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Target intelligence / Profile preview
Chaperonin containing TCP1 subunit 5 (CCT5)
- Target
- CCT5
- Molecular classification
- Molecular chaperone, Chaperonin complex (type II chaperonin, cytosolic), Protein folding complex
01
Overview
Chaperonin containing TCP1 subunit 5 (CCT5) is a core component of the chaperonin containing TCP1 complex (CCT/TRiC), a type II cytosolic chaperonin critical for ATP-dependent folding of cytoskeletal proteins such as actin and tubulin as well as other substrates, including those involved in cell signaling and organelle biogenesis. CCT5 assists the assembly of multi-protein structures, including the BBSome and mTOR complexes, thereby influencing diverse cellular processes, such as cytoskeletal organization, telomere regulation, and cell motility. Mutations in CCT5 are linked to hereditary sensory neuropathies with spastic paraplegia and contribute to pathologies in neurodegenerative disease, muscle atrophy, and cancer progression[1][2][3][4][5][6].
- Other names
- T-complex protein 1 subunit epsilonCCTEKIAA0098TCP-1-epsilonHEL-S-69HSNSPPNAS-102epididymis secretory protein Li 69
02
Biological functions
Protein folding (ATP-dependent)Cytoskeletal protein folding (actin, tubulin)Regulation of actin cytoskeleton and myofilament assemblyTelomere maintenance (via WRAP53/TCAB1 folding)Assembly of macromolecular complexes (e.g., BBSome for ciliogenesis)
03
Disease associations
Neurodegenerative disease (e.g., Alzheimer’s disease)Hereditary sensory and autonomic neuropathy with spastic paraplegiaCancer (e.g., gastric cancer metastasis, breast cancer, glioma, HCC)Muscle atrophyInfection (e.g., Legionella pneumophila)
04
Safety considerations
Mutations can cause hereditary sensory and autonomic neuropathies with spastic paraplegiaPotential for off-target effects if inhibition disrupts essential protein folding/assembly
05
Biomarkers
Prognostic gene signature in various cancers (e.g., hepatocellular carcinoma)
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