E2F1

From Wikipedia, the free encyclopedia
Jump to: navigation, search
E2F transcription factor 1

PDB rendering based on 2aze.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols E2F1 ; E2F-1; RBAP1; RBBP3; RBP3
External IDs OMIM189971 MGI101941 HomoloGene3828 ChEMBL: 4382 GeneCards: E2F1 Gene
RNA expression pattern
PBB GE E2F1 2028 s at tn.png
PBB GE E2F1 204947 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1869 13555
Ensembl ENSG00000101412 ENSMUSG00000027490
UniProt Q01094 Q61501
RefSeq (mRNA) NM_005225 NM_007891
RefSeq (protein) NP_005216 NP_031917
Location (UCSC) Chr 20:
32.26 – 32.27 Mb
Chr 2:
154.56 – 154.57 Mb
PubMed search [1] [2]

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

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 evolutionally 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[edit]

E2F1 promoter[PAX8] => E2F1 [PMID 21602887]

Interactions[edit]

E2F1 has been shown to interact with NCOA6,[3] Retinoblastoma-like protein 1,[4] Retinoblastoma protein,[4][5][6][7][8][9][10] GTF2H1,[11] SKP2,[12] PURA,[13] NPDC1,[14] Sp2 transcription factor,[15] Sp1 transcription factor,[15][16][17] CUL1,[12] ARID3A,[18] TOPBP1,[19][20] Cyclin A1,[21] TP53BP1,[7] Cyclin A2,[22] Sp4 transcription factor,[15] Sp3 transcription factor,[15] Prohibitin,[23][24][25][26] NDN,[10][27] MDM4,[28] TFDP1[9][18][29][30] and Ubiquitin C.[31]

See also[edit]

References[edit]

