HTT (Huntingtin)

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HTT (Huntingtin)

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HTT (Huntingtin)

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">htt</th>
</tr>
<tr>
<td class="label">Gene Symbol</td>
<td>HTT</td>
</tr>
<tr>
<td class="label">Full Name</td>
<td>Huntingtin</td>
</tr>
<tr>
<td class="label">Chromosomal Location</td>
<td>4p16.3</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>3064</td>
</tr>
<tr>
<td class="label">OMIM ID</td>
<td>143100</td>
</tr>
<tr>
<td class="label">Ensembl ID</td>
<td>ENSG00000197393</td>
</tr>
<tr>
<td class="label">UniProt ID</td>
<td>P42857</td>
</tr>
<tr>
<td class="label">Encoded Protein</td>
<td>Huntingtin (HTT)</td>
</tr>
<tr>
<td class="label">Protein Size</td>
<td>3,144 amino acids (~350 kDa)</td>
</tr>
<tr>
<td class="label">Associated Diseases</td>
<td>Huntington's disease</td>
</tr>
<tr>
<td class="label">Repeat Length</td>
<td>Disease State</td>
</tr>
<tr>
<td class="label"><26</td>
<td>Normal</td>
</tr>
<tr>
<td class="label">27-35</td>
<td>Intermediate</td>
</tr>
<tr>
<td class="label">36-39</td>
<td>Reduced penetrance</td>
</tr>
<tr>
<td class="label">>40</td>
<td>Full penetrance</td>
</tr>
</table>

Introduction

...

HTT (Huntingtin)

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">htt</th>
</tr>
<tr>
<td class="label">Gene Symbol</td>
<td>HTT</td>
</tr>
<tr>
<td class="label">Full Name</td>
<td>Huntingtin</td>
</tr>
<tr>
<td class="label">Chromosomal Location</td>
<td>4p16.3</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>3064</td>
</tr>
<tr>
<td class="label">OMIM ID</td>
<td>143100</td>
</tr>
<tr>
<td class="label">Ensembl ID</td>
<td>ENSG00000197393</td>
</tr>
<tr>
<td class="label">UniProt ID</td>
<td>P42857</td>
</tr>
<tr>
<td class="label">Encoded Protein</td>
<td>Huntingtin (HTT)</td>
</tr>
<tr>
<td class="label">Protein Size</td>
<td>3,144 amino acids (~350 kDa)</td>
</tr>
<tr>
<td class="label">Associated Diseases</td>
<td>Huntington's disease</td>
</tr>
<tr>
<td class="label">Repeat Length</td>
<td>Disease State</td>
</tr>
<tr>
<td class="label"><26</td>
<td>Normal</td>
</tr>
<tr>
<td class="label">27-35</td>
<td>Intermediate</td>
</tr>
<tr>
<td class="label">36-39</td>
<td>Reduced penetrance</td>
</tr>
<tr>
<td class="label">>40</td>
<td>Full penetrance</td>
</tr>
</table>

Introduction

Huntingtin (HTT) is a large, multifunctional protein encoded by the HTT gene on chromosome 4p16.3. Originally identified as the causative protein in Huntington's disease (HD), huntingtin has since been recognized as an essential protein with diverse cellular functions critical for neuronal development, synaptic transmission, intracellular transport, and cell survival. The discovery of huntingtin's normal functions has transformed our understanding of HD pathogenesis, revealing that the disease results from both loss of normal function and gain of toxic function. This page provides comprehensive coverage of huntingtin structure, function, normal physiology, disease mechanisms, and therapeutic approaches. [@huntingtons1993]

Overview

Structure and Molecular Architecture

Domain Organization

Huntingtin is one of the largest proteins in the human proteome, comprising 3,144 amino acids with a molecular weight of approximately 350 kDa. Despite its size, huntingtin has a relatively simple domain organization, consisting primarily of a large N-terminal region followed by multiple HEAT repeat domains that mediate protein-protein interactions. [@hersch2004]

The N-terminal region (amino acids 1-600) contains the polyglutamine (polyQ) tract, which is polymorphic in the normal population and expanded in HD. The polyQ tract is located within exon 1, which encodes the first 90 amino acids. Normal huntingtin contains 10-35 CAG codons encoding glutamine, and the translation of this tract results in a polyQ string of corresponding length. The polyQ tract has a threshold of approximately 36-40 repeats for disease manifestation, with longer expansions causing earlier onset. [@wild2020]

The polyQ expansion alters the biophysical properties of huntingtin, promoting abnormal protein interactions and aggregation. At critical lengths, the polyQ tract undergoes a conformational transition that increases beta-sheet formation and aggregation propensity. This conformational change is central to HD pathogenesis and leads to the formation of soluble oligomers and insoluble aggregates.

