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Polyglutamine expansion in huntingtin increases its insertion into lipid bilayers

Item Type:Article
Title:Polyglutamine expansion in huntingtin increases its insertion into lipid bilayers
Creators Name:Kegel, K.B. and Schewkunow, V. and Sapp, E. and Masso, N. and Wanker, E.E. and Difiglia, M. and Goldmann, W.H.
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.
Keywords:Differential Scanning Calorimetry, Huntingtin, Huntington Disease, Membrane, Phospholipid Vesicles
Source:Biochemical and Biophysical Research Communications
ISSN:0006-291X
Publisher:Academic Press (U.S.A.)
Volume:387
Number:3
Page Range:472-475
Date:25 September 2009
Official Publication:https://doi.org/10.1016/j.bbrc.2009.07.039
PubMed:View item in PubMed

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