Journal
BRAIN RESEARCH BULLETIN
Volume 72, Issue 2-3, Pages 121-123Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.brainresbull.2006.10.030
Keywords
Huntington's disease; proteasome activity; inclusion bodies; filaments
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An impairment of the ubiquitin-proteasome system (UPS) has been postulated in Huntington's disease (HD) and in other CAG-triplet repeat disorders. This hypothesis arises from the observation that polyglutamine (polyQ)-containing inclusion bodies that are characteristic of these diseases also contain components of the UPS. However, since that initial discovery, the UPS impairment hypothesis has remained controversial. Recent in vitro enzymatic studies revealed the inability of eukaryotic proteasomes to digest expanded polyQ, thus suggesting that occasional failure of polyQ to exit the proteasome may interfere with its proteolytic function. However, it has also recently been found that in vitro assembled aggregates made of synthetic polyQ fail to inhibit proteasome activity. Here we propose future experiments that may help to ellucidate whether a direct interaction between proteasomes and polyQ stretches or aggregates can result in inhibition of proteasome activity. (c) 2006 Elsevier Inc. All rights reserved.
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