메뉴 건너뛰기




Volumn 37, Issue 2, 2005, Pages 198-204

Polyglutamine expansion of huntingtin impairs its nuclear export

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; HUNTINGTIN; MUTANT PROTEIN; NUCLEOPORIN; POLYGLUTAMINE; RAN PROTEIN; RNA; ONCOPROTEIN; PEPTIDE; TPR PROTEIN, HUMAN;

EID: 13944275615     PISSN: 10614036     EISSN: 15461718     Source Type: Journal    
DOI: 10.1038/ng1503     Document Type: Article
Times cited : (143)

References (29)
  • 1
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi, H.Y. & Orr, H.T. Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci. 23, 217-247 (2000).
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 2
    • 0037408279 scopus 로고    scopus 로고
    • Transcriptional abnormalities in Huntington disease
    • Sugars, K.L. & Rubinsztein, D.C. Transcriptional abnormalities in Huntington disease. Trends Genet. 19, 233-238 (2003).
    • (2003) Trends Genet. , vol.19 , pp. 233-238
    • Sugars, K.L.1    Rubinsztein, D.C.2
  • 3
    • 0028989602 scopus 로고
    • Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons
    • DiFiglia, M. et al. Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons. Neuron 14, 1075-1081 (1995).
    • (1995) Neuron , vol.14 , pp. 1075-1081
    • DiFiglia, M.1
  • 4
    • 0029034511 scopus 로고
    • Widespread expression of Huntington's disease gene (IT15) protein product
    • Sharp, A.H. et al. Widespread expression of Huntington's disease gene (IT15) protein product. Neuron 14, 1065-1074 (1995).
    • (1995) Neuron , vol.14 , pp. 1065-1074
    • Sharp, A.H.1
  • 5
    • 0029152808 scopus 로고
    • Identification and localization of huntingtin in brain and human lymphoblastoid cell lines with anti-fusion protein antibodies
    • Gutekunst, C.A. et al. Identification and localization of huntingtin in brain and human lymphoblastoid cell lines with anti-fusion protein antibodies. Proc. Natl. Acad. Sci. USA 92, 8710-8714 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8710-8714
    • Gutekunst, C.A.1
  • 6
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies, S.W. et al. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90, 537-548 (1997).
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1
  • 7
    • 0033054555 scopus 로고    scopus 로고
    • Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin
    • Schilling, G. et al. Intranuclear inclusions and neuritic aggregates in transgenic mice expressing a mutant N-terminal fragment of huntingtin. Hum. Mol. Genet. 8, 397-407 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 397-407
    • Schilling, G.1
  • 8
    • 2542436167 scopus 로고    scopus 로고
    • Modulating huntingtin half-life alters polyglutamine-dependent aggregate formation and cell toxicity
    • Kaytor, M.D., Wilkinson, K.D. & Warren, S.T. Modulating huntingtin half-life alters polyglutamine-dependent aggregate formation and cell toxicity. J. Neurochem. 89, 962-973 (2004).
    • (2004) J. Neurochem. , vol.89 , pp. 962-973
    • Kaytor, M.D.1    Wilkinson, K.D.2    Warren, S.T.3
  • 9
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich, D. & Kutay, U. Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell. Dev. Biol. 15, 607-660 (1999).
    • (1999) Annu. Rev. Cell. Dev. Biol. , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 10
    • 17044457419 scopus 로고
    • Isolation and characterization of the active cDNA of the human cell cycle gene (RCC1) involved in the regulation of onset of chromosome condensation
    • Ohtsubo, M. et al. Isolation and characterization of the active cDNA of the human cell cycle gene (RCC1) involved in the regulation of onset of chromosome condensation. Genes Dev. 1, 585-593 (1987).
    • (1987) Genes Dev. , vol.1 , pp. 585-593
    • Ohtsubo, M.1
  • 11
    • 0030665816 scopus 로고    scopus 로고
    • Nucleocytoplasmic recycling of the nuclear localization signal receptor alpha subunit in vivo is dependent on a nuclear export signal, energy, and RCC1
    • Boche, I. & Fanning, E. Nucleocytoplasmic recycling of the nuclear localization signal receptor alpha subunit in vivo is dependent on a nuclear export signal, energy, and RCC1. J. Cell. Biol. 139, 313-325 (1997).
    • (1997) J. Cell. Biol. , vol.139 , pp. 313-325
    • Boche, I.1    Fanning, E.2
  • 12
    • 0033548099 scopus 로고    scopus 로고
    • beta-subunit of nuclear pore-targeting complex (importin-beta) can be exported from the nucleus in a Ran-independent manner
    • Kose, S., Imamoto, N., Tachibana, T., Yoshida, M. & Yoneda, Y. beta-subunit of nuclear pore-targeting complex (importin-beta) can be exported from the nucleus in a Ran-independent manner. J. Biol. Chem. 274, 3946-3952 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 3946-3952
    • Kose, S.1    Imamoto, N.2    Tachibana, T.3    Yoshida, M.4    Yoneda, Y.5
  • 13
    • 0032910953 scopus 로고    scopus 로고
    • beta-catenin can be transported into the nucleus in a Ran-unassisted manner
    • Yokoya, F., Imamoto, N., Tachibana, T. & Yoneda, Y. beta-catenin can be transported into the nucleus in a Ran-unassisted manner. Mol. Biol. Cell. 10, 1119-1131 (1999).
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 1119-1131
    • Yokoya, F.1    Imamoto, N.2    Tachibana, T.3    Yoneda, Y.4
  • 14
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: Interaction partners tell many different stories
    • Harjes, P. & Wanker, E.E. The hunt for huntingtin function: interaction partners tell many different stories. Trends Biochem. Sci. 28, 425-433 (2003).
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 15
