ArticleMolecular and cellular biology2005
The nuclear import of TAF10 is regulated by one of its three histone fold domain-containing interaction partners.
Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 53 citations in OpenAlex.
- Step-brothers in arms, SAGA and ATAC co-activator complexes, use different strategies.The EMBO journal · 2026Review
- A recently evolved TAF8 isoform arising from anbioRxiv : the preprint server for biology · 2026Article
- 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
- Loss-of-function variants affecting the STAGA complex component SUPT7L cause a developmental disorder with generalized lipodystrophy.Human genetics · 2024Article
- Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID.Nature structural & molecular biology · 2023Article
- Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID.bioRxiv : the preprint server for biology · 2023Article
- Article
- Loss of TAF8 causes TFIID dysfunction and p53-mediated apoptotic neuronal cell death.Cell death and differentiation · 2022Article
- Article
- Recent insights into the structure of TFIID, its assembly, and its binding to core promoter.Current opinion in structural biology · 2020Review
- Co-translational assembly of mammalian nuclear multisubunit complexes.Nature communications · 2019Article
- Homozygous TAF8 mutation in a patient with intellectual disability results in undetectable TAF8 protein, but preserved RNA polymerase II transcription.Human molecular genetics · 2018Article
- Imaging of native transcription factors and histone phosphorylation at high resolution in live cells.The Journal of cell biology · 2018Article
- Sharing the SAGA.Trends in biochemical sciences · 2017Review
- The TAF10-containing TFIID and SAGA transcriptional complexes are dispensable for early somitogenesis in the mouse embryo.Development (Cambridge, England) · 2017Article
- TAF10 and TAF10b partially redundant roles during Drosophila melanogaster morphogenesis.Transcription · 2017Article
- Zooming in on Transcription Preinitiation.Journal of molecular biology · 2016Review
- TAF10 Interacts with the GATA1 Transcription Factor and Controls Mouse Erythropoiesis.Molecular and cellular biology · 2015Article
- Cytoplasmic TAF2-TAF8-TAF10 complex provides evidence for nuclear holo-TFIID assembly from preformed submodules.Nature communications · 2015Article
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6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TFIID, comprising the TATA box binding protein (TBP) and 13 TBP-associated factors (TAFs), plays a role in nucleation in the assembly of the RNA polymerase II preinitiation complexes on protein-encoding genes. TAFs are shared among other transcription regulatory complexes (e.g., SAGA, TBP-free TAF-containing complex [TFTC], STAGA, and PCAF/GCN5). Human TAF10, a subunit of both TFIID and TFTC, has three histone fold-containing interaction partners: TAF3, TAF8, and SPT7Like (SPT7L). In human cells, exogenously expressed TAF10 remains rather cytoplasmic and leptomycin B does not affect this localization. By using fluorescent fusion proteins, we show that TAF10 does not have an intrinsic nuclear localization signal (NLS) and needs one of its three interaction partners to be transported into the nucleus. When the NLS sequences of either TAF8 or SPT7L are mutated, TAF10 remains cytoplasmic, but a heterologous NLS can drive TAF10 into the nucleus. Experiments using fluorescence recovery after photobleaching show that TAF10 does not associate with any cytoplasmic partner but that once transported into the nucleus it binds to nuclear structures. TAF10 binding to importin beta in vitro is dependent on the coexpression of either TAF8 or TAF3, but not SPT7L. The cytoplasmic-nuclear transport of TAF10 is naturally observed during the differentiation of adult male germ cells. Thus, here we describe a novel role of the three mammalian interacting partners in the nuclear localization of TAF10, and our data suggest that a complex network of regulated cytoplasmic associations may exist among these factors and that this network is important for the composition of different TFIID and TFTC-type complexes in the nucleus.
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