Disease relevance of Tead1

• TEF-1 transcription factors regulate activity of the mouse mammary tumor virus LTR [1].
• Gel mobility shift assays revealed strong TEF-1 factor binding to one site using nuclear extracts from CV-1 cells and from the human breast cancer cell line MCF-7 [1].
• Here we describe that VITO-1, a new SID (scalloped interaction domain)-containing protein, binds to TEF1 in vitro and strongly stimulates transcription of a MCAT reporter plasmid together with TEF-1 [2].
• We demonstrated that TEF-1 represses hCS promoter activity in choriocarcinoma (BeWo) cells (Jiang, S.W., and Eberhardt, N.L. (1995) J. Biol. Chem. 270, 13609-13915), suggesting that TEF-1 interacts with basal transcription factors [3].
• A TEF-1-element is required for activation of the promoter of pseudorabies virus glycoprotein X gene by IE180 [4].

High impact information on Tead1

• Cloning, expression, and transcriptional properties of the human enhancer factor TEF-1 [5].
• Mammals express four highly conserved TEAD/TEF transcription factors that bind the same DNA sequence, but serve different functions during development [6].
• Therefore, the carboxy-terminal acidic activation domain in YAP is the transcriptional activation domain for TEAD transcription factors [6].
• These cells expressed Nkx2.5/Csx, GATA4, TEF-1, and MEF-2C mRNA before 5-azacytidine treatment and expressed MEF-2A and MEF-2D after treatment [7].
• This 'embryo responsive' (ER) enhancer configuration was characterized by a tandem duplication of the region containing a single point mutation that created a DNA binding site for Transcription Enhancer Factor-1 (TEF-1) [8].

Biological context of Tead1

• In transient transfection assays, TEF-1 squelched the basal LTR activity and completely abrogated the response to the glucocorticoid dexamethasone [1].
• Amino acid sequences deduced for ETFR-1 and -2 as well as those of other known proteins of the same family, TEF-1 and ETF, exhibited significant identity (63-75% overall) to each other not only in the TEA DNA binding domain but also in the C-terminal regions [9].
• alpha(1)-Adrenergic signaling in cardiac myocytes activates the skeletal muscle alpha-actin gene through an MCAT cis-element, the binding site of the transcriptional enhancer factor-1 (TEF-1) family of transcription factors [10].
• TEF1 itself is unable to activate reporter plasmids bearing TEF1-binding sites, suggesting that additional bridging or co-activating factors are necessary to allow interaction of TEF1 with the transcriptional machinery [2].
• Both this interaction and sequence-specific DNA binding by TEAD were required for transcriptional activation in mouse cells [6].

Anatomical context of Tead1

• TEF-1 accounts for more than 85% of the MCAT binding activity in neonatal rat cardiac myocytes [10].
• In addition, the Tead transcription factor is required specifically for enhancer activation in neural-crest-derived smooth muscle cells and dorsal aorta [11].
• We show that Tead2, a member of the Tead box family of transcription factors, binds to a neural crest enhancer and activates Pax3 expression [12].
• Inhibition of Tead activity by repressor-modified Tead compromised NE enhancer activation and notochord development in transgenic mouse embryos [13].
• Identification of a murine TEF-1-related gene expressed after mitogenic stimulation of quiescent fibroblasts and during myogenic differentiation [14].

Associations of Tead1 with chemical compounds

• These TEF-1 factors also interfered with the response to dexamethasone [1].
• Site-directed mutagenesis was used to inactivate eight serine residues of RTEF-1, not present in TEF-1, that are putative targets of alpha(1)-adrenergic-dependent kinases [15].
• Chelation of nuclear but not cytosolic Ca(2+) increased TEAD activity two times above control [16].
• Although the Sph element is similar in sequence to the SV40 element, the PLF Sph-binding factor is distinct from TEF-1, the factor that binds to the SV40 Sph motif [17].
• Our findings demonstrate, for the first time, that the cell transformation and tumorigenesis induced by cadmium are due, at least in part, to the overexpression of TEF-1 delta, a novel cadmium-responsive proto-oncogene [18].
• These effects could be reversed in vivo by mechanical overload, which decreased muscle creatine kinase-driven TEAD-1 transgene expression, and in cultured satellite cells by TEAD-1-specific small interfering RNA [19].

Physical interactions of Tead1

• Both a ubiquitous factor mTEF-1 and a distinct muscle-specific factor bind to the M-CAT motif of the myosin heavy chain beta gene [20].
• Here, gel mobility shift assays show that Vgl-2 differentially affects DNA binding of different TEF-1 factors [21].

Regulatory relationships of Tead1

• These results suggest that Tead activates the Foxa2 enhancer core element in the mouse node in cooperation with a second factor that binds to the 5' element, and that a similar mechanism also operates in the zebrafish shield [13].
• However, the mechanism whereby Vgl-2 regulates TEF-1 factors and the requirement for Vgl-2 for muscle-specific gene expression were not known [21].
• Functional analysis of this region reveals that the CCAAT box-binding protein nuclear factor Y (NF-Y) can substitute for TEF-1 in activating VSM alpha-actin transcription but that the TEF-1-binding site is essential for the maintenance of full transcriptional repression [22].

Other interactions of Tead1

• Embryonic TEA domain-containing factor (ETF) belongs to the family of proteins structurally related to transcriptional enhancer factor-1 (TEF-1) and is implicated in neural development [23].
• In contrast, alpha(1)-adrenergic stimulation did not alter, and phosphatase treatment increased, MCAT binding of TEF-1 and RTEF-1 [10].
• Teads and their co-factor YAP65 activated the CE in P19 cells, and binding of Tead to CE was essential for enhancer activity [13].
• These results suggest that the M-CAT binding factors consist of two different factors; the ubiquitous A2 is encoded by mTEF-1, but the muscle-specific A1 factor is distinct from mTEF-1 [20].
• The objective was to determine if the newly discovered TEF1, MSY1, Puralpha and Purbeta VSM alpha-actin transcriptional reprogramming proteins (TRPs) were associated with development of chronic rejection histopathology in accepted murine cardiac allografts [24].

Analytical, diagnostic and therapeutic context of Tead1

• We describe the molecular cloning of two novel human and murine transcription factors containing the TEA/ATTS DNA binding domain and related to transcriptional enhancer factor-1 (TEF-1) [25].
• Vgl-4 functionally interacts with TEF-1 and also with myocyte enhancer factor 2 in a mammalian two-hybrid assay [26].
• 3. In contrast, PCR screening of human/rodent cell hybrid panels identified TEF-1 on chromosome 11p15.2, between D11S1315 and D11S1334, extending a region of known synteny between human chromosomes 11 and 12 and arguing for an ancient divergence between these two closely related genes [27].

References