Biology:E2F1

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Short description: Protein-coding gene in the species Homo sapiens

Transcription factor E2F1 is a protein that in humans is encoded by the E2F1 gene.[1]

Function

The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionarily conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. This protein binds preferentially to retinoblastoma protein pRB in a cell-cycle dependent manner. It can mediate both cell proliferation and p53-dependent/independent apoptosis.[2]

Transcription

E2F1 promoter[PAX8] => E2F1[3]

Interactions

E2F1 has been shown to interact with:


See also

References

  1. ↑ "Structure and partial genomic sequence of the human E2F1 gene". Gene 173 (2): 163–9. December 1996. doi:10.1016/0378-1119(96)00184-9. PMID 8964493. 
  2. ↑ "Entrez Gene: E2F1 E2F transcription factor 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1869. 
  3. ↑ "PAX8 promotes tumor cell growth by transcriptionally regulating E2F1 and stabilizing RB protein". Oncogene 30 (48): 4824–34. December 2011. doi:10.1038/onc.2011.190. PMID 21602887. 
  4. ↑ 4.0 4.1 "A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer". Oncogene 17 (7): 853–65. August 1998. doi:10.1038/sj.onc.1202163. PMID 9780002. 
  5. ↑ 5.0 5.1 "Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation". Nat. Cell Biol. 1 (1): 14–9. May 1999. doi:10.1038/8984. PMID 10559858. 
  6. ↑ "Functions of cyclin A1 in the cell cycle and its interactions with transcription factor E2F-1 and the Rb family of proteins". Mol. Cell. Biol. 19 (3): 2400–7. March 1999. doi:10.1128/mcb.19.3.2400. PMID 10022926. 
  7. ↑ "Cyclin A/CDK2 binds directly to E2F-1 and inhibits the DNA-binding activity of E2F-1/DP-1 by phosphorylation". Mol. Cell. Biol. 14 (12): 8420–31. December 1994. doi:10.1128/MCB.14.12.8420. PMID 7969176. 
  8. ↑ "Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase". EMBO J. 18 (15): 4280–91. August 1999. doi:10.1093/emboj/18.15.4280. PMID 10428966. 
  9. ↑ "The E2F-1 transcription factor is negatively regulated by its interaction with the MDMX protein". J. Cell. Biochem. 88 (3): 557–68. February 2003. doi:10.1002/jcb.10318. PMID 12532331. https://zenodo.org/record/1229214. 
  10. ↑ "Interaction and functional cooperation of the cancer-amplified transcriptional coactivator activating signal cointegrator-2 and E2F-1 in cell proliferation". Mol. Cancer Res. 1 (13): 948–58. November 2003. PMID 14638867. 
  11. ↑ 11.0 11.1 "Necdin, a postmitotic neuron-specific growth suppressor, interacts with viral transforming proteins and cellular transcription factor E2F1". J. Biol. Chem. 273 (2): 720–8. January 1998. doi:10.1074/jbc.273.2.720. PMID 9422723. 
  12. ↑ "Necdin-related MAGE proteins differentially interact with the E2F1 transcription factor and the p75 neurotrophin receptor". J. Biol. Chem. 279 (3): 1703–12. January 2004. doi:10.1074/jbc.M308454200. PMID 14593116. 
  13. ↑ "NPDC-1, a regulator of neural cell proliferation and differentiation, interacts with E2F-1, reduces its binding to DNA and modulates its transcriptional activity". Oncogene 19 (43): 5000–9. October 2000. doi:10.1038/sj.onc.1203843. PMID 11042687. 
  14. ↑ "Association of Pur alpha and E2F-1 suppresses transcriptional activity of E2F-1". Oncogene 18 (46): 6398–402. November 1999. doi:10.1038/sj.onc.1203011. PMID 10597240. 
