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Volumn 1802, Issue 1, 2010, Pages 62-65

Impaired mitochondrial trafficking in Huntington's disease

Author keywords

Huntington; Mitochondria; Neurodegeneration; Trafficking

Indexed keywords

HUNTINGTIN; MITOCHONDRIAL ENZYME; MOLECULAR MOTOR; MUTANT PROTEIN;

EID: 71849091297     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2009.06.008     Document Type: Review
Times cited : (54)

References (49)
  • 1
  • 2
    • 0032416346 scopus 로고    scopus 로고
    • Oxygen and ion concentrations in normoxic and hypoxic brain cells
    • Silver I., and Erecinska M. Oxygen and ion concentrations in normoxic and hypoxic brain cells. Adv. Exp. Med. Biol. 454 (1998) 7-16
    • (1998) Adv. Exp. Med. Biol. , vol.454 , pp. 7-16
    • Silver, I.1    Erecinska, M.2
  • 3
    • 20444376592 scopus 로고    scopus 로고
    • Dendritic spine geometry: functional implication and regulation
    • Hayashi Y., and Majewska A.K. Dendritic spine geometry: functional implication and regulation. Neuron 46 (2005) 529-532
    • (2005) Neuron , vol.46 , pp. 529-532
    • Hayashi, Y.1    Majewska, A.K.2
  • 4
    • 9144269974 scopus 로고    scopus 로고
    • Imaging the motility of dendritic protrusions and axon terminals: roles in axon sampling and synaptic competition
    • Konur S., and Yuste R. Imaging the motility of dendritic protrusions and axon terminals: roles in axon sampling and synaptic competition. Mol. Cell. Neurosci. 27 (2004) 427-440
    • (2004) Mol. Cell. Neurosci. , vol.27 , pp. 427-440
    • Konur, S.1    Yuste, R.2
  • 5
    • 30544452263 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Hollenbeck P.J., and Saxton W.M. The axonal transport of mitochondria. J. Cell Sci. 118 (2005) 5411-5419
    • (2005) J. Cell Sci. , vol.118 , pp. 5411-5419
    • Hollenbeck, P.J.1    Saxton, W.M.2
  • 6
    • 24944534881 scopus 로고    scopus 로고
    • Syntabulin-mediated anterograde transport of mitochondria along neuronal processes
    • Cai Q., Gerwin C., and Sheng Z.H. Syntabulin-mediated anterograde transport of mitochondria along neuronal processes. J. Cell Biol. 170 (2005) 959-969
    • (2005) J. Cell Biol. , vol.170 , pp. 959-969
    • Cai, Q.1    Gerwin, C.2    Sheng, Z.H.3
  • 7
    • 0037137704 scopus 로고    scopus 로고
    • Axonal transport of mitochondria to synapses depends on Milton, a novel Drosophila protein
    • Stowers R.S., Megeath L.J., Gorska-Andrzejak J., Meinertzhagen I.A., and Schwarz T.L. Axonal transport of mitochondria to synapses depends on Milton, a novel Drosophila protein. Neuron 36 (2002) 1063-1077
    • (2002) Neuron , vol.36 , pp. 1063-1077
    • Stowers, R.S.1    Megeath, L.J.2    Gorska-Andrzejak, J.3    Meinertzhagen, I.A.4    Schwarz, T.L.5
  • 8
    • 28444496758 scopus 로고    scopus 로고
    • APLIP1, a kinesin binding JIP-1/JNK scaffold protein, influences the axonal transport of both vesicles and mitochondria in Drosophila
    • Horiuchi D., Barkus R.V., Pilling A.D., Gassman A., and Saxton W.M. APLIP1, a kinesin binding JIP-1/JNK scaffold protein, influences the axonal transport of both vesicles and mitochondria in Drosophila. Curr. Biol. 15 (2005) 2137-2141
    • (2005) Curr. Biol. , vol.15 , pp. 2137-2141
    • Horiuchi, D.1    Barkus, R.V.2    Pilling, A.D.3    Gassman, A.4    Saxton, W.M.5
  • 9
    • 0019796509 scopus 로고
    • Body weight and dietary factors in Huntington's disease patients compared with matched controls
    • Sanberg P.R., Fibiger H.C., and Mark R.F. Body weight and dietary factors in Huntington's disease patients compared with matched controls. Med. J. Aust. 1 (1981) 407-409
    • (1981) Med. J. Aust. , vol.1 , pp. 407-409
    • Sanberg, P.R.1    Fibiger, H.C.2    Mark, R.F.3
  • 10
    • 0019991784 scopus 로고
    • Cerebral metabolism and atrophy in Huntington's disease determined by 18FDG and computed tomographic scan
    • Kuhl D.E., Phelps M.E., Markham C.H., Metter E.J., Riege W.H., and Winter J. Cerebral metabolism and atrophy in Huntington's disease determined by 18FDG and computed tomographic scan. Ann. Neurol. 12 (1982) 425-434
    • (1982) Ann. Neurol. , vol.12 , pp. 425-434
    • Kuhl, D.E.1    Phelps, M.E.2    Markham, C.H.3    Metter, E.J.4    Riege, W.H.5    Winter, J.6
  • 12
  • 15
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin M.T., and Beal M.F. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443 (2006) 787-795
