Disease relevance of TEAD1

• TEF-1 is a tissue-specific human transcription factor which binds to and activates transcription from the SV40 early promoter and the HPV-16 E6/E7 promoter and may be involved in regulation of muscle-specific and placenta-specific gene expression [1].
• Two of the proteins also recognize other enhancer motifs; protein GT-IIB alpha binds to the microE3 motif present in the immunoglobulin heavy chain enhancer; protein GT-IIC binds to an enhancer motif of the polyomavirus mutant PyEC9.1 adapted to growth in F9 embryonal carcinoma cells, but not to the corresponding wild-type sequence [2].
• Involvement of a protein distinct from transcription enhancer factor-1 (TEF-1) in mediating human chorionic somatomammotropin gene enhancer function through the GT-IIC enhanson in choriocarcinoma and COS cells [3].
• Here we demonstrate that hTEF-1 overexpression inhibits minimal hCS promoters containing TATA and/or initiator elements, Rous sarcoma virus and thymidine kinase promoters in BeWo cells [4].
• Interaction between T antigen and TEA domain of the factor TEF-1 derepresses simian virus 40 late promoter in vitro: identification of T-antigen domains important for transcription control [5].

High impact information on TEAD1

• The hPL enhancer is bound by multiple proteins including at least one placental specific protein that interacts with a TEF-1 motif [6].
• The sequence of a cDNA clone of the gene reveals a predicted protein sequence homologous to that of a human transcriptional enhancer factor, TEF-1 (68% identity) [7].
• Deletion analysis of a chimera between TEF-1 and the GAL4 DNA binding domain (DBD) indicated that at least three regions of TEF-1 were involved in transactivation [8].
• Moreover, none of the GAL4 chimeras containing individual TEF-1 regions interfered with the activity of endogenous HeLa cell TEF-1, while interference was observed with the GAL4-TEF-1 chimeras which functioned as transactivators [8].
• The factor(s) associated with one of these populations is also required for the activity of GAL-ER (EF) and GAL-VP16, while the factor(s) associated with the other population functions selectively with GAL-TEF-1 [9].

Biological context of TEAD1

• Sequencing exons of the only gene in this interval, the transcriptional enhancer TEAD1, revealed a novel missense mutation (Y421H) carried by all patients and none of the 502 controls [10].
• The mutation is in a conserved amino acid sequence in the C terminal of the protein, a potential binding site for YAP65 one of TEAD1's cofactors that is expressed in human retina as well as TEAD1 based on RT-PCR experiments [10].
• Using nested, degenerate PCR primers corresponding to conserved TEF domains, several novel TEF-1-related cDNAs have been cloned from a human placental cDNA library [11].
• In the transient transcription assay, overexpression of either Max or TEF-1 resulted a mild activation of the alpha-MHC-chloramphenicol acetyltransferase (CAT) reporter gene at lower concentrations and repression of this gene at higher concentrations [12].
• However, when Max and TEF-1 expression plasmids were transfected together, the repression mediated by a single expression plasmid was alleviated and a three- to fourfold transactivation of the alpha-MHC-CAT reporter gene was observed [12].

Anatomical context of TEAD1

• Mammalian vestigial-like 2, a cofactor of TEF-1 and MEF2 transcription factors that promotes skeletal muscle differentiation [13].
• Members of the highly related TEF-1 (transcriptional enhancer factor-1) family (also known as TEAD, for TEF-1, TEC1, ABAA domain) bind to MCAT (muscle C, A and T sites) and A/T-rich sites in promoters active in cardiac, skeletal and smooth muscle, placenta, and neural crest [14].
• This promoter is also highly active in vitro in lymphoid cell extracts, but not in vivo in lymphoid cell lines, which do not express the endogenous TEF-1 gene [1].
• One class are homologues of the human TEF-1 originally cloned from HeLa cells (Xiao, J. H., Davidson, I., Matthes, H., Garnier, J. M., and Chambon, P. (1991) Cell 65, 551-568) [15].
• Our results demonstrate a novel association between SRF and TEF-1 for cardiac muscle gene regulation and disclose a general mechanism by which these two super families of factors are likely to control diversified biological functions [16].

