ArticleCell stress & chaperones2013
Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro.
Article in Cell stress & chaperones, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- The Human Lens Fiber Cytoskeletome Reveals Neuronal Signatures and the Presence of Chaperonins, Proteasome, Signaling, and Redox Regulators.Investigative ophthalmology & visual science · 2026Article
- Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.Communications biology · 2023Article
- Anticarin-Acta pharmaceutica Sinica. B · 2022Article
- The TRiCky Business of Protein Folding in Health and Disease.Frontiers in cell and developmental biology · 2022Review
- Native mass spectrometry analyses of chaperonin complex TRiC/CCT reveal subunit N-terminal processing and re-association patterns.Scientific reports · 2021Article
- TCP1γ Subunit Is Indispensable for Growth and Infectivity of Leishmania donovani.Antimicrobial agents and chemotherapy · 2020Article
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- An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytes.Nature communications · 2017Article
- Regulation of GPCR expression through an interaction with CCT7, a subunit of the CCT/TRiC complex.Molecular biology of the cell · 2016Article
- Chaperonin TRiC/CCT Recognizes Fusion Oncoprotein AML1-ETO through Subunit-Specific Interactions.Biophysical journal · 2016Article
- Chaperonin TRiC/CCT Modulates the Folding and Activity of Leukemogenic Fusion Oncoprotein AML1-ETO.The Journal of biological chemistry · 2016Article
- Lecithin Prevents Cortical Cytoskeleton Reorganization in Rat Soleus Muscle Fibers under Short-Term Gravitational Disuse.PloS one · 2016Article
- Improved Peak Detection and Deconvolution of Native Electrospray Mass Spectra from Large Protein Complexes.Journal of the American Society for Mass Spectrometry · 2015Article
- Characterization of CCTα and evaluating its expression in the mud crab Scylla paramamosain when challenged by low temperatures alone and in combination with high and low salinity.Cell stress & chaperones · 2015Article
- Biochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 associated with hereditary sensory neuropathy.The Journal of biological chemistry · 2014Article
- The βγ-crystallins: native state stability and pathways to aggregation.Progress in biophysics and molecular biology · 2014Review
- Chaperonin-containing TCP-1 complex directly binds to the cytoplasmic domain of the LOX-1 receptor.FEBS letters · 2014Article
- Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.The Journal of biological chemistry · 2013Article
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3 authors.
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Abstract
Archaeal and eukaryotic cytosols contain group II chaperonins, which have a double-barrel structure and fold proteins inside a cavity in an ATP-dependent manner. The most complex of the chaperonins, the eukaryotic TCP-1 ring complex (TRiC), has eight different subunits, chaperone containing TCP-1 (CCT1-8), that are arranged so that there is one of each subunit per ring. Aspects of the structure and function of the bovine and yeast TRiC have been characterized, but studies of human TRiC have been limited. We have isolated and purified endogenous human TRiC from HeLa suspension cells. This purified human TRiC contained all eight CCT subunits organized into double-barrel rings, consistent with what has been found for bovine and yeast TRiC. The purified human TRiC is active as demonstrated by the luciferase refolding assay. As a more stringent test, the ability of human TRiC to suppress the aggregation of human γD-crystallin was examined. In addition to suppressing off-pathway aggregation, TRiC was able to assist the refolding of the crystallin molecules, an activity not found with the lens chaperone, α-crystallin. Additionally, we show that human TRiC from HeLa cell lysate is associated with the heat shock protein 70 and heat shock protein 90 chaperones. Purification of human endogenous TRiC from HeLa cells will enable further characterization of this key chaperonin, required for the reproduction of all human cells.
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