메뉴 건너뛰기




Volumn 1, Issue 1, 2012, Pages 71-87

Deletion of the huntingtin proline-rich region does not significantly affect normal huntingtin function in mice

Author keywords

huntingtin; Huntington's disease; mouse model; proline rich region

Indexed keywords

HUNTINGTIN; PROLINE; PROLINE RICH REGION; UNCLASSIFIED DRUG; HDH PROTEIN, MOUSE; NERVE PROTEIN; NUCLEAR PROTEIN;

EID: 84892929669     PISSN: 18796397     EISSN: 18796400     Source Type: Journal    
DOI: 10.3233/JHD-2012-120016     Document Type: Article
Times cited : (22)

References (59)
  • 1
    • 0030036206 scopus 로고    scopus 로고
    • Sequence analysis of the CAG triplet repeats region in the Huntington disease gene (IT15) in several mammalian species
    • Pecheux C, Gall AL, Kaplan JC, Dode C. Sequence analysis of the CAG triplet repeats region in the Huntington disease gene (IT15) in several mammalian species. Ann Genet. 1996;39(2):81-6.
    • (1996) Ann Genet , vol.39 , Issue.2 , pp. 81-86
    • Pecheux, C.1    Gall, A.L.2    Kaplan, J.C.3    Dode, C.4
  • 2
    • 0032517139 scopus 로고    scopus 로고
    • Characterization of the Huntington's disease (HD) gene homolog in the zebrafish Danio rerio
    • DOI 10.1016/S0378-1119(98)00342-4, PII S0378111998003424
    • Karlovich CA, John RM, Ramirez L, Stainier DY, Myers RM. Characterization of the Huntington's disease (HD) gene homologue in the zebrafish Danio rerio. Gene. 1998;217 (1-2):117-25. (Pubitemid 28427314)
    • (1998) Gene , vol.217 , Issue.1-2 , pp. 117-125
    • Karlovich, C.A.1    John, R.M.2    Ramirez, L.3    Stainier, D.Y.R.4    Myers, R.M.5
  • 4
    • 0032855148 scopus 로고    scopus 로고
    • A putative Drosophila homolog of the Huntington's disease gene
    • DOI 10.1093/hmg/8.9.1807
    • Li Z, Karlovich CA, Fish MP, Scott MP,MyersRM. Aputative Drosophila homolog of the Huntington's disease gene. Hum Mol Genet. 1999;8(9):1807-15. (Pubitemid 29423893)
    • (1999) Human Molecular Genetics , vol.8 , Issue.9 , pp. 1807-1815
    • Li, Z.1    Karlovich, C.A.2    Fish, M.P.3    Scott, M.P.4    Myers, R.M.5
  • 5
    • 33751193268 scopus 로고    scopus 로고
    • Huntingtin gene evolution in Chordata and its peculiar features in the ascidian Ciona genus
    • Gissi C, Pesole G, Cattaneo E, Tartari M. Huntingtin gene evolution in Chordata and its peculiar features in the ascidian Ciona genus. BMC Genomics. 2006;7:288.
    • (2006) BMC Genomics , vol.7 , pp. 288
    • Gissi, C.1    Pesole, G.2    Cattaneo, E.3    Tartari, M.4
  • 6
    • 35448994487 scopus 로고    scopus 로고
    • Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity
    • DOI 10.1093/hmg/ddm217
    • Atwal RS, Xia J, Pinchev D, Taylor J, Epand RM, Truant R. Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity. Hum Mol Genet. 2007;16(21):2600-15. (Pubitemid 47617727)
    • (2007) Human Molecular Genetics , vol.16 , Issue.21 , pp. 2600-2615
    • Atwal, R.S.1    Xia, J.2    Pinchev, D.3    Taylor, J.4    Epand, R.M.5    Truant, R.6
  • 11
    • 33751282353 scopus 로고    scopus 로고
    • Huntington's disease: From huntingtin function and dysfunction to therapeutic strategies
    • DOI 10.1007/s00018-006-6242-0
    • Borrell-Pages M, Zala D, Humbert S, Saudou F. Huntington's disease: from huntingtin function and dysfunction to therapeutic strategies. Cell Mol Life Sci. 2006;63(22): 2642-60. (Pubitemid 44800717)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.22 , pp. 2642-2660
    • Borrell-Pages, M.1    Zala, D.2    Humbert, S.3    Saudou, F.4
  • 12
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell. 1993;72(6):971-83.
