Journal
NEUROSCIENCE LETTERS
Volume 503, Issue 3, Pages 234-239Publisher
ELSEVIER IRELAND LTD
DOI: 10.1016/j.neulet.2011.08.043
Keywords
Aggregation; Huntingtin; Polyglutamine; Tollip
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Funding
- Japan Society for Promotion of Science
- Grants-in-Aid for Scientific Research [23650416, 23570220, 22020003] Funding Source: KAKEN
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Huntington disease (HD) is caused by the expansion of polyglutamine (polyQ) repeats in the amino-terminal of hungtintin (htt). PolyQ-expanded htt forms intracellular ubiquitinated aggregates in neurons and causes neuronal cell death. Here, utilizing a HD cellular model, we report that Tollip, an ubiquitin binding protein that participates in intracellular transport via endosomes, co-localizes with and stimulates aggregation of polyQ-expanded amino-terminal htt. Furthermore, we demonstrate that Tollip protects cells against the toxicity of polyQ-expanded htt. We propose that association of Tollip with polyubiquitin accelerates aggregation of toxic htt species into inclusions and thus provides a cell protective role by sequestration. (C) 2011 Elsevier Ireland Ltd. All rights reserved.
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