatanik, M.6
  • 39
    • 26644464601 scopus 로고    scopus 로고
    • Selective vulnerability of dopaminergic neurons to microtubule depolymerization
    • Ren Y, Liu W, Jiang H, Jiang Q, Feng J. 2005. Selective vulnerability of dopaminergic neurons to microtubule depolymerization. J Biol Chem 280:34105-12.
    • (2005) J Biol Chem , vol.280 , pp. 34105-34112
    • Ren, Y.1    Liu, W.2    Jiang, H.3    Jiang, Q.4    Feng, J.5
  • 40
    • 0037738525 scopus 로고    scopus 로고
    • Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation
    • Ren Y, Zhao JH, Feng J. 2003. Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation. J Neurosci 23:3316-24.
    • (2003) J Neurosci , vol.23 , pp. 3316-3324
    • Ren, Y.1    Zhao, J.H.2    Feng, J.3
  • 41
    • 0343167942 scopus 로고    scopus 로고
    • 2,4-Dichlorophenoxyacetic acid disrupts the cytoskeleton and disorganizes the Golgi apparatus of cultured neurons
    • Rosso SB, Caceres AO, de Duffard AM, Duffard RO, Quiroga S. 2000. 2,4-Dichlorophenoxyacetic acid disrupts the cytoskeleton and disorganizes the Golgi apparatus of cultured neurons. Toxicol Sci 56:133-40.
    • (2000) Toxicol Sci , vol.56 , pp. 133-140
    • Rosso, S.B.1    Caceres, A.O.2    De Duffard, A.M.3    Duffard, R.O.4    Quiroga, S.5
  • 42
    • 0018393931 scopus 로고
    • NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation
    • Takeshige K, Minakami S. 1979. NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation. Biochem J 180:129-35.
    • (1979) Biochem J , vol.180 , pp. 129-135
    • Takeshige, K.1    Minakami, S.2
  • 44
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai B, Ye Y, Rapoport TA. 2002. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat Rev Mol Cell Biol 3:246-55.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 45
    • 0042626528 scopus 로고    scopus 로고
    • Group III metabotropic glutamate receptor-mediated modulation of the striatopallidal synapse
    • Valenti O, Marino MJ, Wittmann M, Lis E, DiLella AG, Kinney GG, and others. 2003. Group III metabotropic glutamate receptor-mediated modulation of the striatopallidal synapse. J Neurosci 23:7218-26.
    • (2003) J Neurosci , vol.23 , pp. 7218-7226
    • Valenti, O.1    Marino, M.J.2    Wittmann, M.3    Lis, E.4    DiLella, A.G.5    Kinney, G.G.6
  • 46
    • 4043181214 scopus 로고    scopus 로고
    • Cancer genes and the pathways they control
    • Vogelstein B, Kinzler KW. 2004. Cancer genes and the pathways they control. Nat Med 10:789-99.
    • (2004) Nat Med , vol.10 , pp. 789-799
    • Vogelstein, B.1    Kinzler, K.W.2
  • 47
    • 33744955439 scopus 로고    scopus 로고
    • Mutations affecting beta-tubulin folding and degradation
    • Wang Y, Tian G, Cowan NJ, Cabral F. 2006. Mutations affecting beta-tubulin folding and degradation. J Biol Chem 281:13628-35.
    • (2006) J Biol Chem , vol.281 , pp. 13628-13635
    • Wang, Y.1    Tian, G.2    Cowan, N.J.3    Cabral, F.4
  • 48
    • 20444451210 scopus 로고    scopus 로고
    • Parkin stabilizes microtubules through strong binding mediated by three independent domains
    • Yang F, Jiang Q, Zhao J, Ren Y, Sutton MD, Feng J. 2005. Parkin stabilizes microtubules through strong binding mediated by three independent domains. J Biol Chem 280:17154-62.
    • (2005) J Biol Chem , vol.280 , pp. 17154-17162
    • Yang, F.1    Jiang, Q.2    Zhao, J.3    Ren, Y.4    Sutton, M.D.5    Feng, J.6
  • 49
    • 0033302704 scopus 로고    scopus 로고
    • Inheritance of resistance to anti-microtubule dinitroaniline herbicides in an "intermediate" resistant biotype of Eleusine indica (Poaceae)
    • Zeng L, Baird WV. 1999. Inheritance of resistance to anti-microtubule dinitroaniline herbicides in an "intermediate" resistant biotype of Eleusine indica (Poaceae). Am J Bot 86:940.
    • (1999) Am J Bot , vol.86 , pp. 940
    • Zeng, L.1    Baird, W.V.2
  • 50
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • Zhang Y, Gao J, Chung KK, Huang H, Dawson VL, Dawson TM. 2000. Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc Natl Acad Sci U S A 97:13354-59.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6


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