    • (1993) Cell , vol.72 , Issue.6 , pp. 971-983
  • 13
    • 0028049296 scopus 로고
    • Sequence of the murine Huntington disease gene: Evidence for conservation, and polymorphism in a triplet (CCG) repeat alternate splicing
    • Lin B, Nasir J, MacDonald H, Hutchinson G, Graham RK, Rommens JM, Hayden MR. Sequence of the murine Huntington disease gene: evidence for conservation, alternate splicing and polymorphism in a triplet (CCG) repeat [corrected] . Hum Mol Genet. 1994;3(1):85-92. (Pubitemid 24038149)
    • (1994) Human Molecular Genetics , vol.3 , Issue.1 , pp. 85-92
    • Lin, B.1    Nasir, J.2    MacDonald, H.3    Hutchinson, G.4    Graham, R.K.5    Rommens, J.M.6    Hayden, M.R.7
  • 15
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay BK,Williamson MP, Sudol M. The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. Faseb J. 2000;14(2):231-41. (Pubitemid 30086060)
    • (2000) FASEB Journal , vol.14 , Issue.2 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 16
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson MP. The structure and function of proline-rich regions in proteins. Biochem J. 1994;297(Pt 2):249-60. (Pubitemid 24026414)
    • (1994) Biochemical Journal , vol.297 , Issue.2 , pp. 249-260
    • Williamson, M.P.1
  • 18
    • 35648936428 scopus 로고    scopus 로고
    • Flanking Polyproline Sequences Inhibit β-Sheet Structure in Polyglutamine Segments by Inducing PPII-like Helix Structure
    • DOI 10.1016/j.jmb.2007.09.023, PII S0022283607011977
    • Darnell G, Orgel JP, Pahl R, Meredith SC. Flanking polyproline sequences inhibit beta-sheet structure in polyglutamine segments by inducing PPII-like helix structure. J Mol Biol. 2007;374(3):688-704. (Pubitemid 350027728)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.3 , pp. 688-704
    • Darnell, G.1    Orgel, J.P.R.O.2    Pahl, R.3    Meredith, S.C.4
  • 19
    • 77954616668 scopus 로고    scopus 로고
    • Polyglutamine induced misfolding of huntingtin exon1 is modulated by the flanking sequences
    • Lakhani VV, Ding F, Dokholyan NV. Polyglutamine induced misfolding of huntingtin exon1 is modulated by the flanking sequences. PLoS Comput Biol. 2010;6(4):e1000772.
