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TAF4 RNA polymerase II, TATA box binding protein

TAF4, TAFII130, hTAF(II)135, TAF(II)135, hTAFII130
Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes one of the larger subunits of TFIID that has been shown to potentiate transcriptional activation by retinoic acid, thyroid hormone and vitamin D3 receptors. In addition, this subunit interacts with the transcription factor CREB, which has a glutamine-rich activation domain, and binds to other proteins containing glutamine-rich regions. Aberrant binding to this subunit by proteins with expanded polyglutamine regions has been suggested as one of the pathogenetic mechanisms underlying a group of neurodegenerative disorders referred to as polyglutamine diseases. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: TBP, TAF, POLYMERASE, CREB, CAN
Papers on TAF4
TAF4 controls differentiation of human neural progenitor cells through hTAF4-TAFH activity.
Palm et al., Tallinn, Estonia. In J Mol Neurosci, 2015
Expression of general transcription factor and co-activator TAF4 varies during development and in the processes of cell differentiation with suggested connection to neurodegenerative diseases.
A special member of the rice SRO family, OsSRO1c, mediates responses to multiple abiotic stresses through interaction with various transcription factors.
Xiong et al., Wuhan, China. In Plant Mol Biol, 2014
SRO proteins are characterized by containing poly (ADP-ribose) polymerase catalytic (PARP) and C-terminal RCD1-SRO-TAF4 domains, and can be classified into two groups and five subgroups on the basis of their PARP domain.
Targeting TBP-Associated Factors in Ovarian Cancer.
Freiman et al., Providence, United States. In Front Oncol, 2013
TAF4, which is altered in 66% of HGSC, is crucial for the stability of the TFIID complex and helps drive dedifferentiation of mouse embryonic fibroblasts to induced pluripotent stem cells.
Diversity in TAF proteomics: consequences for cellular differentiation and migration.
Palm et al., Tallinn, Estonia. In Int J Mol Sci, 2013
In this review, we focus on the role of TATA-box associated factor 4 (TAF4) and its functional isoforms generated by alternative splicing in controlling lineage-specific differentiation of normal mesenchymal stem cells and cancer stem cells.
TAF4, a subunit of transcription factor II D, directs promoter occupancy of nuclear receptor HNF4A during post-natal hepatocyte differentiation.
Davidson et al., Illkirch-Graffenstaden, France. In Elife, 2013
The functions of the TAF subunits of mammalian TFIID in physiological processes remain poorly characterised.
TAF4 inactivation reveals the 3 dimensional growth promoting activities of collagen 6A3.
Davidson et al., Illkirch-Graffenstaden, France. In Plos One, 2013
In MEFs where the TAF4 subunit of general transcription factor IID (TFIID) has been inactivated, elevated Col6a3 expression prevents contact inhibition promoting their 3 dimensional growth as foci and fibrospheres.
Quantitative proteomic analysis of the Anopheles gambiae (Diptera: Culicidae) midgut infected with o'nyong-nyong virus.
Hong et al., New Orleans, United States. In J Med Entomol, 2013
Of interest, analysis revealed molecular pathways possibly targeted by virus proteins, such as those involving TAF4 and DNA polymerase phi proteins.
Structural bioinformatics of the general transcription factor TFIID.
Wyrwicz et al., Warsaw, Poland. In Biochimie, 2013
The sequence analysis enabled the mapping of previously not fully characterized structural domains in well-studied TAF proteins (including the full histone domains of TAF4 and 12 or TAF3 and 8).
The architecture of human general transcription factor TFIID core complex.
Berger et al., Grenoble, France. In Nature, 2013
A functional core-TFIID subcomplex was revealed in Drosophila nuclei, consisting of a subset of TAFs (TAF4, TAF5, TAF6, TAF9 and TAF12).
TAF4/4b x TAF12 displays a unique mode of DNA binding and is required for core promoter function of a subset of genes.
Dikstein et al., Israel. In J Biol Chem, 2009
Findings suggest that DNA binding by TAF4/4b-TAF12 facilitates the association of TFIID with the core promoter of a subset of genes.
Structural changes in TAF4b-TFIID correlate with promoter selectivity.
Tjian et al., Berkeley, United States. In Mol Cell, 2008
TAF4b incorporation into TFIID induces an open conformation at the lobe involved in TFIIA & putative activator interactions, correlating with differential activator-dependent transcription & promoter recognition by 4b/4-IID.
Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration.
Krainc et al., United States. In Cell, 2006
Mutant huntingtin represses PGC-1alpha gene transcription by associating with the promoter and interfering with the CREB/TAF4-dependent transcriptional pathway critical for the regulation of PGC-1alpha gene expression.
TAF4 nucleates a core subcomplex of TFIID and mediates activated transcription from a TATA-less promoter.
Tjian et al., Berkeley, United States. In Proc Natl Acad Sci U S A, 2006
Daat suggest that holo-TFIID comprises a stable core subcomplex containing TAF4, TAF5, TAF6, TAF9, and TAF12 decorated with peripheral subunits TAF1, TAF2, TAF11, and TBP.
New insights into TAFs as regulators of cell cycle and signaling pathways.
Mengus et al., France. In Cell Cycle, 2005
Moreover, the TAF4 subunit of TFIID negatively regulates proliferation by inhibiting activation of the TGFbeta signalling pathway by its paralogue TAF4b.
What turns CREB on?
Moens et al., Tromsø, Norway. In Cell Signal, 2004
The glutamine-rich Q2 domain, which interacts with the general transcription factor TAFII130/135, is sufficient for the recruitment of a functional RNA polymerase II complex and allows basal transcriptional activity.
E protein silencing by the leukemogenic AML1-ETO fusion protein.
Roeder et al., New York City, United States. In Science, 2004
These interactions are mediated by a conserved ETO TAF4 homology domain and a 17-amino acid p300/CBP and ETO target motif within AD1 activation domains of E proteins.
A role of the TATA box and the general co-activator hTAF(II)130/135 in promoter-specific trans-activation by simian virus 40 small t antigen.
Moens et al., Tromsø, Norway. In J Gen Virol, 2003
trans-activation of promoters by simian virus 40 small t-antigen may depend on a consensus TATA motif and such promoters recruit the general transcription factor hTAF(II)130/135
Crystal structure of a subcomplex of human transcription factor TFIID formed by TATA binding protein-associated factors hTAF4 (hTAF(II)135) and hTAF12 (hTAF(II)20).
Moras et al., Strasbourg, France. In J Biol Chem, 2002
Data present the crystal structure of a complex formed by the interacting domains from two subunits of the general transcription factor TFIID, the human TATA binding protein-associated factors hTAF4 (hTAF(II)135) and hTAF12 (hTAF(II)20).
Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease.
Krainc et al., United States. In Science, 2002
huntingtin interacts with Sp1 and TAFII130; transcriptional activity of SP1 and TAFII130 disrupted in early Huntingtin's Disease
Expanded polyglutamine stretches interact with TAFII130, interfering with CREB-dependent transcription.
Tsuji et al., Niigata, Japan. In Nat Genet, 2000
We found that expanded polyQ stretches preferentially bind to TAFII130, a coactivator involved in cAMP-responsive element binding protein (CREB)-dependent transcriptional activation, and strongly suppress CREB-dependent transcriptional activation.
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