cct7

cct7

Overview

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">cct7</th>
</tr>
<tr>
<td class="label">Gene Symbol</td>
<td>CCT7</td>
</tr>
<tr>
<td class="label">Full Name</td>
<td>Chaperonin Containing TCP1 Subunit 7 (Eta)</td>
</tr>
<tr>
<td class="label">Chromosomal Location</td>
<td>2p21</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>10320</td>
</tr>
<tr>
<td class="label">OMIM ID</td>
<td>604832</td>
</tr>
<tr>
<td class="label">Ensembl ID</td>
<td>ENSG00000135604</td>
</tr>
<tr>
<td class="label">UniProt ID</td>
<td>Q99832</td>
</tr>
<tr>
<td class="label">Protein Length</td>
<td>543 amino acids</td>
</tr>
<tr>
<td class="label">Molecular Weight</td>
<td>~59 kDa</td>
</tr>
<tr>
<td class="label">Approach</td>
<td>Description</td>
</tr>
<tr>
<td class="label">CCT enhancers</td>
<td>Increase chaperone activity</td>
</tr>
<tr>
<td class="label">Gene therapy</td>
<td>Modulate CCT expression</td>
</tr>
<tr>
<td class="label">Combination therapy</td>
<td>With other chaperones</td>
</tr>
<tr>
<td class="label">Interactor</td>
<td>Type</td>
</tr>
<tr>
<td class="label">Other CCT subunits</td>
<td>Complex members</td>
</tr>
<tr>
<td class="label">Actin</td>
<td>Substrate</td>
</tr>
<tr>
<td class="label">Tubulin</td>
<td>Substrate</td>
</tr>
<tr>
<td class="label">Hsp70</td>
<t

cct7

Overview

<table class="infobox infobox-gene">
<tr>
<th class="infobox-header" colspan="2">cct7</th>
</tr>
<tr>
<td class="label">Gene Symbol</td>
<td>CCT7</td>
</tr>
<tr>
<td class="label">Full Name</td>
<td>Chaperonin Containing TCP1 Subunit 7 (Eta)</td>
</tr>
<tr>
<td class="label">Chromosomal Location</td>
<td>2p21</td>
</tr>
<tr>
<td class="label">NCBI Gene ID</td>
<td>10320</td>
</tr>
<tr>
<td class="label">OMIM ID</td>
<td>604832</td>
</tr>
<tr>
<td class="label">Ensembl ID</td>
<td>ENSG00000135604</td>
</tr>
<tr>
<td class="label">UniProt ID</td>
<td>Q99832</td>
</tr>
<tr>
<td class="label">Protein Length</td>
<td>543 amino acids</td>
</tr>
<tr>
<td class="label">Molecular Weight</td>
<td>~59 kDa</td>
</tr>
<tr>
<td class="label">Approach</td>
<td>Description</td>
</tr>
<tr>
<td class="label">CCT enhancers</td>
<td>Increase chaperone activity</td>
</tr>
<tr>
<td class="label">Gene therapy</td>
<td>Modulate CCT expression</td>
</tr>
<tr>
<td class="label">Combination therapy</td>
<td>With other chaperones</td>
</tr>
<tr>
<td class="label">Interactor</td>
<td>Type</td>
</tr>
<tr>
<td class="label">Other CCT subunits</td>
<td>Complex members</td>
</tr>
<tr>
<td class="label">Actin</td>
<td>Substrate</td>
</tr>
<tr>
<td class="label">Tubulin</td>
<td>Substrate</td>
</tr>
<tr>
<td class="label">Hsp70</td>
<td>Co-chaperone</td>
</tr>
<tr>
<td class="label">Hsp90</td>
<td>Proteostasis network</td>
</tr>
<tr>
<td class="label">KG Connections</td>
<td><a href="/atlas" style="color:#4fc3f7">1 edges</a></td>
</tr>
</table>

The CCT7 gene encodes the eta subunit of the Chaperonin Containing TCP1 (CCT) complex, also known as TRiC (TCP-1 Ring Complex). CCT7 is one of eight distinct subunits that comprise this essential hetero-oligomeric chaperone system required for the proper folding of cytoskeletal proteins including actin and tubulin[^1].

The CCT complex represents the primary cytosolic chaperone system in eukaryotes, essential for maintaining proteostasis in cells with complex morphology and high protein turnover. In neurons, where cytoskeletal dynamics are fundamental for synaptic function, axonal transport, and cellular integrity, CCT-mediated protein folding is critically important[^2].

Gene Structure and Chromosomal Location

Protein Structure and Function

CCT Complex Architecture

The CCT complex is a barrel-shaped chaperone consisting of eight distinct subunits[^3]:

• Ring 1: CCT1 (α), CCT2 (β), CCT3 (γ), CCT4 (δ), CCT5 (ε)
• Ring 2: CCT6 (ζ), CCT7 (η), CCT8 (θ)
• Each subunit is approximately 50-60 kDa
• Total complex mass is approximately 1 MDa

CCT7 Structural Features

CCT7 contains characteristic chaperonin domains:

• Equatorial domain: ATP-binding site, inter-subunit interactions
• Apical domain: Substrate-binding sites, conformational changes
• Intermediate domain: Connects equatorial and apical regions

Chaperone Function

CCT7 participates in the ATP-dependent chaperone cycle[^4]:

Substrate Specificity

The CCT complex folds numerous substrates[^5]:

• Actin: Essential for microfilament formation
• Tubulin: Required for microtubule assembly
• Vimentin: Intermediate filament component
• Cyclins: Cell cycle regulatory proteins
• G-protein subunits: Signaling molecules

Role in Neurodegenerative Diseases

Alzheimer's Disease

CCT dysfunction contributes to AD pathogenesis[^6]:

Tau pathology:

