ArticleJournal of Huntington's disease2016
Huntington's Disease Protein Huntingtin Associates with its own mRNA.
Article in Journal of Huntington's disease, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- High-affinity, structure-validated and selective macrocyclic peptide tools for chemical biology studies of Huntingtin.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- ALS and Huntington Disease: Unraveling the Connections between TDP-43 and Huntingtin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026Review
- High-Affinity, Structure-Validated and Selective Macrocyclic Peptide Tools for Chemical Biology Studies of Huntingtin.bioRxiv : the preprint server for biology · 2025Article
- Huntingtin is an RNA binding protein and participates inScience advances · 2024Article
- Bento: a toolkit for subcellular analysis of spatial transcriptomics data.Genome biology · 2024Article
- Spatial multi-omics: novel tools to study the complexity of cardiovascular diseases.Genome medicine · 2024Review
- Editorial: RNA binding proteins in neuroscience.Frontiers in molecular neuroscience · 2023Article
- Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties.Nature communications · 2021Article
- OLIG2 regulates lncRNAs and its own expression during oligodendrocyte lineage formation.BMC biology · 2021Article
- A role of cellular translation regulation associated with toxic Huntingtin protein.Cellular and molecular life sciences : CMLS · 2020Article
- Global Proteome and Ubiquitinome Changes in the Soluble and Insoluble Fractions of Q175 Huntington Mice Brains.Molecular & cellular proteomics : MCP · 2019Article
- Phosphorylated and aggregated TDP-43 with seeding properties are induced upon mutant Huntingtin (mHtt) polyglutamine expression in human cellular models.Cellular and molecular life sciences : CMLS · 2019Article
- Reduced mitochondrial fusion and Huntingtin levels contribute to impaired dendritic maturation and behavioral deficits in Fmr1-mutant mice.Nature neuroscience · 2019Article
- Is Huntingtin Dispensable in the Adult Brain?Journal of Huntington's disease · 2017Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe Huntington's disease (HD) protein huntingtin (Htt) plays a role in multiple cellular pathways. Deregulation of one or more of these pathways by the mutant Htt protein has been suggested to contribute to the disease pathogenesis. Our recent discovery-based proteomics studies have uncovered RNA binding proteins and translation factors associated with the endogenous Htt protein purified from mouse brains, suggesting a potential new role for Htt in RNA transport and translation.
objectiveTo investigate how Htt might affect RNA metabolism we set out to purify and analyze RNA associated with Htt.
methodsRNA was extracted from immunopurified Htt-containing protein complexes and analyzed by microarrays and RNA-Seq.
resultsSurprisingly, the most enriched mRNA that co-purified with Htt was Htt mRNA itself. The association of Htt protein and Htt mRNA was detected independent of intact ribosomes suggesting that it is not an RNA undergoing translation. Furthermore, we identified the recently reported mis-spliced Htt mRNA encoding a truncated protein comprised of exon 1 and a portion of the downstream intron in the immunoprecipitates containing mutant Htt protein. We show that Htt protein co-localizes with Htt mRNA and that wild-type Htt reduces expression of a reporter construct harboring the Htt 3' UTR.
conclusionsHD protein is found in a complex with its own mRNA and RNA binding proteins and translation factors. Htt may be involved in modulating its expression through post-transcriptional pathways. It is possible that Htt shares mechanistic properties similar to RNA binding proteins such as TDP-43 and FUS implicated in other neurodegenerative diseases.
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