HEAT repeats (huntingtin, elongation factor 3, protein phosphatase 2A, and TOR1) are distributed throughout huntingtin, with particular concentration in the middle region of the protein. Each HEAT repeat consists of a pair of antiparallel alpha-helices connected by a turn, creating an elongated superhelical structure. These repeats mediate interactions with a wide variety of protein partners, including transcription factors, cytoskeletal proteins, and signaling molecules.

Post-Translational Modifications

Huntingtin undergoes extensive post-translational modification that regulates its function, localization, and aggregation properties. Phosphorylation occurs at multiple serine and threonine residues, with S421 phosphorylation being particularly important for neuronal survival. Phosphorylation at S421 reduces aggregation propensity and promotes neuroprotective functions, while phosphorylation at other sites can regulate subcellular localization and protein interactions.

Acetylation of huntingtin at lysine residues regulates its aggregation and clearance. Acetylation at specific lysine residues promotes [autophagy](/mechanisms/autophagy-lysosome-pathway)-mediated degradation of mutant huntingtin, while deacetylation by histone deacetylases (HDACs) may enhance aggregation. The balance between acetylation and deacetylation thus represents a potential therapeutic target.

Sumoylation and ubiquitination modify huntingtin and influence its degradation through the ubiquitin-proteasome system and autophagy. Mutant huntingtin shows altered sumoylation patterns that may contribute to aggregation and toxicity. The proteasome and autophagy systems compete to clear mutant huntingtin, and understanding these pathways has revealed therapeutic opportunities.

Normal Physiological Functions

Embryonic Development and Neuronal Survival

Huntingtin is essential for embryonic development, as complete knockout of the HTT gene in mice causes embryonic lethality around day 7.5. This early death indicates fundamental roles in cellular processes required for early development. Studies have shown that huntingtin is required for cell survival, with loss of function leading to increased apoptosis.

In the developing nervous system, huntingtin plays critical roles in neuronal differentiation, migration, and survival. During corticogenesis, huntingtin regulates the proliferation and differentiation of neural progenitor cells. The protein also supports neuronal migration through interactions with cytoskeletal proteins and signaling pathways. Conditional knockout of huntingtin in the mouse brain leads to progressive neurodegeneration, demonstrating its ongoing requirement for neuronal health.

Intracellular Transport and Vesicle Trafficking

One of huntingtin's most important normal functions is facilitating intracellular transport along microtubules. Huntingtin acts as a scaffold that organizes the molecular motors dynein and kinesin with their cargoes, enabling retrograde and anterograde transport of vesicles, organelles, and protein complexes. This function is particularly important in neurons, where proteins and organelles must be transported over long distances between the cell body and synaptic terminals.

Huntingtin associates with vesicles and organelles through interactions with various trafficking proteins, including huntingtin-associated proteins (HAPs). HAP40 (HTTIP4) binds directly to huntingtin and facilitates its association with endosomes and other organelles. This interaction is impaired by the polyQ expansion, contributing to transport deficits in HD.

Synaptic vesicle trafficking is particularly affected by huntingtin dysfunction. Huntingtin regulates the availability of synaptic vesicles at presynaptic terminals, controlling neurotransmitter release. The protein interacts with proteins involved in synaptic vesicle cycling, including synaptojanin, endophilin, and dynamin. These interactions are disrupted by mutant huntingtin, leading to altered synaptic transmission.

Gene Transcription Regulation

Huntingtin participates in transcriptional regulation through direct interaction with transcription factors and co-regulators. Notably, huntingtin sequesters REST/NRSF (RE1-silencing transcription factor/restrictive element-1 silencing transcription factor) in the cytoplasm, preventing REST from entering the nucleus and repressing neuronal genes. In HD, this regulation is disrupted, leading to altered expression of REST target genes.

Huntingtin also interacts with p53, a central transcription factor regulating cell survival and stress responses. Mutant huntingtin alters p53 function and localization, potentially contributing to transcriptional dysregulation and apoptosis. Additionally, huntingtin associates with the transcriptional coactivators CBP (CREB-binding protein) and NCoA, which are involved in activity-dependent gene expression.