  15. ↑ "A putative coiled-coil domain of prohibitin is sufficient to repress E2F1-mediated transcription and induce apoptosis". Biochem. Biophys. Res. Commun. 312 (2): 459–66. December 2003. doi:10.1016/j.bbrc.2003.10.148. PMID 14637159. 
  16. ↑ "Prohibitin induces the transcriptional activity of p53 and is exported from the nucleus upon apoptotic signaling". J. Biol. Chem. 278 (48): 47853–61. November 2003. doi:10.1074/jbc.M305171200. PMID 14500729. 
  17. ↑ "Prohibitin requires Brg-1 and Brm for the repression of E2F and cell growth". EMBO J. 21 (12): 3019–28. June 2002. doi:10.1093/emboj/cdf302. PMID 12065415. 
  18. ↑ "Rb and prohibitin target distinct regions of E2F1 for repression and respond to different upstream signals". Mol. Cell. Biol. 19 (11): 7447–60. November 1999. doi:10.1128/mcb.19.11.7447. PMID 10523633. 
  19. ↑ 19.0 19.1 "Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1". J. Virol. 67 (12): 7641–7. December 1993. doi:10.1128/JVI.67.12.7641-7647.1993. PMID 8230483. 
  20. ↑ "The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein". Nucleic Acids Res. 29 (15): 3131–6. August 2001. doi:10.1093/nar/29.15.3131. PMID 11470869. 
  21. ↑ "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation". J. Biol. Chem. 277 (52): 50860–6. December 2002. doi:10.1074/jbc.M203839200. PMID 12397079. 
  22. ↑ 22.0 22.1 "Inhibition of E2F-mediated transcription by p202". EMBO J. 15 (20): 5668–78. October 1996. doi:10.1002/j.1460-2075.1996.tb00951.x. PMID 8896460. 
  23. ↑ "pRB binds to and modulates the transrepressing activity of the E1A-regulated transcription factor p120E4F". Proc. Natl. Acad. Sci. U.S.A. 97 (14): 7738–43. July 2000. doi:10.1073/pnas.130198397. PMID 10869426. Bibcode: 2000PNAS...97.7738F. 
  24. ↑ 24.0 24.1 "In vivo association of E2F and DP family proteins". Mol. Cell. Biol. 15 (5): 2536–46. May 1995. doi:10.1128/mcb.15.5.2536. PMID 7739537. 
  25. ↑ 25.0 25.1 25.2 25.3 "Transcription factors of the Sp1 family: interaction with E2F and regulation of the murine thymidine kinase promoter". J. Mol. Biol. 293 (5): 1005–15. November 1999. doi:10.1006/jmbi.1999.3213. PMID 10547281. 
  26. ↑ "Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction". Mol. Cell. Biol. 16 (4): 1668–75. April 1996. doi:10.1128/MCB.16.4.1668. PMID 8657142. 
  27. ↑ "Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F". Mol. Cell. Biol. 16 (4): 1659–67. April 1996. doi:10.1128/mcb.16.4.1659. PMID 8657141. 
  28. ↑ "E2F-4 and E2F-5, two members of the E2F family, are expressed in the early phases of the cell cycle". Proc. Natl. Acad. Sci. U.S.A. 92 (6): 2403–7. March 1995. doi:10.1073/pnas.92.6.2403. PMID 7892279. Bibcode: 1995PNAS...92.2403S. 
  29. ↑ "Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative trans-activation". Genes Dev. 7 (10): 1850–61. October 1993. doi:10.1101/gad.7.10.1850. PMID 8405995. 
  30. ↑ "Regulation of E2F1 by BRCT domain-containing protein TopBP1". Mol. Cell. Biol. 23 (9): 3287–304. May 2003. doi:10.1128/mcb.23.9.3287-3304.2003. PMID 12697828. 
  31. ↑ "The BRCT domain is a phospho-protein binding domain". Science 302 (5645): 639–42. October 2003. doi:10.1126/science.1088753. PMID 14576433. Bibcode: 2003Sci...302..639Y. 
  32. ↑ "The association of GSK3 beta with E2F1 facilitates nerve growth factor-induced neural cell differentiation". J. Biol. Chem. 283 (21): 14506–15. May 2008. doi:10.1074/jbc.M706136200. PMID 18367454. 

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.



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