Article ID Journal Published Year Pages File Type
1933116 Biochemical and Biophysical Research Communications 2009 4 Pages PDF
Abstract

An expanded polyglutamine (Q) tract (>37Q) in huntingtin (htt) causes Huntington disease. Htt associates with membranes and polyglutamine expansion in htt may alter membrane function in Huntington disease through a mechanism that is not known. Here we used differential scanning calorimetry to examine the effects of polyQ expansion in htt on its insertion into lipid bilayers. We prepared synthetic lipid vesicles composed of phosphatidylcholine and phosphatidylethanolamine and tested interactions of htt amino acids 1–89 with 20Q, 32Q or 53Q with the vesicles. GST-htt1–89 with 53Q inserted into synthetic lipid vesicles significantly more than GST-htt1–89 with 20Q or 32Q. We speculate that by inserting more into cell membranes, mutant huntingtin could increase disorder within the lipid bilayer and thereby disturb cellular membrane function.

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