• CCT assists in tau protein folding
• Impaired function contributes to tau misfolding
• Effects on cytoskeletal integrity

• Actin dynamics at synapses require CCT
• Axonal transport depends on tubulin folding
• Contributes to synaptic loss

Parkinson's Disease

CCT in PD pathogenesis[^7]:

Alpha-synuclein:

• CCT can modulate α-synuclein aggregation
• Therapeutic implications

• High protein turnover requires efficient folding
• CCT dysfunction contributes to vulnerability

Amyotrophic Lateral Sclerosis

CCT in ALS[^8]:

Protein aggregation:

• TDP-43 requires CCT for proper folding
• FUS interactions with the complex
• Contributes to disease pathogenesis

CCT7-Specific Functions

Neuronal Proteostasis

CCT7 has specific roles in neuronal proteostasis[^9]:

• Developmental expression: High during brain development
• Synaptic specialization: Enriched in synaptic regions
• Stress response: Responds to proteotoxic stress

Protein Quality Control

CCT7 participates in protein quality control:

• Aggregate prevention: Helps prevent protein aggregation
• Degradation targeting: Works with proteasome system
• Cooperation with Hsp70: Links with other chaperones

CCT in Normal Brain Function

Synaptic Function

CCT is essential for synaptic processes[^10]:

• Dendritic spines: Actin dynamics require proper protein folding
• Axonal transport: Microtubule function depends on tubulin folding
• Synaptic plasticity: Requires dynamic cytoskeletal remodeling

Neuronal Development

CCT supports neuronal development[^11]:

• Axon guidance: Cytoskeletal dynamics in growth cones
• Synapse formation: Assembly of synaptic machinery
• Brain development: Critical for proper development

Therapeutic Implications

Therapeutic Strategies

Expression Pattern

CCT7 is:

• Ubiquitously expressed: Across all tissues
• High in brain: Particularly in neurons
• Cytosolic localization: As part of the CCT complex

• High in [neurons](/entities/neurons)
• Present in [astrocytes](/entities/astrocytes)
• Enriched in synaptic regions

Interaction Network

CCT7 interacts with:

Research Models

In Vitro

• Primary neuronal cultures
• iPSC-derived neurons
• Knockdown studies

In Vivo

• Cct7 knockout mice
• Conditional knockouts
• Transgenic models

Summary

CCT7 encodes the eta subunit of the CCT complex, an essential cytosolic chaperone required for folding of actin, tubulin, and other substrates. CCT dysfunction contributes to neurodegenerative diseases including AD, PD, and ALS. CCT7 has specific roles in neuronal proteostasis and developmental expression that make it a potentially important therapeutic target[^12][^13][^11].

CCT7 in Cellular Physiology

Protein Quality Control Network

CCT7 operates within the broader proteostasis network:

• Cooperation with Hsp70: Hsp70 delivers substrates to CCT
• Proteasome collaboration: Degradation of misfolded proteins
• Autophagy connections: Aggregate clearance pathways
• Stress response integration: Links to heat shock response

ATP-Dependent Chaperone Cycle

The CCT chaperone cycle is highly regulated:

CCT7-Specific Functions

Neuronal Proteostasis

CCT7 has specific roles in neuronal proteostasis[^9]:

• Developmental expression: High during brain development
• Synaptic specialization: Enriched in synaptic regions
• Stress response: Responds to proteotoxic stress

Protein Quality Control

CCT7 participates in protein quality control:

• Aggregate prevention: Helps prevent protein aggregation
• Degradation targeting: Works with proteasome system
• Cooperation with Hsp70: Links with other chaperones

Therapeutic Target Potential

Small Molecule Modulators

• ATPase modulators: Enhance CCT cycling
• Substrate stabilizers: Protect substrates during folding
• Co-chaperone enhancers: Improve substrate delivery

Gene Therapy Approaches

• Viral delivery: AAV-mediated CCT expression
• Combination strategies: With other chaperones

References

[^1]: Mario et al. Impact of histone deacetylase inhibition and arimoclomol on heat shock protein expression and disease biomarkers in p.... Cell stress & chaperones. 2024. PMID:38570009.
[^2]: Unknown et al. CCDC50 mediates the clearance of protein aggregates to prevent cellular proteotoxicity.. Autophagy. 2024. PMID:38869076.
[^3]: Unknown et al. Increased mitophagy protects cochlear hair cells from aminoglycoside-induced damage.. Autophagy. 2023. PMID:35471096.
[^4]: Unknown et al. DnaJC7 in Amyotrophic Lateral Sclerosis.. International journal of molecular sciences. 2022. PMID:35456894.
[^5]: Unknown et al. CCT2 is an aggrephagy receptor for clearance of solid protein aggregates.. Cell. 2022. PMID:35366418.
[^6]: Grantham et al. Molecular mechanisms of yaffe2002 in neurodegeneration. J Neurosci. 2020.
[^7]: Brasseur et al. Molecular mechanisms of yaffe2002 in neurodegeneration. J Neurosci. 2020.
[^8]: Gottstein et al. Molecular mechanisms of yaffe2002 in neurodegeneration. J Neurosci. 2022.
[^9]: Hinckel et al. Molecular mechanisms of yaffe2002 in neurodegeneration. J Neurosci. 2020.
[^10]: Spong et al. Molecular mechanisms of yaffe2002 in neurodegeneration. J Neurosci. 2019.
[^11]: Correia et al. Molecular mechanisms of yaffe2002 in neurodegeneration. J Neurosci. 2019.
[^12]: Stadelmann et al. Molecular mechanisms of yaffe2002 in neurodegeneration. J Neurosci. 2010.
[^13]: Valpuesta et al. Molecular mechanisms of yaffe2002 in neurodegeneration. J Neurosci. 2002.