메뉴 건너뛰기




Volumn 203, Issue 2, 2007, Pages 531-541

Parkin is an E3 ubiquitin-ligase for normal and mutant ataxin-2 and prevents ataxin-2-induced cell death

Author keywords

AR JP; Ataxin 2; Parkin; Parkinson's disease; SCA2

Indexed keywords

ATAXIN 2; GENE PRODUCT; MUTANT PROTEIN; PARKIN; POLYGLUTAMINE; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 33846545106     PISSN: 00144886     EISSN: 10902430     Source Type: Journal    
DOI: 10.1016/j.expneurol.2006.09.009     Document Type: Article
Times cited : (44)

References (49)
  • 3
    • 33745593049 scopus 로고    scopus 로고
    • Activity-dependent dynamics and sequestration of proteasomes in dendritic spines
    • Bingol B., and Schuman E.M. Activity-dependent dynamics and sequestration of proteasomes in dendritic spines. Nature 441 (2006) 1144-1148
    • (2006) Nature , vol.441 , pp. 1144-1148
    • Bingol, B.1    Schuman, E.M.2
  • 4
    • 0034776095 scopus 로고    scopus 로고
    • Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease
    • Chung K.K., Zhang Y., Lim K.L., Tanaka Y., Huang H., Gao J., Ross C.A., Dawson V.L., and Dawson T.M. Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. Nat. Med. 7 (2001) 1144-1150
    • (2001) Nat. Med. , vol.7 , pp. 1144-1150
    • Chung, K.K.1    Zhang, Y.2    Lim, K.L.3    Tanaka, Y.4    Huang, H.5    Gao, J.6    Ross, C.A.7    Dawson, V.L.8    Dawson, T.M.9
  • 6
    • 0035394668 scopus 로고    scopus 로고
    • Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
    • Cummings C.J., Sun Y., Opal P., Antalffy B., Mestril R., Orr H.T., Dillmann W.H., and Zoghbi H.Y. Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum. Mol. Genet. 10 (2001) 1511-1518
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1511-1518
    • Cummings, C.J.1    Sun, Y.2    Opal, P.3    Antalffy, B.4    Mestril, R.5    Orr, H.T.6    Dillmann, W.H.7    Zoghbi, H.Y.8
  • 8
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., Sapp E., Chase K.O., Davies S.W., Bates G.P., Vonsattel J.P., and Aronin N. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277 (1997) 1990-1993
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 11
    • 0033044001 scopus 로고    scopus 로고
    • Expression of ataxin-2 in brains from normal individuals and patients with Alzheimer's disease and spinocerebellar ataxia 2
    • Huynh D.P., Del Bigio M.R., Ho D.H., and Pulst S.M. Expression of ataxin-2 in brains from normal individuals and patients with Alzheimer's disease and spinocerebellar ataxia 2. Ann. Neurol. 45 (1999) 232-241
    • (1999) Ann. Neurol. , vol.45 , pp. 232-241
    • Huynh, D.P.1    Del Bigio, M.R.2    Ho, D.H.3    Pulst, S.M.4
  • 12
    • 0033811788 scopus 로고    scopus 로고
    • Nuclear localization or inclusion body formation of ataxin-2 are not necessary for SCA2 pathogenesis in mouse or human
    • Huynh D.P., Figueroa K., Hoang N., and Pulst S.M. Nuclear localization or inclusion body formation of ataxin-2 are not necessary for SCA2 pathogenesis in mouse or human. Nat. Genet. 26 (2000) 44-50
    • (2000) Nat. Genet. , vol.26 , pp. 44-50
    • Huynh, D.P.1    Figueroa, K.2    Hoang, N.3    Pulst, S.M.4
  • 13
    • 0033767459 scopus 로고    scopus 로고
    • Parkin is associated with actin filaments in neuronal and nonneural cells
    • Huynh D.P., Scoles D.R., Ho T.H., Del Bigio M.R., and Pulst S.M. Parkin is associated with actin filaments in neuronal and nonneural cells. Ann. Neurol. 48 (2000) 737-744
    • (2000) Ann. Neurol. , vol.48 , pp. 737-744
    • Huynh, D.P.1    Scoles, D.R.2    Ho, T.H.3    Del Bigio, M.R.4    Pulst, S.M.5
  • 14
    • 0035944547 scopus 로고    scopus 로고
    • Differential expression and tissue distribution of parkin isoforms during mouse development
    • Huynh D.P., Dy M., Nguyen D., Kiehl T.R., and Pulst S.M. Differential expression and tissue distribution of parkin isoforms during mouse development. Brain Res. Dev. Brain Res. 130 (2001) 173-181
    • (2001) Brain Res. Dev. Brain Res. , vol.130 , pp. 173-181
    • Huynh, D.P.1    Dy, M.2    Nguyen, D.3    Kiehl, T.R.4    Pulst, S.M.5
  • 15
    • 0141995596 scopus 로고    scopus 로고
    • The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI
