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Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi.

Abstract：

:In Huntington disease, polyglutamine expansion of the protein huntingtin (Htt) leads to selective neurodegenerative loss of medium spiny neurons throughout the striatum by an unknown apoptotic mechanism. Binding of Hip-1, a protein normally associated with Htt, is reduced by polyglutamine expansion. Free Hip-1 binds to a hitherto unknown polypeptide, Hippi (Hip-1 protein interactor), which has partial sequence homology to Hip-1 and similar tissue and subcellular distribution. The availability of free Hip-1 is modulated by polyglutamine length within Htt, with disease-associated polyglutamine expansion favouring the formation of pro-apoptotic Hippi-Hip-1 heterodimers. This heterodimer can recruit procaspase-8 into a complex of Hippi, Hip-1 and procaspase-8, and launch apoptosis through components of the 'extrinsic' cell-death pathway. We propose that Htt polyglutamine expansion liberates Hip-1 so that it can form a caspase-8 recruitment complex with Hippi. This novel non-receptor-mediated pathway for activating caspase-8 might contribute to neuronal death in Huntington disease.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Gervais FG,Singaraja R,Xanthoudakis S,Gutekunst CA,Leavitt BR,Metzler M,Hackam AS,Tam J,Vaillancourt JP,Houtzager V,Rasper DM,Roy S,Hayden MR,Nicholson DW

doi

10.1038/ncb735

keywords:

subject

Has Abstract

pub_date

2002-02-01 00:00:00

pages

95-105

issue

2

eissn

1465-7392

issn

1476-4679

pii

ncb735

journal_volume

4

pub_type

杂志文章

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