    • (2010) PLoS Comput Biol , vol.6 , Issue.4
    • Lakhani, V.V.1    Ding, F.2    Dokholyan, N.V.3
  • 20
  • 21
    • 39449105711 scopus 로고    scopus 로고
    • Mutant huntingtin can paradoxically protect neurons from death
    • DOI 10.1038/sj.cdd.4402261, PII 4402261
    • Zuchner T, Brundin P. Mutant huntingtin can paradoxically protect neurons from death. Cell Death Differ. 2008; 15(3):435-42. (Pubitemid 351267294)
    • (2008) Cell Death and Differentiation , vol.15 , Issue.3 , pp. 435-442
    • Zuchner, T.1    Brundin, P.2
  • 23
    • 33845204276 scopus 로고    scopus 로고
    • Structural Insights into the Specific Binding of Huntingtin Proline-Rich Region with the SH3 and WW Domains
    • DOI 10.1016/j.str.2006.09.014, PII S0969212606004035
    • Gao YG, Yan XZ, Song AX, Chang YG, Gao XC, Jiang N, Zhang Q, Hu HY. Structural Insights into the specific binding of huntingtin proline-rich region with the SH3 and WW domains. Structure. 2006;14(12):1755-65. (Pubitemid 44855626)
    • (2006) Structure , vol.14 , Issue.12 , pp. 1755-1765
    • Gao, Y.-G.1    Yan, X.-Z.2    Song, A.-X.3    Chang, Y.-G.4    Gao, X.-C.5    Jiang, N.6    Zhang, Q.7    Hu, H.-Y.8
  • 24
    • 0000790724 scopus 로고    scopus 로고
    • SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes
    • DOI 10.1074/jbc.272.13.8121
    • Liu YF, Deth RC, Devys D. SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes. J Biol Chem. 1997;272(13):8121-4. (Pubitemid 27147757)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.13 , pp. 8121-8124
    • Liu, Y.F.1    Deth, R.C.2    Devys, D.3
  • 25
    • 0036796261 scopus 로고    scopus 로고
    • PACSIN 1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntington's disease brains
    • Modregger J, DiProspero NA, Charles V, Tagle DA, Plomann M. PACSIN 1 interacts with huntingtin and is absent from synaptic varicosities in presymptomatic Huntington's disease brains. Hum Mol Genet. 2002;11(21):2547-58. (Pubitemid 35174685)
    • (2002) Human Molecular Genetics , vol.11 , Issue.21 , pp. 2547-2558
    • Modregger, J.1    DiProspero, N.A.2    Charles, V.3    Tagle, D.A.4    Plomann, M.5
  • 26
    • 0034284565 scopus 로고    scopus 로고
    • Huntingtin's WW domain partners in Huntington's disease post-mortem brain fulfill genetic criteria for direct involvement in Huntington's disease pathogenesis
    • Passani LA, Bedford MT, Faber PW, McGinnis KM, Sharp AH, Gusella JF, Vonsattel JP, MacDonald ME. Huntingtin's WW domain partners in Huntington's disease post-mortem brain fulfill genetic criteria for direct involvement in Huntington's disease pathogenesis. Hum Mol Genet. 2000;9(14):2175-82.
    • (2000) Hum Mol Genet , vol.9 , Issue.14 , pp. 2175-2182
    • Passani, L.A.1    Bedford, M.T.2    Faber, P.W.3    McGinnis, K.M.4    Sharp, A.H.5    Gusella, J.F.6    Vonsattel, J.P.7    Macdonald, M.E.8
  • 30
    • 24044540256 scopus 로고    scopus 로고
    • Specificity and versatility of SH3 and other proline-recognition domains: Structural basis and implications for cellular signal transduction
    • DOI 10.1042/BJ20050411
    • Li SS. Specificity and versatility of SH3 and other prolinerecognition domains: structural basis and implications for cellular signal transduction. Biochem J. 2005;390(Pt 3):641-53. (Pubitemid 41395346)
    • (2005) Biochemical Journal , vol.390 , Issue.3 , pp. 641-653
    • Li, S.S.-C.1
  • 31
    • 0037138411 scopus 로고    scopus 로고
    • WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
    • DOI 10.1016/S0014-5793(01)03290-2, PII S0014579301032902
    • Macias MJ,Wiesner S, Sudol M. WWand SH3 domains, two different scaffolds to recognize proline-rich ligands. FEBS Lett. 2002;513(1):30-7. (Pubitemid 34242975)
    • (2002) FEBS Letters , vol.513 , Issue.1 , pp. 30-37
    • Macias, M.J.1    Wiesner, S.2    Sudol, M.3
  • 32
    • 4644307407 scopus 로고    scopus 로고
    • Activation of the IκB kinase complex and nuclear factor-κB contributes to mutant huntingtin neurotoxicity
    • DOI 10.1523/JNEUROSCI.2675-04.2004
    • Khoshnan A,Ko J,Watkin EE, Paige LA, Reinhart PH, Patterson PH. Activation of the IkappaB kinase complex and nuclear factor-kappaB contributes to mutant huntingtin neurotoxicity. J Neurosci. 2004;24(37):7999-8008. (Pubitemid 39280819)
    • (2004) Journal of Neuroscience , vol.24 , Issue.37 , pp. 7999-8008
    • Khoshnan, A.1    Ko, J.2    Watkin, E.E.3    Paige, L.A.4    Reinhart, P.H.5    Patterson, P.H.6
  • 34
    • 55549105778 scopus 로고    scopus 로고
    • Triggering aggresome formation. Dissecting aggresome-targeting and aggregation signals in synphilin 1
    • Zaarur N, Meriin AB, Gabai VL, Sherman MY. Triggering aggresome formation. Dissecting aggresome-targeting and aggregation signals in synphilin 1. J Biol Chem. 2008; 283(41):27575-84.
