ArticleNature structural & molecular biology2008
Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT.
Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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Who cites it
49 citing papers in PubMed, 1 synthesis or guideline pooled it, 93 citations in OpenAlex.
- Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells.Cell stress & chaperones · 2011Pooled it
- Disease-causing mutations in the G protein β5 β-propeller disrupt its chaperonin-mediated folding trajectory.bioRxiv : the preprint server for biology · 2025Article
- Molecular, structural, and functional characterization of delta subunit of T-complex protein-1 fromInfection and immunity · 2024Article
- The role of molecular chaperone CCT/TRiC in translation elongation: A literature review.Heliyon · 2024Review
- Visualizing the chaperone-mediated folding trajectory of the G protein β5 β-propeller.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
- The TRiCky Business of Protein Folding in Health and Disease.Frontiers in cell and developmental biology · 2022Review
- Interaction with the CCT chaperonin complex limits APOBEC3A cytidine deaminase cytotoxicity.EMBO reports · 2021Article
- An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly.Nature communications · 2019Article
- Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle.Science advances · 2018Article
- Time-Resolved Measurement of the ATP-Dependent Motion of the Group II Chaperonin by Diffracted Electron Tracking.International journal of molecular sciences · 2018Article
- Single-Ring Intermediates Are Essential for Some Chaperonins.Frontiers in molecular biosciences · 2018Article
- Asymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiC.PloS one · 2017Article
- Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.Nature structural & molecular biology · 2016Article
- Structural and mechanistic insights into human splicing factor SF3b complex derived using an integrated approach guided by the cryo-EM density maps.RNA biology · 2016Article
- Ring Separation Highlights the Protein-Folding Mechanism Used by the Phage EL-Encoded Chaperonin.Structure (London, England : 1993) · 2016Article
- The Mechanism and Function of Group II Chaperonins.Journal of molecular biology · 2015Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
All chaperonins mediate ATP-dependent polypeptide folding by confining substrates within a central chamber. Intriguingly, the eukaryotic chaperonin TRiC (also called CCT) uses a built-in lid to close the chamber, whereas prokaryotic chaperonins use a detachable lid. Here we determine the mechanism of lid closure in TRiC using single-particle cryo-EM and comparative protein modeling. Comparison of TRiC in its open, nucleotide-free, and closed, nucleotide-induced states reveals that the interdomain motions leading to lid closure in TRiC are radically different from those of prokaryotic chaperonins, despite their overall structural similarity. We propose that domain movements in TRiC are coordinated through unique interdomain contacts within each subunit and, further, these contacts are absent in prokaryotic chaperonins. Our findings show how different mechanical switches can evolve from a common structural framework through modification of allosteric networks.
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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.