TEAD1

TEAD1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases TEAD1, AA, NTEF-1, REF1, TCF-13, TCF13, TEAD-1, TEF-1, TEA domain transcription factor 1
External IDs MGI: 101876 HomoloGene: 2418 GeneCards: TEAD1
Orthologs
Species Human Mouse
Entrez

7003

21676

Ensembl

ENSG00000187079

ENSMUSG00000055320

UniProt

P28347

P30051

RefSeq (mRNA)

NM_021961

NM_001166584
NM_001166585
NM_009346
NM_175559

RefSeq (protein)

NP_068780.2

NP_033372.1

Location (UCSC) Chr 11: 12.67 – 12.94 Mb Chr 7: 112.68 – 112.91 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Transcriptional enhancer factor TEF-1 also known as TEA domain family member 1 (TEAD1) and transcription factor 13 (TCF-13) is a protein that in humans is encoded by the TEAD1 gene.[3][4][5][6] TEAD1 was the first member of the TEAD family of transcription factors to be identified.[3][7]

Structure

All members of the TEAD family share a highly conserved DNA binding domain called the TEA domain.[8] This DNA binding domain has a consensus DNA sequence 5’-CATTCCA/T-3’ that is called the MCAT element.[9] The three dimensional structure of the TEA domain has been identified [5]. Its conformation is close to that of the homeodomain and contains 3 α helixes (H1, H2 and H3). It is the H3 helix that enables TEAD proteins to bind DNA.[10]

Another conserved domain of TEAD1 is located at the C terminus of the protein. It allows the binding of cofactors and has been called the YAP1 binding domain, because it is its ability to bind this well-known TEAD proteins co-factor that led to its identification. Indeed, TEAD proteins cannot induce gene expression on their own. They have to associate with cofactors to be able to act[11]

Tissue distribution

TEAD1 is expressed in various tissues including skeletal muscle, pancreas, placenta, lung, and heart.[12][13][14][15][16][17][18]

Orthologs

TEAD proteins are found in many organisms under different names, assuming different functions. For example in Saccharomyces cerevisiae TEC-1 regulates the transposable element TY1 and is involved in pseudohyphale growth (the elongated shape that yeasts take when grown in nutrient-poor conditions).[19] In Aspergillus nidulans, the TEA domain protein ABAA regulates the differentiation of conidiophores.[20] In drosophila the transcription factor Scalloped is involved in the development of the wing disc, survival and cell growth.[21] Finally in Xenopus it has been demonstrated that the ortholog of TEAD1 regulates muscle differentiation.[22]

Function

Post-transcriptional modifications

Protein Kinase A (pKA) can phosphorylate TEAD1 at serine 102, after the TEA domain. This phosphorylation is needed for the transcriptional activation of the α MyHC gene.[34] Protein Kinase C (pKC) phosphorylates TEAD1 on serine and threonine next to the last alpha loop in the TEA domain. This phosphorylation decreases TEAD1 binding to the GTIIC enhancer.[35] TEAD1 can be palmitoylated on a conserved cysteine at the C-term of the protein. This post-translational modification is critical for proper folding of TEAD proteins and their stability.[36]

Cofactors

TEAD proteins require cofactors to induce the transcription of target genes.[12] TEAD1 interacts with all members of the SRC family of steroid receptor coactivators. In HeLa cells TEAD1 and SRC induce gene expression,[37] TEAD1 interacts with PARP (Poly-ADP ribose polymerase) to regulate smooth muscle α-actin expression. PARP can also ADP-ribosylate the TEAD proteins and make the chromatin context favorable to transcription through histone modification,[38] SRF (Serum response factor) and TEAD1 together regulate gene expression.[39]

TEAD proteins and MEF2 (myocyte enhancer factor 2) interact physically. The binding of MEF2 on DNA induces and potentiates TEAD1 recruitment at MCAT sequences that are adjacent to MEF2 binding sites. This recruitment leads to the repression of the MLC2v (Myosin Light Chain 2 v) and βMHC ( β-myosin heavy chain ) promoter.[40] TEAD1 and the phosphoprotein MAX interact in vivo and in vitro. Once this complex is formed, these two proteins can regulate the alpha-myosin heavy chain (α-MHC) gene expression.[41]

