ArticleNature communications2015
Cytoplasmic TAF2-TAF8-TAF10 complex provides evidence for nuclear holo-TFIID assembly from preformed submodules.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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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
60 citing papers in PubMed, 93 citations in OpenAlex.
- Article
- Step-brothers in arms, SAGA and ATAC co-activator complexes, use different strategies.The EMBO journal · 2026Review
- High-resolution binding data of TFIID and cofactors show promoter-specific differences in vivo.Research square · 2026Article
- A recently evolved TAF8 isoform arising from anbioRxiv : the preprint server for biology · 2026Article
- Peri-implantitis: a systemic burden for our patients.Frontiers in dental medicine · 2026Review
- High-resolution binding data of TFIID and cofactors show promoter-specific differencesbioRxiv : the preprint server for biology · 2025Article
- Probing the extent of importin-α targeting of the TAF8 NLS by eliminating its cationic net-charge.Protein science : a publication of the Protein Society · 2025Article
- Novel fetal phenotype of TAF8 deficiency.European journal of human genetics : EJHG · 2025Article
- The TATA-box binding protein-associated factor TAF12b facilitates the degradation of type B response regulators to negatively regulate cytokinin signaling.Plant communications · 2024Article
- RNA polymerase II transcription initiation in holo-TFIID-depleted mouse embryonic stem cells.Cell reports · 2024Article
- The roles of TAF1 in neuroscience and beyond.Royal Society open science · 2024Review
- TAF2, within the TFIID complex, regulates the expression of a subset of protein-coding genes.Cell death discovery · 2024Article
- Inducing mitochondriopathy-like damages by transformable nucleopeptide nanoparticles for targeted therapy of bladder cancer.National science review · 2024Article
- Exploiting the endogenous yeast nuclear proteome to identify short linear motifs in vivo.Cell reports methods · 2023Article
- ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct.Cell reports · 2023Article
- Binding of viral nuclear localization signal peptides to importin-α nuclear transport protein.Biophysical journal · 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
- Multiple intermolecular interactions facilitate rapid evolution of essential genes.Nature ecology & evolution · 2023Article
- Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID.bioRxiv : the preprint server for biology · 2023Article
Corrections and comments
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Authors and funding
16 authors at 9 institutions in 2 countries.
Funding
Abstract
General transcription factor TFIID is a cornerstone of RNA polymerase II transcription initiation in eukaryotic cells. How human TFIID-a megadalton-sized multiprotein complex composed of the TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs)-assembles into a functional transcription factor is poorly understood. Here we describe a heterotrimeric TFIID subcomplex consisting of the TAF2, TAF8 and TAF10 proteins, which assembles in the cytoplasm. Using native mass spectrometry, we define the interactions between the TAFs and uncover a central role for TAF8 in nucleating the complex. X-ray crystallography reveals a non-canonical arrangement of the TAF8-TAF10 histone fold domains. TAF2 binds to multiple motifs within the TAF8 C-terminal region, and these interactions dictate TAF2 incorporation into a core-TFIID complex that exists in the nucleus. Our results provide evidence for a stepwise assembly pathway of nuclear holo-TFIID, regulated by nuclear import of preformed cytoplasmic submodules.
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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.