Expansion of the polyQ repeat in ataxin-2 alters its Golgi localization, disrupts the Golgi complex and causes cell death

被引:108
作者
Huynh, DP
Yang, HT
Vakharia, H
Nguyen, D
Pulst, SM
机构
[1] Cedars Sinai Med Ctr, Div Neurol, Los Angeles, CA 90048 USA
[2] Burns & Allen Res Inst, Rose Moss Lab Parkinson & Neurodegenerat Dis, Los Angeles, CA USA
[3] Univ Calif Los Angeles, Sch Med, Dept Med, Los Angeles, CA 90024 USA
[4] Univ Calif Los Angeles, Sch Med, Dept Neurobiol, Los Angeles, CA 90024 USA
关键词
D O I
10.1093/hmg/ddg175
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Spinocerebellar ataxia type 2 (SCA2) is caused by the expansion of a polyglutamine (polyQ) repeat in ataxin-2, the SCA2 gene product. In contrast to other polyQ diseases, intranuclear inclusions are not prominent in SCA2. In animal models with expression of mutant ataxin-2 targeted to Purkinje cells, neuronal dysfunction and morphologic changes are observed without the formation of intranuclear aggregates. In this report, we investigated the mechanisms underlying SCA2 pathogenesis using cellular models. We confirmed that the SCA2 gene product, ataxin-2, was predominantly located in the Golgi apparatus. Deletion of ER-exit and trans-Golgi signals in ataxin-2 resulted in an altered subcellular distribution. Expression of full-length ataxin-2 with an expanded repeat disrupted the normal morphology of the Golgi complex and colocalization with Golgi markers was lost. Intranuclear inclusions were only seen when the polyQ repeat was expanded to 104 glutamines, and even then were only observed in a small minority of cells. Expression of ataxin-2 with expanded repeats in PC12 and COS1 cells increased cell death compared with normal ataxin-2 and elevated the levels of activated caspase-3 and TUNEL-positive cells. These results suggest a link between cell death mediated by mutant ataxin-2 and the stability of the Golgi complex. The formation of intranuclear aggregates is not necessary for in vitro cell death caused by expression of full-length mutant ataxin-2.
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页码:1485 / 1496
页数:12
相关论文
共 44 条
[11]   Spinocerebellar ataxia 2 (SCA2): morphometric analyses in 11 autopsies [J].
Estrada, R ;
Galarraga, J ;
Orozco, G ;
Nodarse, A ;
Auburger, G .
ACTA NEUROPATHOLOGICA, 1999, 97 (03) :306-310
[12]   Polyglutamine-expanded ataxin-7 promotes non-cell-autonomous Purkinje cell degeneration and displays proteolytic cleavage in ataxic transgenic mice [J].
Garden, GA ;
Libby, RT ;
Fu, YH ;
Kinoshita, Y ;
Huang, J ;
Possin, DE ;
Smith, AC ;
Martinez, RA ;
Fine, GC ;
Grote, SK ;
Ware, CB ;
Einum, DD ;
Morrison, RS ;
Ptacek, LJ ;
Sopher, BL ;
La Spada, AR .
JOURNAL OF NEUROSCIENCE, 2002, 22 (12) :4897-4905
[13]   Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract [J].
Goldberg, YP ;
Nicholson, DW ;
Rasper, DM ;
Kalchman, MA ;
Koide, HB ;
Graham, RK ;
Bromm, M ;
KazemiEsfarjani, P ;
Thornberry, NA ;
Vaillancourt, JP ;
Hayden, MR .
NATURE GENETICS, 1996, 13 (04) :442-449
[14]  
Huynh DP, 1999, ANN NEUROL, V45, P232, DOI 10.1002/1531-8249(199902)45:2<232::AID-ANA14>3.0.CO
[15]  
2-7
[16]   Nuclear localization or inclusion body formation of ataxin-2 are not necessary for SCA2 pathogenesis in mouse or human [J].
Huynh, DP ;
Figueroa, K ;
Hoang, N ;
Pulst, SM .
NATURE GENETICS, 2000, 26 (01) :44-50
[17]   Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy [J].
Kegel, KB ;
Kim, M ;
Sapp, E ;
McIntyre, C ;
Castaño, JG ;
Aronin, N ;
DiFiglia, M .
JOURNAL OF NEUROSCIENCE, 2000, 20 (19) :7268-7278
[18]   Ataxin-1 nuclear localization and aggregation:: Role in polyglutamine-induced disease in SCA1 transgenic mice [J].
Klement, IA ;
Skinner, PJ ;
Kaytor, MD ;
Yi, H ;
Hersch, SM ;
Clark, HB ;
Zoghbi, HY ;
Orr, HT .
CELL, 1998, 95 (01) :41-53
[19]   Neuronal intranuclear inclusions in spinocerebellar ataxia type 2: triple-labeling immunofluorescent study [J].
Koyano, S ;
Uchihara, T ;
Fujigasaki, H ;
Nakamura, A ;
Yagishita, S ;
Iwabuchi, K .
NEUROSCIENCE LETTERS, 1999, 273 (02) :117-120
[20]   Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis [J].
Lane, JD ;
Lucocq, J ;
Pryde, J ;
Barr, F ;
Woodman, PG ;
Allan, VJ ;
Lowe, M .
JOURNAL OF CELL BIOLOGY, 2002, 156 (03) :495-509