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Vol. 16, No. 11, pp. 1345-1355, June 1, 2002
1 Laboratory of Cell Signaling, Graduate School, Tokyo
Medical and Dental University, Bunkyo-ku, Tokyo 113-8549, Japan;
2 The Fourth Department, Osaka Bioscience Institute, Osaka
565-0874, Japan; 3 Kyoto University Graduate School of
Biostudies, Kyoto 606-8501, Japan; 4 Core Research for
Evolutional Science and Technology, Japan Science and Technology
Corporation
Expansion of CAG trinucleotide repeats that encode polyglutamine is
the underlying cause of at least nine inherited human neurodegenerative
disorders, including Huntington's disease and spinocerebellar ataxias.
PolyQ fragments accumulate as aggregates in the cytoplasm and/or in the
nucleus, and induce neuronal cell death. However, the molecular
mechanism of polyQ-induced cell death is controversial. Here, we show
the following: (1) polyQ with pathogenic repeat length triggers ER
stress through proteasomal dysfunction; (2) ER stress activates ASK 1 through formation of an IRE1-TRAF2-ASK1 complex; and (3)
ASK1
/ primary neurons are defective in polyQ-,
proteasome inhibitor-, and ER stress-induced JNK activation and cell
death. These findings suggest that ASK1 is a key element in ER
stress-induced cell death that plays an important role in the
neuropathological alterations in polyQ diseases.
[Key Words: ASK1; JNK; endoplasmic reticulum stress; polyglutamine disease; ubiquitine-proteasome system; apoptosis]]
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