ArticleProceedings of the National Academy of Sciences of the United States of America2007
Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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.
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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
29 citing papers in PubMed, 42 citations in OpenAlex.
- The mechanism of YAP/TAZ transactivation and dual targeting for cancer therapy.Nature communications · 2025Article
- Interaction modules that impart specificity to disordered protein.Trends in biochemical sciences · 2023Review
- De novo putative loss-of-function variants in TAF4 are associated with a neuro-developmental disorder.Human mutation · 2022Article
- αα-hub coregulator structure and flexibility determine transcription factor binding and selection in regulatory interactomes.The Journal of biological chemistry · 2022Article
- What do Transcription Factors Interact With?Journal of molecular biology · 2021Review
- Analysis of TATA-box binding protein associated factor 4b gene mutations in a Chinese population with nonobstructive azoospermia.Medicine · 2020Observational
- Structure of human TFIID and mechanism of TBP loading onto promoter DNA.Science (New York, N.Y.) · 2018Article
- Identification of heteromolecular binding sites in transcription factors Sp1 and TAF4 using high-resolution nuclear magnetic resonance spectroscopy.Protein science : a publication of the Protein Society · 2017Article
- Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1.The Journal of biological chemistry · 2017Article
- New insights into transcriptional and leukemogenic mechanisms of AML1-ETO and E2A fusion proteins.Frontiers in biology · 2016Article
- Zooming in on Transcription Preinitiation.Journal of molecular biology · 2016Review
- Article
- Structural basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2015Review
- Diversity in TAF proteomics: consequences for cellular differentiation and migration.International journal of molecular sciences · 2014Review
- A TAF4 coactivator function for E proteins that involves enhanced TFIID binding.Genes & development · 2013Article
- Article
- Article
- TFIID TAF6-TAF9 complex formation involves the HEAT repeat-containing C-terminal domain of TAF6 and is modulated by TAF5 protein.The Journal of biological chemistry · 2012Article
- Direct transactivator-transcription factor IID (TFIID) contacts drive yeast ribosomal protein gene transcription.The Journal of biological chemistry · 2010Article
- Mammalian SWI/SNF--a subunit BAF250/ARID1 is an E3 ubiquitin ligase that targets histone H2B.Molecular and cellular biology · 2010Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
TBP-associated factor 4 (TAF4), an essential subunit of the TFIID complex acts as a coactivator for multiple transcriptional regulators, including Sp1 and CREB. However, little is known regarding the structural properties of the TAF4 subunit that lead to the coactivator function. Here, we report the crystal structure at 2.0-A resolution of the human TAF4-TAFH domain, a conserved domain among all metazoan TAF4, TAF4b, and ETO family members. The hTAF4-TAFH structure adopts a completely helical fold with a large hydrophobic groove that forms a binding surface for TAF4 interacting factors. Using peptide phage display, we have characterized the binding preference of the hTAF4-TAFH domain for a hydrophobic motif, DPsiPsizetazetaPsiPhi, that is present in a number of nuclear factors, including several important transcriptional regulators with roles in activating, repressing, and modulating posttranslational modifications. A comparison of the hTAF4-TAFH structure with the homologous ETO-TAFH domain reveals several critical residues important for hTAF4-TAFH target specificity and suggests that TAF4 has evolved in response to the increased transcriptional complexity of metazoans.
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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.