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.
引用
收藏
页码:1485 / 1496
页数:12
相关论文
共 44 条
[1]   Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis [J].
Chai, YH ;
Shao, JQ ;
Miller, VM ;
Williams, A ;
Paulson, HL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (14) :9310-9315
[2]   Evidence for proteasome involvement in polyglutamine disease:: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro [J].
Chai, YH ;
Koppenhafer, SL ;
Shoesmith, SJ ;
Perez, MK ;
Paulson, HL .
HUMAN MOLECULAR GENETICS, 1999, 8 (04) :673-682
[3]   The role of protein composition in specifying nuclear inclusion formation in polyglutamine disease [J].
Chai, YH ;
Wu, LZ ;
Griffin, JD ;
Paulson, HL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (48) :44889-44897
[4]  
Chai YH, 1999, J NEUROSCI, V19, P10338
[5]   Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice [J].
Cummings, CJ ;
Reinstein, E ;
Sun, YL ;
Antalffy, B ;
Jiang, YH ;
Ciechanover, A ;
Orr, HT ;
Beaudet, AL ;
Zoghbi, HY .
NEURON, 1999, 24 (04) :879-892
[6]   Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice [J].
Cummings, CJ ;
Sun, YL ;
Opal, P ;
Antalffy, B ;
Mestril, R ;
Orr, HT ;
Dillmann, WH ;
Zoghbi, HY .
HUMAN MOLECULAR GENETICS, 2001, 10 (14) :1511-1518
[7]   Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1 [J].
Cummings, CJ ;
Mancini, MA ;
Antalffy, B ;
DeFranco, DB ;
Orr, HT ;
Zoghbi, HY .
NATURE GENETICS, 1998, 19 (02) :148-154
[8]   Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation [J].
Davies, SW ;
Turmaine, M ;
Cozens, BA ;
DiFiglia, M ;
Sharp, AH ;
Ross, CA ;
Scherzinger, E ;
Wanker, EE ;
Mangiarini, L ;
Bates, GP .
CELL, 1997, 90 (03) :537-548
[9]   Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain [J].
DiFiglia, M ;
Sapp, E ;
Chase, KO ;
Davies, SW ;
Bates, GP ;
Vonsattel, JP ;
Aronin, N .
SCIENCE, 1997, 277 (5334) :1990-1993
[10]   Golgi-disturbing agents [J].
Dinter, A ;
Berger, EG .
HISTOCHEMISTRY AND CELL BIOLOGY, 1998, 109 (5-6) :571-590