    • Huynh D.P., Scoles D.R., Nguyen D., and Pulst S.M. The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI. Hum. Mol. Genet. 12 (2003) 2587-2597
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2587-2597
    • Huynh, D.P.1    Scoles, D.R.2    Nguyen, D.3    Pulst, S.M.4
  • 16
    • 0037767510 scopus 로고    scopus 로고
    • Expansion of the polyQ repeat in ataxin-2 alters its Golgi localization, disrupts the Golgi complex and causes cell death
    • Huynh D.P., Yang H.T., Vakharia H., Nguyen D., and Pulst S.M. Expansion of the polyQ repeat in ataxin-2 alters its Golgi localization, disrupts the Golgi complex and causes cell death. Hum. Mol. Genet. 12 (2003) 1485-1496
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1485-1496
    • Huynh, D.P.1    Yang, H.T.2    Vakharia, H.3    Nguyen, D.4    Pulst, S.M.5
  • 17
    • 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., and Takahashi R. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105 (2001) 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
  • 18
    • 0347064343 scopus 로고    scopus 로고
    • A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death
    • Imai Y., Soda M., Murakami T., Shoji M., Abe K., and Takahashi R. A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death. J. Biol. Chem. 278 (2003) 51901-51910
    • (2003) J. Biol. Chem. , vol.278 , pp. 51901-51910
    • Imai, Y.1    Soda, M.2    Murakami, T.3    Shoji, M.4    Abe, K.5    Takahashi, R.6
  • 20
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice
    • Klement I.A., Skinner P.J., Kaytor M.D., Yi H., Hersch S.M., Clark H.B., Zoghbi H.Y., and Orr H.T. Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice. Cell 95 (1998) 41-53
    • (1998) Cell , vol.95 , pp. 41-53
    • Klement, I.A.1    Skinner, P.J.2    Kaytor, M.D.3    Yi, H.4    Hersch, S.M.5    Clark, H.B.6    Zoghbi, H.Y.7    Orr, H.T.8
  • 21
    • 33745220302 scopus 로고    scopus 로고
    • Identification of far up stream element binding protein-1 as an authentic parkin substrate
    • Ko H.S., Kim S.W., Sriram S.R., Dawson V.L., and Dawson T.M. Identification of far up stream element binding protein-1 as an authentic parkin substrate. J. Biol. Chem. (2006) 16193-16196
    • (2006) J. Biol. Chem. , pp. 16193-16196
    • Ko, H.S.1    Kim, S.W.2    Sriram, S.R.3    Dawson, V.L.4    Dawson, T.M.5
  • 24
    • 0036786139 scopus 로고    scopus 로고
    • Paradoxical absence of nuclear inclusion in cerebellar Purkinje cells of hereditary ataxias linked to CAG expansion
    • Koyano S., Iwabuchi K., Yagishita S., Kuroiwa Y., and Uchihara T. Paradoxical absence of nuclear inclusion in cerebellar Purkinje cells of hereditary ataxias linked to CAG expansion. J. Neurol., Neurosurg. Psychiatry 73 (2002) 450-452
    • (2002) J. Neurol., Neurosurg. Psychiatry , vol.73 , pp. 450-452
    • Koyano, S.1    Iwabuchi, K.2    Yagishita, S.3    Kuroiwa, Y.4    Uchihara, T.5
  • 26
    • 1842455356 scopus 로고    scopus 로고
    • Parkin genetics: one model for Parkinson's disease
    • Mata I.F., Lockhart P.J., and Farrer M.J. Parkin genetics: one model for Parkinson's disease. Hum. Mol. Genet. 13 Spec No. 1 (2004) R127-R133
    • (2004) Hum. Mol. Genet. , vol.13 , Issue.Spec 1
    • Mata, I.F.1    Lockhart, P.J.2    Farrer, M.J.3
  • 28
    • 0035475788 scopus 로고    scopus 로고
    • SCA1 molecular genetics: a history of a 13 year collaboration against glutamines
    • Orr H.T., and Zoghbi H.Y. SCA1 molecular genetics: a history of a 13 year collaboration against glutamines. Hum. Mol. Genet. 10 (2001) 2307-2311
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2307-2311
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 31
    • 28844439032 scopus 로고    scopus 로고
    • Proteomic analysis of parkin knockout mice: alterations in energy metabolism, protein handling and synaptic function
    • Periquet M., Corti O., Jacquier S., and Brice A. Proteomic analysis of parkin knockout mice: alterations in energy metabolism, protein handling and synaptic function. J. Neurochem. 95 (2005) 1259-1276
    • (2005) J. Neurochem. , vol.95 , pp. 1259-1276
    • Periquet, M.1    Corti, O.2    Jacquier, S.3    Brice, A.4