    • (2008) J Biol Chem , vol.283 , Issue.41 , pp. 27575-27584
    • Zaarur, N.1    Meriin, A.B.2    Gabai, V.L.3    Sherman, M.Y.4
  • 35
    • 32144455692 scopus 로고    scopus 로고
    • Deletion of the triplet repeat encoding polyglutamine within the mouse Huntington's disease gene results in subtle behavioral/motor phenotypes in vivo and elevated levels of ATP with cellular senescence in vitro
    • DOI 10.1093/hmg/ddi477
    • Clabough EB, Zeitlin SO. Deletion of the triplet repeat encoding polyglutamine within the mouse Huntington's disease gene results in subtle behavioral/motor phenotypes in vivo and elevated levels of ATP with cellular senescence in vitro. Hum Mol Genet. 2006;15(4):607-23. (Pubitemid 43205425)
    • (2006) Human Molecular Genetics , vol.15 , Issue.4 , pp. 607-623
    • Clabough, E.B.D.1    Zeitlin, S.O.2
  • 37
    • 0034971846 scopus 로고    scopus 로고
    • Nuclear relocation of normal huntingtin
    • DOI 10.1034/j.1600-0854.2001.002006385.x
    • Tao T, Tartakoff AM. Nuclear relocation of normal huntingtin. Traffic. 2001;2(6):385-94. (Pubitemid 32574005)
    • (2001) Traffic , vol.2 , Issue.6 , pp. 385-394
    • Tao, T.1    Tartakoff, A.M.2
  • 38
    • 35348980793 scopus 로고    scopus 로고
    • Nucleocytoplasmic trafficking and transcription effects of huntingtin in Huntington's disease
    • DOI 10.1016/j.pneurobio.2006.11.004, PII S0301008206001547, Chromatin Dysfunction in Huntington's Disease
    • Truant R, Atwal RS, Burtnik A. Nucleocytoplasmic trafficking and transcription effects of huntingtin in Huntington's disease. Prog Neurobiol. 2007;83(4):211-27. (Pubitemid 47595404)
    • (2007) Progress in Neurobiology , vol.83 , Issue.4 , pp. 211-227
    • Truant, R.1    Atwal, R.S.2    Burtnik, A.3
  • 39
    • 38049053467 scopus 로고    scopus 로고
    • A stress sensitive ER membraneassociation domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy
    • Atwal RS, Truant R. A stress sensitive ER membraneassociation domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy. Autophagy. 2008;4(1):91-3.
    • (2008) Autophagy , vol.4 , Issue.1 , pp. 91-93
    • Atwal, R.S.1    Truant, R.2
  • 43
    • 0033757718 scopus 로고    scopus 로고
    • Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice
    • Dragatsis I, Levine MS, Zeitlin S. Inactivation of Hdh in the brain and testis results in progressive neurodegeneration and sterility in mice. Nat Genet. 2000;26(3):300-6.