  1. ^ Neuman E, Sellers WR, McNeil JA, Lawrence JB, Kaelin WG Jr (December 1996). "Structure and partial genomic sequence of the human E2F1 gene". Gene 173 (2): 163–9. doi:10.1016/0378-1119(96)00184-9. PMID 8964493. 
  2. ^ "Entrez Gene: E2F1 E2F transcription factor 1". 
  3. ^ Kong, Hee Jeong; Yu Hyun Jung, Hong SunHwa, Park Min Jung, Choi Young Hyun, An Won Gun, Lee Jae Woon, Cheong JaeHun (November 2003). "Interaction and functional cooperation of the cancer-amplified transcriptional coactivator activating signal cointegrator-2 and E2F-1 in cell proliferation". Mol. Cancer Res. (United States) 1 (13): 948–58. ISSN 1541-7786. PMID 14638867. 
  4. ^ a b Dyson, N; Dembski M, Fattaey A, Ngwu C, Ewen M, Helin K (December 1993). "Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1". J. Virol. (UNITED STATES) 67 (12): 7641–7. ISSN 0022-538X. PMC 238233. PMID 8230483. 
  5. ^ Nicolas, E; Ait-Si-Ali S, Trouche D (August 2001). "The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein". Nucleic Acids Res. (England) 29 (15): 3131–6. doi:10.1093/nar/29.15.3131. PMC 55834. PMID 11470869. 
  6. ^ Pardo, Patricia S; Leung James K, Lucchesi John C, Pereira-Smith Olivia M (December 2002). "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation". J. Biol. Chem. (United States) 277 (52): 50860–6. doi:10.1074/jbc.M203839200. ISSN 0021-9258. PMID 12397079. 
  7. ^ a b Choubey, D; Li S J, Datta B, Gutterman J U, Lengyel P (October 1996). "Inhibition of E2F-mediated transcription by p202". EMBO J. (ENGLAND) 15 (20): 5668–78. ISSN 0261-4189. PMC 452311. PMID 8896460. 
  8. ^ Fajas, L; Paul C, Zugasti O, Le Cam L, Polanowska J, Fabbrizio E, Medema R, Vignais M L, Sardet C (July 2000). "pRB binds to and modulates the transrepressing activity of the E1A-regulated transcription factor p120E4F". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (14): 7738–43. doi:10.1073/pnas.130198397. ISSN 0027-8424. PMC 16614. PMID 10869426. 
  9. ^ a b Wu, C L; Zukerberg L R, Ngwu C, Harlow E, Lees J A (May 1995). "In vivo association of E2F and DP family proteins". Mol. Cell. Biol. (UNITED STATES) 15 (5): 2536–46. ISSN 0270-7306. PMC 230484. PMID 7739537. 
  10. ^ a b Taniura, H; Taniguchi N, Hara M, Yoshikawa K (January 1998). "Necdin, a postmitotic neuron-specific growth suppressor, interacts with viral transforming proteins and cellular transcription factor E2F1". J. Biol. Chem. (UNITED STATES) 273 (2): 720–8. doi:10.1074/jbc.273.2.720. ISSN 0021-9258. PMID 9422723. 
  11. ^ Vandel, L; Kouzarides T (August 1999). "Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase". EMBO J. (ENGLAND) 18 (15): 4280–91. doi:10.1093/emboj/18.15.4280. ISSN 0261-4189. PMC 1171504. PMID 10428966. 
  12. ^ a b Marti, A; Wirbelauer C, Scheffner M, Krek W (May 1999). "Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation". Nat. Cell Biol. (ENGLAND) 1 (1): 14–9. doi:10.1038/8984. ISSN 1465-7392. PMID 10559858. 
  13. ^ Darbinian, N; Gallia G L, Kundu M, Shcherbik N, Tretiakova A, Giordano A, Khalili K (November 1999). "Association of Pur alpha and E2F-1 suppresses transcriptional activity of E2F-1". Oncogene (ENGLAND) 18 (46): 6398–402. doi:10.1038/sj.onc.1203011. ISSN 0950-9232. PMID 10597240. 
  14. ^ Sansal, I; Dupont E, Toru D, Evrard C, Rouget P (October 2000). "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 (ENGLAND) 19 (43): 5000–9. doi:10.1038/sj.onc.1203843. ISSN 0950-9232. PMID 11042687. 
  15. ^ a b c d Rotheneder, H; Geymayer S, Haidweger E (November 1999). "Transcription factors of the Sp1 family: interaction with E2F and regulation of the murine thymidine kinase promoter". J. Mol. Biol. (ENGLAND) 293 (5): 1005–15. doi:10.1006/jmbi.1999.3213. ISSN 0022-2836. PMID 10547281. 
  16. ^ Lin, S Y; Black A R, Kostic D, Pajovic S, Hoover C N, Azizkhan J C (April 1996). "Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction". Mol. Cell. Biol. (UNITED STATES) 16 (4): 1668–75. ISSN 0270-7306. PMC 231153. PMID 8657142. 
  17. ^ Karlseder, J; Rotheneder H, Wintersberger E (April 1996). "Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F". Mol. Cell. Biol. (UNITED STATES) 16 (4): 1659–67. ISSN 0270-7306. PMC 231152. PMID 8657141. 