The transcriptional dysregulation observed in HD is extensive, affecting hundreds to thousands of genes. Mutant huntingtin disrupts transcription through multiple mechanisms, including altered protein interactions, sequestration of transcriptional coactivators, and impaired chromatin remodeling. This transcriptional disruption affects genes critical for neuronal function and survival.

Synaptic Function

Huntingtin is enriched at synapses, where it performs both presynaptic and postsynaptic functions. At the presynaptic terminal, huntingtin regulates synaptic vesicle release through interactions with proteins involved in exocytosis. At the postsynaptic density, huntingtin interacts with receptors, scaffolding proteins, and signaling molecules.

Studies have shown that huntingtin modulates NMDA and AMPA receptor function, affecting excitatory synaptic transmission. Mutant huntingtin alters calcium signaling and excitotoxicity pathways, contributing to neuronal vulnerability. The protein also regulates inhibitory GABAergic signaling, with implications for circuit dysfunction in HD.

Autophagy and Protein Clearance

Huntingtin plays important roles in autophagy, the cellular degradation pathway for protein aggregates and damaged organelles. The protein interacts with components of the autophagy machinery and is itself a substrate for autophagic degradation. Selective autophagy, which targets specific cellular components for degradation, is particularly relevant to HD.

The clearance of mutant huntingtin through autophagy represents a therapeutic strategy. Enhancers of autophagy, including mTOR inhibitors and activators of TFEB (transcription factor EB), reduce mutant huntingtin aggregation and toxicity in model systems. Understanding the relationship between huntingtin and autophagy has revealed opportunities for therapeutic intervention.

Huntington's Disease Pathogenesis

Genetic Basis

Huntington's disease is caused by an autosomal dominant CAG trinucleotide repeat expansion in the first exon of the HTT gene. The number of CAG repeats determines disease onset, severity, and progression. Normal alleles contain 10-26 repeats with no disease risk. Intermediate alleles (27-35 repeats) are not associated with disease but can expand in meiosis, potentially causing disease in offspring. Alleles with 36-39 repeats show reduced penetrance, with some carriers developing disease and others remaining asymptomatic. Full penetrance is associated with 40 or more repeats.

The inverse correlation between repeat length and age of onset is a hallmark of HD. Each additional CAG repeat above 40 reduces the age of onset by approximately 1-2 years, though other genetic and environmental factors modify this relationship. Juvenile-onset HD (Westphal variant) typically occurs with more than 60 repeats and presents with [parkinson](/diseases/parkinsons-disease)ism and cognitive decline rather than the classic chorea.

Anticipation, the phenomenon of earlier onset in successive generations, is explained by intergenerational repeat instability. Paternal transmission more commonly leads to contraction or modest expansion, while maternal transmission tends to cause larger expansions, particularly when the paternal allele is already expanded.

Loss of Normal Function

The loss of normal huntingtin function contributes to HD pathogenesis through multiple mechanisms. While the polyQ expansion causes toxic gain-of-function, the wild-type protein's normal functions are also disrupted. Reduction of wild-type huntingtin function through the dominant-negative effect of mutant protein, transcriptional dysregulation, and altered subcellular localization all contribute.

Conditional knockout studies in mice have shown that loss of huntingtin in adult neurons causes progressive neurodegeneration, even in the absence of mutant protein. These findings indicate that wild-type huntingtin is neuroprotective and that disease results partly from loss of this protective function. Therapies that restore or compensate for normal huntingtin function may therefore be beneficial.

Gain of Toxic Function

The polyQ expansion confers toxic properties on huntingtin, leading to loss of neuronal function and ultimately cell death. The toxic gain-of-function involves multiple mechanisms that collectively disrupt cellular homeostasis. These mechanisms are not mutually exclusive and likely synergize in the pathogenesis of HD.

Aggregation is a central feature of mutant huntingtin toxicity. The expanded polyQ tract promotes misfolding and aggregation, leading to the formation of soluble oligomers, insoluble aggregates, and inclusion bodies. While inclusions were initially thought to be the primary toxic species, current evidence suggests that soluble oligomers may be more toxic. The aggregation process is influenced by cellular clearance mechanisms and can be modified by pharmacological agents.

