Any feedback?
Literature summary for 3.6.4.B10 extracted from
- Contribution of the type II chaperonin, TRiC/CCT, to oncogenesis (2015), Int. J. Mol. Sci., 16, 26706-26720 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structure analysis of the open conformation of the mammalian chaperonin CCT in complex with tubulin, overview | Bos taurus |
| structure analysis of the open conformation of the mammalian chaperonin CCT in complex with tubulin, overview | Homo sapiens |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Bos taurus |  |
| Mg2+ | required | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Bos taurus | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Homo sapiens | - |
ADP + phosphate | - |
? | |
| additional information | Homo sapiens | TRiC binds to and modulates cancer related proteins | ? | - |
- |
|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | Q32L40 AND Q3ZBH0 AND Q3T0K2 AND F1N0E5 AND F1MWD3 AND Q3MHL7 AND Q2NKZ1 AND Q3ZCI9 | genes CCT1-5, 6A, 7, and 8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta | - |
| Homo sapiens | P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990 | genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| HeLa cell | - |
Homo sapiens | - |
| Hep-G2 cell | - |
Homo sapiens | - |
| Hs-578T cell | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Bos taurus | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Homo sapiens | ADP + phosphate | - |
? | |
| additional information | TRiC binds to and modulates cancer related proteins | Homo sapiens | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterohexadecamer | TRiC is a double-ringed structure composed of eight homologous but distinct subunits (CCT1-8) | Bos taurus |
| heterohexadecamer | TRiC is a double-ringed structure composed of eight homologous but distinct subunits (CCT1-8) | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CCT | - |
Bos taurus |
| CCT | - |
Homo sapiens |
| T-complex protein-1 ring complex | - |
Bos taurus |
| T-complex protein-1 ring complex | - |
Homo sapiens |
| TRiC/CCT | - |
Bos taurus |
| TRiC/CCT | - |
Homo sapiens |
| type II chaperonin | - |
Bos taurus |
| type II chaperonin | - |
Homo sapiens |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Bos taurus | subunit CCT1 is transcriptionally modulated by the driver oncogene, phosphatidylinositide 3-kinases (PI3K) | additional information |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the eukaryotic chaperonin family includes the type I chaperonin, HSP60, and the type II hetero-oligomeric chaperonin, TRiC (T-complex protein-1 ring complex, also known as CCT). Chaperones often function as large protein complexes that include other proteins called co-chaperones | Bos taurus |
| evolution | the eukaryotic chaperonin family includes the type I chaperonin, HSP60, and the type II hetero-oligomeric chaperonin, TRiC (T-complex protein-1 ring complex, also known as CCT). Chaperones often function as large protein complexes that include other proteins called co-chaperones | Homo sapiens |
| malfunction | knockdown of TRiC in HEPG2 cells reduces their sensitivity to interleukin-6 induced STAT3 activation | Homo sapiens |
| metabolism | chaperone network involving HSP70, HSP90, and TRiC, overview | Bos taurus |
| metabolism | chaperone network involving HSP70, HSP90, and TRiC, overview | Homo sapiens |
| additional information | individual subunits of TRiC have been shown to have protein-folding capacity | Homo sapiens |
| additional information | large conformational changes occur upon nucleotide binding and hydrolysis. The conformational cycling begins with the binding of ATP and a transition of the complex to the closed conformation required for ATP hydrolysis to bring the lid helices into close proximity. Opening of the lid occurs in conjunction with releasing ADP from the active site. The complex can exist in an asymmetrical conformation with one ring closed and one open even during ATP cycling conditions, suggesting a inter-ring allosteric model mediated through a two-stroke mechanism. Molecular architecture of TRiC/CCT from the crystal structure, PDB ID 2XSM | Bos taurus |
| physiological function | chaperonins are essential for cell survival as they protect against proteotoxic stress that may lead to protein misfolding and aggregation. Chaperonin TRiC (T-complex protein-1 ring complex, also known as CCT) in the development and progression of cancer. Type II chaperonin TRiC/CCT contributes to oncogenesis. TRiC assists productive folding of substrate proteins by undergoing conformational changes that are ATP-dependent. Interaction of TRiC with p53 promotes the protein folding and activity of p53, a tumor suppressor protein that plays a critical role in preventing malignant cancer cell development. p53 primarily functions as a transcription factor that modulates the expression of a variety of genes involved in cellular responses such as cell-cycle arrest and apoptosis. Contribution of TRiC to mutant p53-mediated oncogenesis is not as straightforward as it is for STAT3. TRiC plays a critical role in the regulation of cell cycle progression and modulates cell cycle regulatory proteins | Bos taurus |
| physiological function | chaperonins are essential for cell survival as they protect against proteotoxic stress that may lead to protein misfolding and aggregation. Chaperonin TRiC (T-complex protein-1 ring complex, also known as CCT) is involved in the development and progression of cancer mediated through its critical interactions with oncogenic clients, it modulates growth deregulation, apoptosis, and genome instability in cancer cells. Type II chaperonin TRiC/CCT contributes to oncogenesis. TRiC assists productive folding of substrate proteins by undergoing conformational changes that are ATP-dependent. Interaction of TRiC with p53 promotes the protein folding and activity of p53, a tumor suppressor protein that plays a critical role in preventing malignant cancer cell development. p53 primarily functions as a transcription factor that modulates the expression of a variety of genes involved in cellular responses such as cell-cycle arrest and apoptosis. Contribution of TRiC to mutant p53-mediated oncogenesis is not as straightforward as it is for STAT3. TRiC contributes to STAT protein folding and function, STAT3 requires TRiC for folding and proper functioning. TRiC plays a critical role in the regulation of cell cycle progression and modulates cell cycle regulatory proteins. HSP70 and TRiC appear to function sequentially in the Von Hippel-Lindau protein (VHL) folding pathway, with loss of HSP70 function blocking association with TRiC and loss of TRiC function having no effect on HSP70 association. TRiC subunits, CCT2 and CCT1, are essential for survival and proliferation of breast cancer. Chaperonin TRiC works as an assembly station for the tumor suppressor protein, VHL (Von Hippel-Lindau), mechanism, overview. TRiC chaperonin contributes to carcinogenesis through its contribution to STAT3 signaling | Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
