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Article

Polyglutamine expansion in huntingtin alters its interaction with phospholipids.

Journal of neurochemistry - 1 Sept 2009

Kegel Kimberly B, Sapp Ellen, Alexander Jonathan, Valencia Antonio, Reeves Patrick, Li Xueyi, Masso Nicholas, Sobin Lindsay, Aronin Neil, DiFiglia Marian

Abstract excerpt

Huntingtin has an expanded polyglutamine tract in patients with Huntington's disease. Huntingtin localizes to intracellular and plasma membranes but the function of huntingtin at membranes is unknown. Previously we reported that exogenously expressed huntingtin bound pure phospholipids using protein-lipid overlays. Here we show that endogenous huntingtin from normal (Hdh(7Q/7Q)) mouse brain and mutant huntingtin...

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Identifiers

PMID: 19566678
DOI: 10.1111/j.1471-4159.2009.06255.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Polyglutamine expansion in huntingtin alters its interaction with phospholipids.PMID 19566678Read ↗

Hypothesis: huntingtin may function in membrane association and vesicular traffickingThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB — Membrane Proteins in Health and Disease.Semantic proximity Read ↗

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Membranes as targets and modifiers of mutant huntingtin aggregation.Semantic proximity Read ↗

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Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity.Semantic proximity Read ↗

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Mutant huntingtin inhibits clathrin-independent endocytosis and causes accumulation of cholesterol in vitro and in vivo.Semantic proximity Read ↗

Early whole-body mutant huntingtin lowering averts changes in proteins and lipids important for synapse function and white matter maintenance in the LacQ140 mouse modelSemantic proximity Read ↗

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