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 16
    • 34247158550 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial dysfunction in neurodegenerative diseases
    • Trushina E., and McMurray C.T. Oxidative stress and mitochondrial dysfunction in neurodegenerative diseases. Neuroscience 145 (2007) 1233-1248
    • (2007) Neuroscience , vol.145 , pp. 1233-1248
    • Trushina, E.1    McMurray, C.T.2
  • 17
    • 1242338856 scopus 로고    scopus 로고
    • Huntingtin-protein interactions and the pathogenesis of Huntington's disease
    • Li S.H., and Li X.J. Huntingtin-protein interactions and the pathogenesis of Huntington's disease. Trends Genet. 20 (2004) 146-154
    • (2004) Trends Genet. , vol.20 , pp. 146-154
    • Li, S.H.1    Li, X.J.2
  • 19
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • Cui L., Jeong H., Borovecki F., Parkhurst C.N., Tanese N., and Krainc D. Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration. Cell 127 (2006) 59-69
    • (2006) Cell , vol.127 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 22
    • 3543141113 scopus 로고    scopus 로고
    • Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release
    • Choo Y.S., Johnson G.V., MacDonald M., Detloff P.J., and Lesort M. Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release. Hum. Mol. Genet. 13 (2004) 1407-1420
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1407-1420
    • Choo, Y.S.1    Johnson, G.V.2    MacDonald, M.3    Detloff, P.J.4    Lesort, M.5
  • 23
    • 31444432457 scopus 로고    scopus 로고
    • Polyglutamine expansion inhibits respiration by increasing reactive oxygen species in isolated mitochondria
    • Puranam K.L., Wu G., Strittmatter W.J., and Burke J.R. Polyglutamine expansion inhibits respiration by increasing reactive oxygen species in isolated mitochondria. Biochem. Biophys. Res. Commun. 341 (2006) 607-613
    • (2006) Biochem. Biophys. Res. Commun. , vol.341 , pp. 607-613
    • Puranam, K.L.1    Wu, G.2    Strittmatter, W.J.3    Burke, J.R.4
  • 24
    • 33646136884 scopus 로고    scopus 로고
    • Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons
    • Chang D.T., Rintoul G.L., Pandipati S., and Reynolds I.J. Mutant huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons. Neurobiol. Dis. 22 (2006) 388-400
    • (2006) Neurobiol. Dis. , vol.22 , pp. 388-400
    • Chang, D.T.1    Rintoul, G.L.2    Pandipati, S.3    Reynolds, I.J.4
  • 30
    • 0041632303 scopus 로고    scopus 로고
    • Lack of huntingtin-associated protein-1 causes neuronal death resembling hypothalamic degeneration in Huntington's disease
    • Li S.H., Yu Z.X., Li C.L., Nguyen H.P., Zhou Y.X., Deng C., and Li X.J. Lack of huntingtin-associated protein-1 causes neuronal death resembling hypothalamic degeneration in Huntington's disease. J. Neurosci. 23 (2003) 6956-6964
    • (2003) J. Neurosci. , vol.23 , pp. 6956-6964
    • Li, S.H.1    Yu, Z.X.2    Li, C.L.3    Nguyen, H.P.4    Zhou, Y.X.5    Deng, C.6    Li, X.J.7
  • 33
    • 33645642673 scopus 로고    scopus 로고
    • Interaction of Huntingtin-associated protein-1 with kinesin light chain: implications in intracellular trafficking in neurons
    • McGuire J.R., Rong J., Li S.H., and Li X.J. Interaction of Huntingtin-associated protein-1 with kinesin light chain: implications in intracellular trafficking in neurons. J. Biol. Chem. 281 (2006) 3552-3559
    • (2006) J. Biol. Chem. , vol.281 , pp. 3552-3559
    • McGuire, J.R.1    Rong, J.2    Li, S.H.3    Li, X.J.4
  • 35
    • 33646117742 scopus 로고    scopus 로고
    • The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking
    • Fransson S., Ruusala A., and Aspenstrom P. The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking. Biochem. Biophys. Res. Commun. 344 (2006) 500-510
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 500-510
    • Fransson, S.1    Ruusala, A.2    Aspenstrom, P.3
  • 36
    • 33646768127 scopus 로고    scopus 로고
    • Axonal transport of mitochondria requires Milton to recruit kinesin heavy chain and is light chain independent
    • Glater E.E., Megeath L.J., Stowers R.S., and Schwarz T.L. Axonal transport of mitochondria requires Milton to recruit kinesin heavy chain and is light chain independent. J. Cell Biol. 173 (2006) 545-557
    • (2006) J. Cell Biol. , vol.173 , pp. 545-557
    • Glater, E.E.1    Megeath, L.J.2    Stowers, R.S.3    Schwarz, T.L.4
