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Article

Prevention of ubiquitination at K6 and K9 in mutant huntingtin exacerbates disease pathology in a knock-in mouse model.

Proceedings of the National Academy of Sciences of the United States of America - 13 Jan 2026

Qi Pengfei, Yu-Taeger Libo, Han Hezhou, Zhou Junbo, Singer-Mikosch Elisabeth, Casadei Nicolas, Riess Olaf, Ziv Noam E, Ciechanover Aaron, Phuc Nguyen Hoa Huu

Abstract excerpt

Huntington disease (HD) is caused by an expansion of the polyglutamine (polyQ) tract in the huntingtin protein (HTT), leading to its misfolding and aggregation. The subcellular localization of mutant HTT (mHTT) aggregates critically influences their neuronal toxicity, with nuclear aggregates contributing more significantly to neurodegeneration than those in the neuropil. Our previous findings demonstrated that...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 41505525
DOI: 10.1073/pnas.2527258122
PMCID: PMC12799157

Genes

HTT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

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Research trail→

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Prevention of ubiquitination at K6 and K9 in mutant huntingtin exacerbates disease pathology in a knock-in mouse model.PMID 41505525Read ↗

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Inhibiting the ubiquitin-proteasome system leads to preferential accumulation of toxic N-terminal mutant huntingtin fragments.Semantic proximity Read ↗

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