    • 0041353535 scopus 로고    scopus 로고
    • Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes
    • Zuccato, C. et al. Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes. Nat. Genet. 35, 76-83 (2003).
    • (2003) Nat. Genet. , vol.35 , pp. 76-83
    • Zuccato, C.1
  • 16
    • 0028091980 scopus 로고
    • Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex
    • Byrd, D.A. et al. Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex. J. Cell. Biol. 127, 1515-1526 (1994).
    • (1994) J. Cell. Biol. , vol.127 , pp. 1515-1526
    • Byrd, D.A.1
  • 17
    • 0031043895 scopus 로고    scopus 로고
    • Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments
    • Cordes, V.C., Reidenbach, S., Rackwitz, H.R. & Franke, W.W. Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments. J. Cell Biol. 136, 515-529 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 515-529
    • Cordes, V.C.1    Reidenbach, S.2    Rackwitz, H.R.3    Franke, W.W.4
  • 18
    • 0037128215 scopus 로고    scopus 로고
    • Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export
    • Frosst, P., Guan, T., Subauste, C., Hahn, K. & Gerace, L. Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export. J. Cell Biol. 156, 617-630 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 617-630
    • Frosst, P.1    Guan, T.2    Subauste, C.3    Hahn, K.4    Gerace, L.5
  • 19
    • 0036671821 scopus 로고    scopus 로고
    • Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions
    • Lunkes, A. et al. Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions. Mol. Cell 10, 259-269 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 259-269
    • Lunkes, A.1
  • 20
    • 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. et al. Huntingtin forms toxic NH2-terminal fragment complexes that are promoted by the age-dependent decrease in proteasome activity. J. Cell Biol. 163, 109-118 (2003).
    • (2003) J. Cell Biol. , vol.163 , pp. 109-118
    • Zhou, H.1
  • 21
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M. et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990-1993 (1997).
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1
  • 22
    • 0033119123 scopus 로고    scopus 로고
    • Nuclear and neuropil aggregates in Huntington's disease: Relationship to neuropathology
    • Gutekunst, C.A. et al. Nuclear and neuropil aggregates in Huntington's disease: relationship to neuropathology. J. Neurosci. 19, 2522-2534 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 2522-2534
    • Gutekunst, C.A.1
  • 23
    • 0035930598 scopus 로고    scopus 로고
    • Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation
    • Zhou, H., Li, S.H. & Li, X.J. Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation. J. Biol. Chem. 276, 48417-48424 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 48417-48424
    • Zhou, H.1    Li, S.H.2    Li, X.J.3
  • 24
    • 0036870329 scopus 로고    scopus 로고
    • The evolutionary conserved single-copy gene for murine Tpr encodes one prevalent isoform in somatic cells and lacks paralogs in higher eukaryotes
    • Kuznetsov, N.V. et al. The evolutionary conserved single-copy gene for murine Tpr encodes one prevalent isoform in somatic cells and lacks paralogs in higher eukaryotes. Chromosoma 111, 236-255 (2002).
    • (2002) Chromosoma , vol.111 , pp. 236-255
    • Kuznetsov, N.V.1
  • 25
    • 0036241342 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport of proteins and poly(A)+ RNA in reconstituted Tpr-less nuclei in living mammalian cells
    • Shibata, S., Matsuoka, Y. & Yoneda, Y. Nucleocytoplasmic transport of proteins and poly(A)+ RNA in reconstituted Tpr-less nuclei in living mammalian cells. Genes Cells 7, 421-434 (2002).
    • (2002) Genes Cells , vol.7 , pp. 421-434
    • Shibata, S.1    Matsuoka, Y.2    Yoneda, Y.3
  • 26
    • 11144353613 scopus 로고    scopus 로고
    • SUMO modification of Huntingtin and Huntington's disease pathology
    • Steffan, J.S. et al. SUMO modification of Huntingtin and Huntington's disease pathology. Science 304, 100-104 (2004).
    • (2004) Science , vol.304 , pp. 100-104
    • Steffan, J.S.1
  • 27
    • 0037701612 scopus 로고    scopus 로고
    • Huntingtin contains a highly conserved nuclear export signal
    • Xia, J., Lee, D.H., Taylor, J., Vandelft, M. & Truant, R. Huntingtin contains a highly conserved nuclear export signal. Hum. Mol. Genet. 12, 1393-1403 (2003).
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1393-1403
    • Xia, J.1    Lee, D.H.2    Taylor, J.3    Vandelft, M.4    Truant, R.5
  • 28
    • 0038104366 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport signals affect the age at onset of abnormalities in knock-in mice expressing polyglutamine within an ectopic protein context
    • Jackson, W.S., Tallaksen-Greene, S.J., Albin, R.L. & Detloff, P.J. Nucleocytoplasmic transport signals affect the age at onset of abnormalities in knock-in mice expressing polyglutamine within an ectopic protein context. Hum. Mol. Genet. 12, 1621-1629 (2003).
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1621-1629
    • Jackson, W.S.1    Tallaksen-Greene, S.J.2    Albin, R.L.3    Detloff, P.J.4
  • 29
    • 0028803757 scopus 로고
    • A huntingtin-associated protein enriched in brain with implications for pathology
    • Li, X.J. et al. A huntingtin-associated protein enriched in brain with implications for pathology. Nature 378, 398-402 (1995).
    • (1995) Nature , vol.378 , pp. 398-402
    • Li, X.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.