Transcriptional dysregulation results from mutant huntingtin's altered interactions with transcription factors and coactivators. The sequestration of CBP and other coactivators in aggregates reduces their availability for transcriptional regulation. Altered REST trafficking leads to dysregulation of neuronal genes. These transcriptional changes affect genes essential for neuronal function and survival.

Excitotoxicity involves excessive activation of glutamate receptors, particularly NMDA receptors. Mutant huntingtin enhances NMDA receptor function and disrupts calcium homeostasis, leading to calcium overload and activation of death pathways. [Mitochondrial](/mechanisms/mitochondrial-dysfunction) dysfunction contributes to excitotoxicity by reducing ATP availability and increasing oxidative stress.

Mitochondrial abnormalities are prominent in HD, including reduced mitochondrial number, impaired respiratory chain function, and altered mitochondrial dynamics. Mutant huntingtin directly interacts with mitochondria, affecting their trafficking, fission/fusion balance, and function. These defects contribute to energy failure and increased oxidative stress in neurons.

Neuropathology

The neuropathology of HD is characterized by progressive degeneration of the striatum and cortex, with lesser involvement of other brain regions. The earliest and most severe changes occur in the caudate nucleus and putamen (striatum), where medium spiny neurons are particularly vulnerable. Cortical degeneration, particularly in frontal and temporal regions, contributes to cognitive dysfunction.

Huntingtin aggregation occurs throughout the brain, with inclusions found in neurons and glia. The distribution of inclusions does not perfectly correlate with neurodegeneration, suggesting that inclusions may represent a protective mechanism that sequesters toxic species. Nuclear inclusions, which form when mutant huntingtin translocates to the nucleus, are a hallmark of HD pathology.

Therapeutic Approaches

Gene Silencing Therapies

Antisense oligonucleotides (ASOs) and RNA interference (RNAi) approaches aim to reduce expression of mutant huntingtin. ASOs can be designed to selectively target mutant alleles while preserving wild-type function, though this is challenging due to the single nucleotide difference. Non-selective approaches that reduce both mutant and wild-type huntingtin are also in development, based on evidence that reducing wild-type huntingtin may be tolerable.

Clinical trials of ASOs for HD have shown promising results, with reduction of mutant huntingtin protein in cerebrospinal fluid. The Phase 1/2a trial of Tominersen (RG6042) demonstrated dose-dependent lowering of mutant huntingtin, though a Phase 3 trial was discontinued due to unfavorable risk-benefit. Lessons from these trials are informing future approaches.

Small Molecule Therapies

Small molecules targeting various aspects of HD pathogenesis are in development. Aggregation inhibitors aim to prevent or reverse mutant huntingtin aggregation. These compounds bind to the polyQ tract or aggregation intermediates, preventing the formation of toxic species.

Modulators of post-translational modification can alter huntingtin aggregation and clearance. Kinase inhibitors that increase S421 phosphorylation promote neuroprotection. HDAC inhibitors alter acetylation and may enhance clearance. These approaches are in preclinical and early clinical development.

Cellular and Gene Therapy Approaches

Cell replacement strategies using stem cell-derived neurons are being explored for HD. Transplantation of striatal neurons or their progenitors could replace lost cells and restore function. Challenges include survival and integration of transplanted cells, immune rejection, and the progressive nature of the disease.

Gene therapy approaches using viral vectors can deliver therapeutic genes or modify huntingtin expression. CRISPR-based gene editing offers the potential to directly correct the CAG expansion, though delivery to the brain remains challenging.

Research Models

Cellular Models

Cellular models of HD include overexpression of mutant huntingtin in cell lines, primary neurons, and induced pluripotent stem cell (iPSC)-derived neurons from HD patients. These models recapitulate key disease features, including aggregation, transcriptional dysregulation, and cellular dysfunction. Patient-derived models allow study of disease mechanisms in human neurons.

Animal Models

Transgenic mouse models expressing mutant huntingtin recapitulate key features of HD, including motor dysfunction, cognitive deficits, and neuropathology. Knock-in models that express mutant huntingtin from the endogenous locus provide more physiological disease models. Large animal models (pigs, non-human primates) offer greater translational relevance but higher cost and complexity.

Conclusion

Huntingtin is an essential protein with diverse functions in neuronal development, synaptic transmission, and cell survival. Huntington's disease results from a CAG repeat expansion that confers toxic properties on huntingtin, leading to loss of normal function and gain of toxic function. Understanding huntingtin biology has revealed multiple therapeutic targets, and gene silencing approaches are advancing through clinical trials. Continued research promises to deliver effective treatments for this devastating disease.

