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Huntingtinmicrotubule interactions (p. 941)

Mutations in the protein huntingtin that expand its N-terminal polyglutamine tract cause the inherited neurodegenerative disorder Huntington disease. The expanded polyglutamine repeat is thought to reduce the solubility of the protein, resulting in formation of the characteristic nuclear/perinuclear aggregates that probably cause neuronal cell death. Phillippe Djian and co-workers now show that huntingtin binds to microtubules. They demonstrate that the protein interacts specifically with ß-tubulin (but not -tubulin or MAP2) in lymphoblasts and brain. In addition, they demonstrate that it copurifies with polymerized microtubules in vitro and colocalizes with microtubules and centrosomes in vivo. This ability to associate with ß-tubulin seems to be a property of both wild-type and mutant huntintin. The authors suggest that a high density of microtubules in the perinuclear region could make huntingtin aggregates more likely to develop in the perinuclear region. Since ß-tubulin is more abundant in neurons than in any other cell type, such inclusions might form more rapidly in these cells.

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Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with ß-tubulin: relevance to Huntington's disease

Guylaine Hoffner, Pascal Kahlem, and Philippe Djian
JCS 2002 115: 941-948. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?