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Target intelligence / Profile preview
T-complex protein Ring Complex (TRiC)
- Target
- TRiC
- Molecular classification
- Chaperonin, Group II chaperonin
01
Overview
The T-complex protein Ring Complex (TRiC), also known as Chaperonin Containing TCP-1 (CCT), is a eukaryotic group II chaperonin responsible for folding newly synthesized proteins. It is a double-ringed barrel structure, with each ring consisting of eight unique but homologous subunits. TRiC uses ATP hydrolysis to facilitate proper protein folding within its central cavity, primarily acting on actin, tubulin, and other select client proteins. It plays a crucial role in proteostasis, preventing protein aggregation, and its dysfunction is linked to diseases such as Huntington’s disease and cancer.
- Other names
- CCTChaperonin Containing TCP-1TCP-1 ring complex
02
Mechanism of action
ATP-dependent protein folding within a central cavity, utilizing conformational changes mediated by ATP hydrolysis; does not require a co-chaperonin.
03
Biological functions
Protein foldingProteostasisPreventing protein aggregationCytoskeletal protein folding (actin, tubulin)Cell cycle regulationTranscription initiationSignal transductionAutophagyEpigenetic regulationCellular immortalityT-cell immunityApoptosis suppression
04
Disease associations
Neurodegenerative diseaseHuntington’s diseaseCancer
05
Safety considerations
Knockdown or dysfunction can induce apoptosis or impair cell proliferation.
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