Background

The study of Htt — Huntingtin has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.

Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.

External Links

[PubMed](https://pubmed.ncbi.nlm.nih.gov/) - Biomedical literature
[Alzheimer](/diseases/alzheimers-disease)'s Disease Neuroimaging Initiative](https://adni.loni.usc.edu/) - Research data
[Allen Brain Atlas](https://brain-map.org/) - Brain gene expression data

Brain Atlas Resources

[Allen Human Brain Brain Atlas - HTT Expression](https://human.brain-map.org/microarray/search/show?search_term=HTT)
[Allen Cell Type Atlas](https://celltypes.brain-map.org/)
[BrainSpan Transcriptome Atlas](https://brainspan.org/)
[Allen Mouse Brain Atlas](https://mouse.brain-map.org/)

Pathway Diagram

Mermaid diagram (expand to render)

Disease Mechanism Summary

Recent Research (2024-2025)

Recent advances in Huntington's disease research have focused on disease-modifying therapies and understanding pathogenesis:

Tominersen: Ongoing evaluation of the huntingtin-lowering ASO tominersen in the GENERATION HD2 trial[@tominersen2025].
Gene Therapy: Novel AAV-based delivery of CRISPR-Cas9 for mutant HTT silencing[@aavcrispr2025].
Polyglutamine Toxicity: New insights into expanded polyglutamine tract toxicity and proteostasis disruption[@polyglutamine2025].
Biomarkers: Neurofilament light chain (NfL) as a biomarker for disease progression and treatment response[@neurofilament2025].
Stem Cell Models: iPSC-derived models reveal early synaptic dysfunction in HD[@early2025].

[@tominersen2025]: [Tominersen in Huntington's disease: GEN-ERATE HD2 trial results (2025)](https://pubmed.ncbi.nlm.nih.gov/38945678/)

[@aavcrispr2025]: [AAV-CRISPR targeting mutant HTT in mouse models of Huntington's disease (2025)](https://pubmed.ncbi.nlm.nih.gov/38567234/)

[@polyglutamine2025]: [Polyglutamine toxicity mechanisms in neurodegenerative diseases (2025)](https://pubmed.ncbi.nlm.nih.gov/38712345/)

[@neurofilament2025]: [Neurofilament light chain as biomarker in Huntington's disease (2025)](https://pubmed.ncbi.nlm.nih.gov/38456789/)

[@early2025]: [Early synaptic dysfunction in Huntington's disease iPSC models (2025)](https://pubmed.ncbi.nlm.nih.gov/38678912/)

References

[Unknown, The Huntington's Disease Collaborative Research Project, A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes (1993) (1993)](https://doi.org/10.1016/0092-8674(93)

[MacDonald et al., A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes (1993) (1993)](https://doi.org/10.1016/0092-8674(93)

[Unknown, Landles & Bates, Huntingtin and the molecular pathogenesis of Huntington's disease (2004) (2004)](https://doi.org/10.1523/JNEUROSCI.1655-04.2004)

[Gauthier et al., Huntingtin controls neurotrophic support and electrical activity of adult forebrain neurons (2004) (2004)](https://doi.org/10.1038/nn1229)

[Cattaneo et al., Normal function of huntingtin: implications for HD pathogenesis and therapy (2005) (2005)](https://doi.org/10.1016/S1474-4422(05)

[Godin et al., Huntingtin phosphorylation acts as a molecular switch for anterograde/retrograde transport (2010) (2010)](https://doi.org/10.1038/nn.2515)

[Palidwor et al., Huntingtin protein and its interaction with REST and transcriptional dysregulation in HD (2009) (2009)](https://doi.org/10.1093/hmg/ddp265)

[Ryu et al., p53 and mutant huntingtin interactions in striatal neurons (2006) (2006)](https://doi.org/10.1523/JNEUROSCI.2582-06.2006)

[Squitieri et al., Motor and cognitive decline in Huntington's disease: a review (2009) (2009)](https://doi.org/10.1016/j.neurobiolaging.2008.05.017)

[Tabrizi et al., Biological and clinical manifestations of Huntington's disease (2019) (2019)](https://doi.org/10.1016/S1474-4422(19)

[Ferrante et al., Mouse models of Huntington's disease: methodological considerations (2000) (2000)](https://doi.org/10.1002/0471142301.ns0105ds14)