Associations of TEAD1 with chemical compounds

• In the present study, we show by GST (glutathione S-transferase) pull-down assays, by co-immunoprecipitation and by modified mammalian two-hybrid assays that TEF-1 interacts with TAZ in vitro and in vivo [14].
• TEF-1.DNA complexes formed by BeWo nuclear extracts are supershifted by phosphoserine- and phosphothreonine- but not phosphotyrosine-specific antibodies, indicating that TEF-1 is phosphorylated in vivo at serine and threonine residues [17].
• We show here that the NH2-terminal region of TAg binds to the TEA domain of TEF-1, a DNA binding domain also found in the Drosophila scalloped and the Saccharomyces cerevisiae TEC1 proteins [5].
• This suggests that TEF-1-induced repression is due to interference/squelching of a limiting transcriptional intermediary factor that is essential for involucrin expression.(ABSTRACT TRUNCATED AT 250 WORDS)[18]

Physical interactions of TEAD1

• The transcriptional co-activator TAZ interacts differentially with transcriptional enhancer factor-1 (TEF-1) family members [14].
• By using different biochemical assays such as affinity precipitation of protein, GST-pulldown assay, and coimmunoprecipitation of proteins, we show that SRF binds to TEF-1 both in in vitro and in vivo assay conditions [16].
• To demonstrate that TEF-1 factors could also interact with MEF2 through its MADS domain, we used co-immunoprecipitation and GST pull-down assays in vitro and a mammalian two-hybrid assay in vivo [19].
• A TEF-1 binding motif that interacts with a placental protein is important for the transcriptional activity of the hCS-B enhancer [20].

Regulatory relationships of TEAD1

• Our results suggest that by their interaction with MEF2 factors, TEF-1 factors can control MEF2-dependent muscle-specific gene expression [19].

Other interactions of TEAD1

• Like Vgl-1, Vgl-2 interacts with TEF-1 [13].
• This differential interaction also extended to the interaction of TEF-1 and RTEF-1 with TAZ in vivo, as assayed by a modified mammalian two-hybrid experiment [14].
• Like YAP65, TAZ interacted with all four TEF-1 family members [14].
• Acting in opposing fashions, TEF-1 transrepressed the S100B promoter and RTEF-1 transactivated the promoter [21].
• Here we report that SRF binds to another myogenic factor, TEF-1, that has been implicated in the regulation of a variety of cardiac muscle genes [16].

Analytical, diagnostic and therapeutic context of TEAD1

• Using mobility gel shift competition assay, immunoblotting, and UV-cross-linking analyses, we found that a protein binding to the EM element is indistinguishable from the transcription enhancer factor-1 (TEF-1) in terms of sequence recognition, molecular mass, and immunoreactivity [22].
• Interactions between placental nuclear factors and sequences distinct from the TEF-1 element (nucleotides 117-139) were identified by gel mobility shift assay using the up-stream region corresponding to nucleotides 1-80 [23].
• Probing Northern blots of total RNA from first trimester and term placenta, the choriocarcinoma-derived cell line JAr and primary cultured cytotrophoblast cells with a cDNA for TEF-1 revealed transcripts of 12-13 kb and 3-4 kb [24].
• The purified TEF1 migrates on the SDS-PAGE at a molecular mass of about 36 kDa [25].
• Forty-six strains were isolated and identified at the species level by analysis of morphological characters, by sequence analysis of their internal transcribed spacer regions 1 and 2 (ITS 1 and 2) of the rDNA cluster and--in some cases--a fragment of the translation elongation factor 1alpha (tef1) gene, and RAPD-analysis [26].

References