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Interaction of huntingtin fragments with brain membranes--clues to early dysfunction in Huntington's disease.

Abstract：

:Abstract Huntingtin is a large, multi-domain protein of unknown function in the brain. An abnormally elongated polyglutamine stretch in its N-terminus causes Huntington's disease (HD), a progressive neurodegenerative disorder. Huntingtin has been proposed to play a functional role in membrane trafficking via proteins involved in endo- and exocytosis. Here, we supply evidence for a direct association between huntingtin and membranes. In the brains of R6/2 mice with HD pathology, a 64 kDa N-terminal huntingtin fragment accumulated in postsynaptic membranes during the pre-symptomatic period of 4-8 weeks of age. In addition, an oligomeric fragment of approximately 200 kDa was detected at 8 weeks of age. Simultaneous progressive changes in distribution of amphiphysin, synaptojanin, and subunits of NMDA- and AMPA-receptors provide a strong indication of dysfunctional synaptic trafficking. Composition of the major phospholipids in the synaptic membranes was unaffected. In vitro, large unilamellar vesicles of brain lipids readily associated with soluble N-terminal huntingtin exon 1 fragments and stimulated fibrillogenesis of mutant huntingtin aggregates. Moreover, interaction of both mutant and wild-type huntingtin exon 1 fragments with brain lipids caused bilayer perturbation, mediated through a proline-rich region adjacent to the polyglutamines. This suggests that lipid interactions in vivo could influence misfolding of huntingtin and may play an early role in HD pathogenesis.

journal_name

J Neurochem

journal_title

Journal of neurochemistry

authors

Suopanki J,Götz C,Lutsch G,Schiller J,Harjes P,Herrmann A,Wanker EE

doi

10.1111/j.1471-4159.2005.03620.x

keywords:

subject

Has Abstract

pub_date

2006-02-01 00:00:00

pages

870-84

issue

3

eissn

0022-3042

issn

1471-4159

pii

JNC3620

journal_volume

96

pub_type

杂志文章

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