Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons

George R. Jackson, Iris Salecker, Xinzhong Dong, Xiang Yao, Norman Arnheim, Peter W. Faber, Marcy E. MacDonald, S. Lawrence Zipursky

Research output: Contribution to journalArticlepeer-review

405 Scopus citations


Huntington's disease (HD) is an autosomal dominant neurodegenerative disorder. Disease alleles contain a trinucleotide repeat expansion of variable length, which encodes polyglutamine tracts near the amino terminus of the HD protein, huntingtin. Polyglutamine-expanded huntingtin, but not normal huntingtin, forms nuclear inclusions. We describe a Drosophila model for HD. Amine-terminal fragments of human huntingtin containing tracts of 2, 75, and 120 glutamine residues were expressed in photoreceptor neurons in the compound eye. As in human neurons, polyglutamine-expanded huntingtin induced neuronal degeneration. The age of onset and severity of neuronal degeneration correlated with repeat length, and nuclear localization of huntingtin presaged neuronal degeneration. In contrast to other cell death paradigms in Drosophila, coexpression of the viral antiapoptotic protein, P35, did not rescue the cell death phenotype induced by polyglutamine-expanded huntingtin.

Original languageEnglish (US)
Pages (from-to)633-642
Number of pages10
Issue number3
StatePublished - Sep 1998
Externally publishedYes

ASJC Scopus subject areas

  • Neuroscience(all)


Dive into the research topics of 'Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons'. Together they form a unique fingerprint.

Cite this