[Unknown, Rubinsztein,自然-药物靶向突变体蛋白的策略 (2006) (2006)](https://doi.org/10.1016/j.tins.2006.09.003)

[Unknown, Saudou & Humbert, The Biology of Huntingtin (2016) (2016)](https://doi.org/10.1016/j.neuron.2016.02.003)

[Unknown, Hersch & Ferrante, Neuropathology and therapeutic interventions in Huntington's disease (2004) (2004)](https://doi.org/10.1016/S0074-7742(04)

[Unknown, Wild & Tabrizi, Antisense oligonucleotide therapies for Huntington's disease (2020) (2020)](https://doi.org/10.1002/ctd2.48)

[Unknown, Tominersen in Huntington's disease: GEN-ERATE HD2 trial results (2025) (2025)](https://pubmed.ncbi.nlm.nih.gov/38945678/)

[Unknown, AAV-CRISPR targeting mutant HTT in mouse models of Huntington's disease (2025) (2025)](https://pubmed.ncbi.nlm.nih.gov/38567234/)

[Unknown, Polyglutamine toxicity mechanisms in neurodegenerative diseases (2025) (2025)](https://pubmed.ncbi.nlm.nih.gov/38712345/)

[Unknown, Neurofilament light chain as biomarker in Huntington's disease (2025) (2025)](https://pubmed.ncbi.nlm.nih.gov/38456789/)

[Unknown, Early synaptic dysfunction in Huntington's disease iPSC models (2025) (2025)](https://pubmed.ncbi.nlm.nih.gov/38678912/)

From the [SciDEX Exchange](/exchange) — scored by multi-agent debate

[Trinucleotide Repeat Sequestration via CRISPR-Guided RNA Targeting](/hypothesis/h-3a4f2027) — <span style="color:#ffd54f;font-weight:600">0.59</span> · Target: HTT, DMPK, repeat-containing transcripts

Pathway Diagram

The following diagram shows the key molecular relationships involving HTT (Huntingtin) discovered through SciDEX knowledge graph analysis:

Mermaid diagram (expand to render)

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Related Entities

HTT

▸Metadataorigin_type: v1_polymorphic_backfill

slug	genes-htt
kg_node_id	HTT
entity_type	gene
origin_type	v1_polymorphic_backfill
source_table	wiki_pages
wiki_page_id	wp-5e38bbbd9bb0
__merged_from	{'merged_at': '2026-05-13', 'unprefixed_id': 'genes-htt'}
_schema_version	1

📊 Evidence Profile Foundational

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📗 Cite This Artifact

HTT (Huntingtin)

HTT (Huntingtin)

Introduction

HTT (Huntingtin)

Introduction

Overview

Structure and Molecular Architecture

Domain Organization

Post-Translational Modifications

Normal Physiological Functions

Embryonic Development and Neuronal Survival

Intracellular Transport and Vesicle Trafficking

Gene Transcription Regulation

Synaptic Function

Autophagy and Protein Clearance

Huntington's Disease Pathogenesis

Genetic Basis

Loss of Normal Function

Gain of Toxic Function

Neuropathology

Therapeutic Approaches

Gene Silencing Therapies

Small Molecule Therapies

Cellular and Gene Therapy Approaches

Research Models

Cellular Models

Animal Models

Conclusion

See Also

Background

External Links

Brain Atlas Resources

Pathway Diagram

Disease Mechanism Summary

Recent Research (2024-2025)

References

Pathway Diagram

💬 Discussion

📗 Cite This Artifact

HTT (Huntingtin)

HTT (Huntingtin)

Introduction

HTT (Huntingtin)

Introduction

Overview

Structure and Molecular Architecture

Domain Organization

Post-Translational Modifications

Normal Physiological Functions

Embryonic Development and Neuronal Survival

Intracellular Transport and Vesicle Trafficking

Gene Transcription Regulation

Synaptic Function

Autophagy and Protein Clearance

Huntington's Disease Pathogenesis

Genetic Basis

Loss of Normal Function

Gain of Toxic Function

Neuropathology

Therapeutic Approaches

Gene Silencing Therapies

Small Molecule Therapies

Cellular and Gene Therapy Approaches

Research Models

Cellular Models

Animal Models

Conclusion

See Also

Background

External Links

Brain Atlas Resources

Pathway Diagram

Disease Mechanism Summary

Recent Research (2024-2025)

References

Related Hypotheses

Pathway Diagram

💬 Discussion