ArticleNature structural & molecular biology2018
Chaperonin CCT checkpoint function in basal transcription factor TFIID assembly.
Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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.
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.
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Who cites it
33 citing papers in PubMed, 60 citations in OpenAlex.
- TRiC/CCT chaperonin governs RNA polymerase II activity in the nucleus to support RNA homeostasis.Molecular cell · 2026Article
- MSTO1 functions as a TRiC assembly factor linking cytosolic proteostasis to mitochondrial function.bioRxiv : the preprint server for biology · 2026Article
- TRiC-assisted folding of class I HDAC family proteins regulated by distinct co-chaperone and cofactor networks.Science advances · 2026Article
- High-resolution binding data of TFIID and cofactors show promoter-specific differences in vivo.Research square · 2026Article
- High-resolution binding data of TFIID and cofactors show promoter-specific differencesbioRxiv : the preprint server for biology · 2025Article
- LncRNA938/ TAF9/TTK axis promotes EMT and serves as a therapeutic target in hepatoblastoma.Journal of translational medicine · 2025Article
- A function of TPL/TBL1-type corepressors is to nucleate the assembly of the preinitiation complex.The Journal of cell biology · 2025Article
- O-GlcNAc transferase congenital disorder of glycosylation (OGT-CDG): Potential mechanistic targets revealed by evaluating the OGT interactome.The Journal of biological chemistry · 2024Review
- Genome-scale exon perturbation screens uncover exons critical for cell fitness.Molecular cell · 2024Article
- A conserved function of corepressors is to nucleate assembly of the transcriptional preinitiation complex.bioRxiv : the preprint server for biology · 2024Article
- Revisiting the chaperonin T-complex protein-1 ring complex in human health and disease: A proteostasis modulator and beyond.Clinical and translational medicine · 2024Review
- Simple model systems reveal conserved mechanisms of Alzheimer's disease and related tauopathies.Molecular neurodegeneration · 2023Review
- Release of Histone H3K4-reading transcription factors from chromosomes in mitosis is independent of adjacent H3 phosphorylation.Nature communications · 2023Article
- ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct.Cell reports · 2023Article
- ATAC and SAGA coactivator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct.bioRxiv : the preprint server for biology · 2023Article
- Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID.Nature structural & molecular biology · 2023Article
- Alternative mRNA Splicing Controls the Functions of the Histone H3K27 Demethylase UTX/KDM6A.Cancers · 2023Article
- Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID.bioRxiv : the preprint server for biology · 2023Article
- Article
- Tandem Affinity Purification (TAP) of Interacting Prey Proteins with FLAG- and HA-Tagged Bait Proteins.Methods in molecular biology (Clifton, N.J.) · 2023Article
Corrections and comments
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Authors and funding
14 authors at 6 institutions in 6 countries.
Funding
Abstract
TFIID is a cornerstone of eukaryotic gene regulation. Distinct TFIID complexes with unique subunit compositions exist and several TFIID subunits are shared with other complexes, thereby conveying precise cellular control of subunit allocation and functional assembly of this essential transcription factor. However, the molecular mechanisms that underlie the regulation of TFIID remain poorly understood. Here we use quantitative proteomics to examine TFIID submodules and assembly mechanisms in human cells. Structural and mutational analysis of the cytoplasmic TAF5-TAF6-TAF9 submodule identified novel interactions that are crucial for TFIID integrity and for allocation of TAF9 to TFIID or the Spt-Ada-Gcn5 acetyltransferase (SAGA) co-activator complex. We discover a key checkpoint function for the chaperonin CCT, which specifically associates with nascent TAF5 for subsequent handover to TAF6-TAF9 and ultimate holo-TFIID formation. Our findings illustrate at the molecular level how multisubunit complexes are generated within the cell via mechanisms that involve checkpoint decisions facilitated by a chaperone.
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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.