The four Vestigial-like (VGLL) proteins are able to interact with all TEADs.[42] The precise function of TEAD and VGLL interaction is still poorly understood. It has been shown that TEAD/VGLL1 complexes promote anchorage-independent cell proliferation in prostate cancer cell lines suggesting a role in cancer progression [43] Moreover VGLL2 interaction with TEAD1 activates muscle promoter upon C2C12 differentiation and enhances MyoD-mediated myogenic in 10T1/2.[44] Finally the complex TEAD/VGLL4 acts as a default transcriptional repressor.[45]

The interaction between YAP (Yes Associated Protein 65), TAZ, a transcriptional coactivator paralog to YAP, and all TEAD proteins was demonstrated both in vitro and in vivo. In both cases the interaction of the proteins leads to increased TEAD transcriptional activity.[45][46] YAP/TAZ are effectors of the Hippo tumor suppressor pathway that restricts organ growth by keeping in check cell proliferation and promoting apoptosis in mammals and also in Drosophila.[29][47]

Role in cancer

Analysis of cancer transcriptome databases (www.ebi.ac.uk/gxa) showed that TEAD1 is dysregulated in several types of cancers. First in Kaposi sarcoma there is a 300-fold increase in TEAD1 levels. Moreover the increase of TEAD expression can be detected in basal-like breast cancers,[48][49] fallopian tube carcinoma,[50] and germ cell tumors.[51] Otherwise, in other types of cancer TEAD expression is decreased, for example in other breast cancer types and in renal or bladder cancers. This dual role can be explained by the different targets and the differential regulation of target genes by TEAD transcription factors.[33][52] Finally recent studies showed that TEAD1 and YAP in ovarian cancer can induces cell stemness and chemoresistance.[53] and that genetic variant of TEAD protein and YAP are enriched in some cancers.[54]