  • 37
    • 49149112606 scopus 로고    scopus 로고
    • Huntingtin phosphorylation acts as a molecular switch for anterograde/retrograde transport in neurons
    • Colin E., Zala D., Liot G., Rangone H., Borrell-Pages M., Li X.J., Saudou F., and Humbert S. Huntingtin phosphorylation acts as a molecular switch for anterograde/retrograde transport in neurons. EMBO J. 27 (2008) 2124-2134
    • (2008) EMBO J. , vol.27 , pp. 2124-2134
    • Colin, E.1    Zala, D.2    Liot, G.3    Rangone, H.4    Borrell-Pages, M.5    Li, X.J.6    Saudou, F.7    Humbert, S.8
  • 40
    • 0141891952 scopus 로고    scopus 로고
    • Huntingtin forms toxic NH2-terminal fragment complexes that are promoted by the age-dependent decrease in proteasome activity
    • Zhou H., Cao F., Wang Z., Yu Z.X., Nguyen H.P., Evans J., Li S.H., and Li X.J. Huntingtin forms toxic NH2-terminal fragment complexes that are promoted by the age-dependent decrease in proteasome activity. J. Cell Biol. 163 (2003) 109-118
    • (2003) J. Cell Biol. , vol.163 , pp. 109-118
    • Zhou, H.1    Cao, F.2    Wang, Z.3    Yu, Z.X.4    Nguyen, H.P.5    Evans, J.6    Li, S.H.7    Li, X.J.8
  • 41
    • 34248166420 scopus 로고    scopus 로고
    • Multiple pathways contribute to the pathogenesis of Huntington disease
    • Li S., and Li X.J. Multiple pathways contribute to the pathogenesis of Huntington disease. Mol. Neurodegener. 1 (2006) 19
    • (2006) Mol. Neurodegener. , vol.1 , pp. 19
    • Li, S.1    Li, X.J.2
  • 42
    • 33747074063 scopus 로고    scopus 로고
    • Neurodegenerative disease: cut to the chase
    • Ellerby L.M., and Orr H.T. Neurodegenerative disease: cut to the chase. Nature 442 (2006) 641-642
    • (2006) Nature , vol.442 , pp. 641-642
    • Ellerby, L.M.1    Orr, H.T.2
  • 45
    • 41549129945 scopus 로고    scopus 로고
    • Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice
    • Wang J., Wang C.E., Orr A., Tydlacka S., Li S.H., and Li X.J. Impaired ubiquitin-proteasome system activity in the synapses of Huntington's disease mice. J. Cell Biol. 180 (2008) 1177-1189
    • (2008) J. Cell Biol. , vol.180 , pp. 1177-1189
    • Wang, J.1    Wang, C.E.2    Orr, A.3    Tydlacka, S.4    Li, S.H.5    Li, X.J.6
  • 46
    • 0034881326 scopus 로고    scopus 로고
    • Inter-mitochondrial complementation: mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA
    • Nakada K., Inoue K., Ono T., Isobe K., Ogura A., Goto Y.I., Nonaka I., and Hayashi J.I. Inter-mitochondrial complementation: mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA. Nat. Med. 7 (2001) 934-940
    • (2001) Nat. Med. , vol.7 , pp. 934-940
    • Nakada, K.1    Inoue, K.2    Ono, T.3    Isobe, K.4    Ogura, A.5    Goto, Y.I.6    Nonaka, I.7    Hayashi, J.I.8
  • 47
    • 0034938453 scopus 로고    scopus 로고
    • Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria
    • Ono T., Isobe K., Nakada K., and Hayashi J.I. Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria. Nat. Genet. 28 (2001) 272-275
    • (2001) Nat. Genet. , vol.28 , pp. 272-275
    • Ono, T.1    Isobe, K.2    Nakada, K.3    Hayashi, J.I.4
  • 48
    • 58149380769 scopus 로고    scopus 로고
    • Differential activities of the ubiquitin-proteasome system in neurons versus glia may account for the preferential accumulation of misfolded proteins in neurons
    • Tydlacka S., Wang C.E., Wang X., Li S., and Li X.J. Differential activities of the ubiquitin-proteasome system in neurons versus glia may account for the preferential accumulation of misfolded proteins in neurons. J. Neurosci. 28 (2008) 13285-13295
    • (2008) J. Neurosci. , vol.28 , pp. 13285-13295
    • Tydlacka, S.1    Wang, C.E.2    Wang, X.3    Li, S.4    Li, X.J.5
  • 49
    • 44649113841 scopus 로고    scopus 로고
    • Suppression of neuropil aggregates and neurological symptoms by an intracellular antibody implicates the cytoplasmic toxicity of mutant huntingtin
    • Wang C.E., Zhou H., McGuire J.R., Cerullo V., Lee B., Li S.H., and Li X.J. Suppression of neuropil aggregates and neurological symptoms by an intracellular antibody implicates the cytoplasmic toxicity of mutant huntingtin. J. Cell Biol. 181 (2008) 803-816
    • (2008) J. Cell Biol. , vol.181 , pp. 803-816
    • Wang, C.E.1    Zhou, H.2    McGuire, J.R.3    Cerullo, V.4    Lee, B.5    Li, S.H.6    Li, X.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.