ArticleNature structural & molecular biology2016
Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
41 citing papers in PubMed, 76 citations in OpenAlex.
- TRiC-assisted folding of class I HDAC family proteins regulated by distinct co-chaperone and cofactor networks.Science advances · 2026Article
- The Open Conformation of CCT: How to Achieve High Resolution Using CryoEM.Methods in molecular biology (Clifton, N.J.) · 2026Article
- CryoEM Strategies for Elucidating the Closed State Architecture of CCT.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Protein folding by the CCT/TRiC chaperone complex.Current opinion in structural biology · 2025Review
- The conformational landscape of TRiC ring-opening and its underlying stepwise mechanism revealed by cryo-EM.QRB discovery · 2025Article
- Role of the chaperonin TCP-1 ring complex in protein aggregation and neurodegeneration.Frontiers in molecular neuroscience · 2025Review
- The role of molecular chaperone CCT/TRiC in translation elongation: A literature review.Heliyon · 2024Review
- The structural basis of eukaryotic chaperonin TRiC/CCT: Action and folding.Molecules and cells · 2024Review
- CCT2 prevented β-catenin proteasomal degradation to sustain cancer stem cell traits and promote tumor progression in epithelial ovarian cancer.Molecular biology reports · 2024Article
- Molecular Dynamics Mappings of the CCT/TRiC Complex-Mediated Protein Folding Cycle Using Diffracted X-ray Tracking.International journal of molecular sciences · 2023Article
- A hierarchical assembly pathway directs the unique subunit arrangement of TRiC/CCT.Molecular cell · 2023Article
- Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.Communications biology · 2023Article
- Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.Science advances · 2023Article
- Structural and Dynamic Disturbances Revealed by Molecular Dynamics Simulations Predict the Impact on Function of CCT5 Chaperonin Mutations Associated with Rare Severe Distal Neuropathies.International journal of molecular sciences · 2023Article
- Mechanistic insights into protein folding by the eukaryotic chaperonin complex CCT.Biochemical Society transactions · 2022Review
- Snapshots of actin and tubulin folding inside the TRiC chaperonin.Nature structural & molecular biology · 2022Article
- Hidden information on protein function in censuses of proteome foldedness.Nature communications · 2022Article
- Disruption of actin dynamics induces autophagy of the eukaryotic chaperonin TRiC/CCT.Cell death discovery · 2022Article
- Developing Graphene Grids for Cryoelectron Microscopy.Frontiers in molecular biosciences · 2022Review
- Chaperonin containing TCP-1 (CCT/TRiC) is a novel therapeutic and diagnostic target for neuroblastoma.Frontiers in oncology · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The eukaryotic chaperonin TRiC (or CCT) assists in the folding of 10% of cytosolic proteins. Here we present two cryo-EM structures of Saccharomyces cerevisiae TRiC in a newly identified nucleotide partially preloaded (NPP) state and in the ATP-bound state, at 4.7-Å and 4.6-Å resolution, respectively. Through inner-subunit eGFP tagging, we identified the subunit locations in open-state TRiC and found that the CCT2 subunit pair forms an unexpected Z shape. ATP binding induces a dramatic conformational change on the CCT2 side, thereby suggesting that CCT2 plays an essential role in TRiC allosteric cooperativity. Our structural and biochemical data reveal a staggered ATP binding mechanism of TRiC with preloaded nucleotide on the CCT6 side of NPP-TRiC and demonstrate that TRiC has evolved into a complex that is structurally divided into two sides. This work offers insight into how the TRiC nucleotide cycle coordinates with its mechanical cycle in preparing folding intermediates for further productive folding.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.