References

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  2. "Mouse PubMed Reference:".
  3. 1 2 Xiao JH, Davidson I, Matthes H, Garnier JM, Chambon P (May 1991). "Cloning, expression, and transcriptional properties of the human enhancer factor TEF-1". Cell. 65 (4): 551–68. doi:10.1016/0092-8674(91)90088-G. PMID 1851669.
  4. Jacquemin P, Depetris D, Mattei MG, Martial JA, Davidson I (Jan 1999). "Localization of human transcription factor TEF-4 and TEF-5 (TEAD2, TEAD3) genes to chromosomes 19q13.3 and 6p21.2 using fluorescence in situ hybridization and radiation hybrid analysis". Genomics. 55 (1): 127–9. doi:10.1006/geno.1998.5628. PMID 9889009.
  5. Fossdal R, Jonasson F, Kristjansdottir GT, Kong A, Stefansson H, Gosh S, Gulcher JR, Stefansson K (May 2004). "A novel TEAD1 mutation is the causative allele in Sveinsson's chorioretinal atrophy (helicoid peripapillary chorioretinal degeneration)". Human Molecular Genetics. 13 (9): 975–81. doi:10.1093/hmg/ddh106. PMID 15016762.
  6. "Entrez Gene: TEAD1 TEA domain family member 1 (SV40 transcriptional enhancer factor)".
  7. 1 2 Mar JH, Ordahl CP (September 1988). "A conserved CATTCCT motif is required for skeletal muscle-specific activity of the cardiac troponin T gene promoter". Proceedings of the National Academy of Sciences of the United States of America. 85 (17): 6404–8. doi:10.1073/pnas.85.17.6404. PMC 281980Freely accessible. PMID 3413104.
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  10. Anbanandam A, Albarado DC, Nguyen CT, Halder G, Gao X, Veeraraghavan S (November 2006). "Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain". Proceedings of the National Academy of Sciences of the United States of America. 103 (46): 17225–30. doi:10.1073/pnas.0607171103. PMC 1859914Freely accessible. PMID 17085591.
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  22. Naye F, Tréguer K, Soulet F, Faucheux C, Fédou S, Thézé N, Thiébaud P (2007). "Differential expression of two TEF-1 (TEAD) genes during Xenopus laevis development and in response to inducing factors". The International Journal of Developmental Biology. 51 (8): 745–52. doi:10.1387/ijdb.072375fn. PMID 17939122.
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  29. 1 2 Yu FX, Zhao B, Guan KL (November 2015). "Hippo Pathway in Organ Size Control, Tissue Homeostasis, and Cancer". Cell. 163 (4): 811–28. doi:10.1016/j.cell.2015.10.044. PMID 26544935.
  30. Landin Malt A, Cagliero J, Legent K, Silber J, Zider A, Flagiello D (2012). "Alteration of TEAD1 expression levels confers apoptotic resistance through the transcriptional up-regulation of Livin". PloS One. 7 (9): e45498. doi:10.1371/journal.pone.0045498. PMC 3454436Freely accessible. PMID 23029054.
  31. Zhao B, Li L, Lei Q, Guan KL (May 2010). "The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version". Genes & Development. 24 (9): 862–74. doi:10.1101/gad.1909210. PMC 2861185Freely accessible. PMID 20439427.
  32. Landin Malt A, Cagliero J, Legent K, Silber J, Zider A, Flagiello D (2012). "Alteration of TEAD1 expression levels confers apoptotic resistance through the transcriptional up-regulation of Livin". PloS One. 7 (9): e45498. doi:10.1371/journal.pone.0045498. PMC 3454436Freely accessible. PMID 23029054.
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  45. 1 2 Koontz LM, Liu-Chittenden Y, Yin F, Zheng Y, Yu J, Huang B, Chen Q, Wu S, Pan D (May 2013). "The Hippo effector Yorkie controls normal tissue growth by antagonizing scalloped-mediated default repression". Developmental Cell. 25 (4): 388–401. doi:10.1016/j.devcel.2013.04.021. PMC 3705890Freely accessible. PMID 23725764.
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  47. Zhao B, Li L, Lei Q, Guan KL (May 2010). "The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version". Genes & Development. 24 (9): 862–74. doi:10.1101/gad.1909210. PMC 2861185Freely accessible. PMID 20439427.
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  50. Nowee ME, Snijders AM, Rockx DA, de Wit RM, Kosma VM, Hämäläinen K, Schouten JP, Verheijen RH, van Diest PJ, Albertson DG, Dorsman JC (September 2007). "DNA profiling of primary serous ovarian and fallopian tube carcinomas with array comparative genomic hybridization and multiplex ligation-dependent probe amplification". The Journal of Pathology. 213 (1): 46–55. doi:10.1002/path.2217. PMID 17668415.
  51. Skotheim RI, Autio R, Lind GE, Kraggerud SM, Andrews PW, Monni O, Kallioniemi O, Lothe RA (2006). "Novel genomic aberrations in testicular germ cell tumors by array-CGH, and associated gene expression changes". Cellular Oncology. 28 (5-6): 315–26. PMC 4615958Freely accessible. PMID 17167184.
  52. Landin Malt A, Cagliero J, Legent K, Silber J, Zider A, Flagiello D (2012). "Alteration of TEAD1 expression levels confers apoptotic resistance through the transcriptional up-regulation of Livin". PloS One. 7 (9): e45498. doi:10.1371/journal.pone.0045498. PMC 3454436Freely accessible. PMID 23029054.
  53. Xia Y, Zhang YL, Yu C, Chang T, Fan HY (2014). "YAP/TEAD co-activator regulated pluripotency and chemoresistance in ovarian cancer initiated cells". PloS One. 9 (11): e109575. doi:10.1371/journal.pone.0109575. PMC 4219672Freely accessible. PMID 25369529.
  54. Yuan H, Liu H, Liu Z, Zhu D, Amos CI, Fang S, Lee JE, Wei Q (August 2015). "Genetic variants in Hippo pathway genes YAP1, TEAD1 and TEAD4 are associated with melanoma-specific survival". International Journal of Cancer. 137 (3): 638–45. doi:10.1002/ijc.29429. PMID 25628125.

Further reading

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