    • (2000) Nat Genet , vol.26 , Issue.3 , pp. 300-306
    • Dragatsis, I.1    Levine, M.S.2    Zeitlin, S.3
  • 44
    • 54049111928 scopus 로고    scopus 로고
    • Intrabodies binding the proline-rich domains of mutant huntingtin increase its turnover and reduce neurotoxicity
    • Southwell AL, Khoshnan A, Dunn DE, Bugg CW, Lo DC, Patterson PH. Intrabodies binding the proline-rich domains of mutant huntingtin increase its turnover and reduce neurotoxicity. J Neurosci. 2008;28(36):9013-20.
    • (2008) J Neurosci , vol.28 , Issue.36 , pp. 9013-9020
    • Southwell, A.L.1    Khoshnan, A.2    Dunn, D.E.3    Bugg, C.W.4    Lo, D.C.5    Patterson, P.H.6
  • 45
    • 33846025461 scopus 로고    scopus 로고
    • Critical role of the proline-rich region in Huntingtin for aggregation and cytotoxicity in yeast
    • DOI 10.1074/jbc.M605558200
    • Dehay B, Bertolotti A. Critical role of the proline-rich region in Huntingtin for aggregation and cytotoxicity in yeast. J Biol Chem. 2006;281(47):35608-15. (Pubitemid 46041291)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.47 , pp. 35608-35615
    • Dehay, B.1    Bertolotti, A.2
  • 48
    • 77649219699 scopus 로고    scopus 로고
    • Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice
    • Zheng S, Clabough EB, Sarkar S, Futter M, Rubinsztein DC, Zeitlin SO. Deletion of the huntingtin polyglutamine stretch enhances neuronal autophagy and longevity in mice. PLoS Genet. 2010;6(2):e1000838.
    • (2010) PLoS Genet , vol.6 , Issue.2
    • Zheng, S.1    Clabough, E.B.2    Sarkar, S.3    Futter, M.4    Rubinsztein, D.C.5    Zeitlin, S.O.6
  • 51
    • 33846906945 scopus 로고    scopus 로고
    • Sex differences in behavior and striatal ascorbate release in the 140 CAG knock-in mouse model of Huntington's disease
    • DOI 10.1016/j.bbr.2006.12.004, PII S0166432806006954
    • Dorner JL, Miller BR, Barton SJ, Brock TJ, Rebec GV. Sex differences in behavior and striatal ascorbate release in the 140 CAG knock-in mouse model of Huntington's disease. Behav Brain Res. 2007;178(1):90-7. (Pubitemid 46240343)
    • (2007) Behavioural Brain Research , vol.178 , Issue.1 , pp. 90-97
    • Dorner, J.L.1    Miller, B.R.2    Barton, S.J.3    Brock, T.J.4    Rebec, G.V.5
  • 53
    • 47049115892 scopus 로고    scopus 로고
    • Sex-dependent effect of BAG1 in ameliorating motor deficits of Huntington disease transgenic mice
    • Orr AL, Huang S, Roberts MA, Reed JC, Li S, Li XJ. Sex-dependent effect of BAG1 in ameliorating motor deficits of Huntington disease transgenic mice. J Biol Chem. 2008;283(23):16027-36.
    • (2008) J Biol Chem , vol.283 , Issue.23 , pp. 16027-16036
    • Orr, A.L.1    Huang, S.2    Roberts, M.A.3    Reed, J.C.4    Li, S.5    Li, X.J.6
  • 56
    • 19744380273 scopus 로고    scopus 로고
    • Loss of wild-type huntingtin influences motor dysfunction and survival in the YAC128 mouse model of Huntington disease
    • DOI 10.1093/hmg/ddi147
    • Van Raamsdonk JM, Pearson J, Rogers DA, Bissada N, Vogl AW, Hayden MR, Leavitt BR. Loss of wild-type huntingtin influences motor dysfunction and survival in the YAC128 mouse model of Huntington disease. Hum Mol Genet. 2005;14(10):1379-92. (Pubitemid 40744495)
    • (2005) Human Molecular Genetics , vol.14 , Issue.10 , pp. 1379-1392
    • Van Raamsdonk, J.M.1    Pearson, J.2    Rogers, D.A.3    Bissada, N.4    Vogl, A.W.5    Hayden, M.R.6    Leavitt, B.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.