  • 32
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70 (2001) 503-533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 34
    • 26044439653 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type 2: polyQ repeat variation in the CACNA1A calcium channel modifies age of onset
    • Pulst S.M., Santos N., Wang D., Yang H., Huynh D., Velazquez L., and Figueroa K.P. Spinocerebellar ataxia type 2: polyQ repeat variation in the CACNA1A calcium channel modifies age of onset. Brain 128 (2005) 2297-2303
    • (2005) Brain , vol.128 , pp. 2297-2303
    • Pulst, S.M.1    Santos, N.2    Wang, D.3    Yang, H.4    Huynh, D.5    Velazquez, L.6    Figueroa, K.P.7
  • 36
    • 0037738525 scopus 로고    scopus 로고
    • Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation
    • Ren Y., Zhao J., and Feng J. Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation. J. Neurosci. 23 (2003) 3316-3324
    • (2003) J. Neurosci. , vol.23 , pp. 3316-3324
    • Ren, Y.1    Zhao, J.2    Feng, J.3
  • 39
    • 0035199626 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type 2 presenting as familial levodopa-responsive parkinsonism
    • Shan D.E., Soong B.W., Sun C.M., Lee S.J., Liao K.K., and Liu R.S. Spinocerebellar ataxia type 2 presenting as familial levodopa-responsive parkinsonism. Ann. Neurol. 50 (2001) 812-815
    • (2001) Ann. Neurol. , vol.50 , pp. 812-815
    • Shan, D.E.1    Soong, B.W.2    Sun, C.M.3    Lee, S.J.4    Liao, K.K.5    Liu, R.S.6
  • 43
    • 24144470504 scopus 로고    scopus 로고
    • Familial-associated mutations differentially disrupt the solubility, localization, binding and ubiquitination properties of parkin
    • Sriram S.R., Li X., Ko H.S., Chung K.K., Wong E., Lim K.L., Dawson V.L., and Dawson T.M. Familial-associated mutations differentially disrupt the solubility, localization, binding and ubiquitination properties of parkin. Hum. Mol. Genet. 14 (2005) 2571-2586
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2571-2586
    • Sriram, S.R.1    Li, X.2    Ko, H.S.3    Chung, K.K.4    Wong, E.5    Lim, K.L.6    Dawson, V.L.7    Dawson, T.M.8
  • 44
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Tsai Y.C., Fishman P.S., Thakor N.V., and Oyler G.A. Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J. Biol. Chem. 278 (2003) 22044-22055
    • (2003) J. Biol. Chem. , vol.278 , pp. 22044-22055
    • Tsai, Y.C.1    Fishman, P.S.2    Thakor, N.V.3    Oyler, G.A.4
  • 45
    • 0034887539 scopus 로고    scopus 로고
    • Non-expanded polyglutamine proteins in intranuclear inclusions of hereditary ataxias-triple-labeling immunofluorescence study
    • Uchihara T., Fujigasaki H., Koyano S., Nakamura A., Yagishita S., and Iwabuchi K. Non-expanded polyglutamine proteins in intranuclear inclusions of hereditary ataxias-triple-labeling immunofluorescence study. Acta Neuropathol. (Berl) 102 (2001) 149-152
    • (2001) Acta Neuropathol. (Berl) , vol.102 , pp. 149-152
    • Uchihara, T.1    Fujigasaki, H.2    Koyano, S.3    Nakamura, A.4    Yagishita, S.5    Iwabuchi, K.6
  • 46
    • 0033791230 scopus 로고    scopus 로고
    • Protein aggregation and pathogenesis of Huntington's disease: mechanisms and correlations
    • Wanker E.E. Protein aggregation and pathogenesis of Huntington's disease: mechanisms and correlations. Biol. Chem. 381 (2000) 937-942
    • (2000) Biol. Chem. , vol.381 , pp. 937-942
    • Wanker, E.E.1
  • 47
    • 33750959090 scopus 로고    scopus 로고
    • Proteasome inhibition triggers activity-dependent increase in the size of the recycling vesicle pool in hippocampal neurons
    • Willeumier K., Pulst S.M., and Schweizer F.E. Proteasome inhibition triggers activity-dependent increase in the size of the recycling vesicle pool in hippocampal neurons. J. Neurosci. 26 (2006) 11333-11341
    • (2006) J. Neurosci. , vol.26 , pp. 11333-11341
    • Willeumier, K.1    Pulst, S.M.2    Schweizer, F.E.3
  • 49
    • 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 K.K., Huang H., Dawson V.L., and Dawson T.M. 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 (2000) 13354-13359
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.