  18. ^ a b Suzuki, M; Okuyama S, Okamoto S, Shirasuna K, Nakajima T, Hachiya T, Nojima H, Sekiya S, Oda K (August 1998). "A novel E2F binding protein with Myc-type HLH motif stimulates E2F-dependent transcription by forming a heterodimer". Oncogene (ENGLAND) 17 (7): 853–65. doi:10.1038/sj.onc.1202163. ISSN 0950-9232. PMID 9780002. 
  19. ^ Liu, Kang; Lin Fang-Tsyr, Ruppert J Michael, Lin Weei-Chin (May 2003). "Regulation of E2F1 by BRCT domain-containing protein TopBP1". Mol. Cell. Biol. (United States) 23 (9): 3287–304. doi:10.1128/MCB.23.9.3287-3304.2003. ISSN 0270-7306. PMC 153207. PMID 12697828. 
  20. ^ Yu, Xiaochun; Chini Claudia Christiano Silva, He Miao, Mer Georges, Chen Junjie (October 2003). "The BRCT domain is a phospho-protein binding domain". Science (United States) 302 (5645): 639–42. doi:10.1126/science.1088753. PMID 14576433. 
  21. ^ Yang, R; Müller C, Huynh V, Fung Y K, Yee A S, Koeffler H P (March 1999). "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. (UNITED STATES) 19 (3): 2400–7. ISSN 0270-7306. PMC 84032. PMID 10022926. 
  22. ^ Xu, M; Sheppard K A, Peng C Y, Yee A S, Piwnica-Worms H (December 1994). "Cyclin A/CDK2 binds directly to E2F-1 and inhibits the DNA-binding activity of E2F-1/DP-1 by phosphorylation". Mol. Cell. Biol. (UNITED STATES) 14 (12): 8420–31. ISSN 0270-7306. PMC 359381. PMID 7969176. 
  23. ^ Joshi, Bharat; Ko Danette, Ordonez-Ercan Dalia, Chellappan Srikumar P (December 2003). "A putative coiled-coil domain of prohibitin is sufficient to repress E2F1-mediated transcription and induce apoptosis". Biochem. Biophys. Res. Commun. (United States) 312 (2): 459–66. doi:10.1016/j.bbrc.2003.10.148. ISSN 0006-291X. PMID 14637159. 
  24. ^ Fusaro, Gina; Dasgupta Piyali, Rastogi Shipra, Joshi Bharat, Chellappan Srikumar (November 2003). "Prohibitin induces the transcriptional activity of p53 and is exported from the nucleus upon apoptotic signaling". J. Biol. Chem. (United States) 278 (48): 47853–61. doi:10.1074/jbc.M305171200. ISSN 0021-9258. PMID 14500729. 
  25. ^ Wang, Sheng; Zhang Baohua, Faller Douglas V (June 2002). "Prohibitin requires Brg-1 and Brm for the repression of E2F and cell growth". EMBO J. (England) 21 (12): 3019–28. doi:10.1093/emboj/cdf302. ISSN 0261-4189. PMC 126057. PMID 12065415. 
  26. ^ Wang, S; Nath N, Fusaro G, Chellappan S (November 1999). "Rb and prohibitin target distinct regions of E2F1 for repression and respond to different upstream signals". Mol. Cell. Biol. (UNITED STATES) 19 (11): 7447–60. ISSN 0270-7306. PMC 84738. PMID 10523633. 
  27. ^ Kuwako, Ken-ichiro; Taniura Hideo, Yoshikawa Kazuaki (January 2004). "Necdin-related MAGE proteins differentially interact with the E2F1 transcription factor and the p75 neurotrophin receptor". J. Biol. Chem. (United States) 279 (3): 1703–12. doi:10.1074/jbc.M308454200. ISSN 0021-9258. PMID 14593116. 
  28. ^ Strachan, Gordon D; Jordan-Sciutto Kelly L, Rallapalli Ravikumar, Tuan Rocky S, Hall David J (February 2003). "The E2F-1 transcription factor is negatively regulated by its interaction with the MDMX protein". J. Cell. Biochem. (United States) 88 (3): 557–68. doi:10.1002/jcb.10318. ISSN 0730-2312. PMID 12532331. 
  29. ^ Sardet, C; Vidal M, Cobrinik D, Geng Y, Onufryk C, Chen A, Weinberg R A (March 1995). "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. (UNITED STATES) 92 (6): 2403–7. doi:10.1073/pnas.92.6.2403. ISSN 0027-8424. PMC 42492. PMID 7892279. 
  30. ^ Helin, K; Wu C L, Fattaey A R, Lees J A, Dynlacht B D, Ngwu C, Harlow E (October 1993). "Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative trans-activation". Genes Dev. (UNITED STATES) 7 (10): 1850–61. doi:10.1101/gad.7.10.1850. ISSN 0890-9369. PMID 8405995. 
  31. ^ Zhou, Fangfang; Zhang Long, Wang Aijun, Song Bo, Gong Kai, Zhang Lihai, Hu Min, Zhang Xiufang, Zhao Nanming, Gong Yandao (May 2008). "The association of GSK3 beta with E2F1 facilitates nerve growth factor-induced neural cell differentiation". J. Biol. Chem. (United States) 283 (21): 14506–15. doi:10.1074/jbc.M706136200. ISSN 0021-9258. PMID 18367454. 

PI3K signaling maintains c-myc expression to regulate transcription of E2F1 in pancreatic cancer cells.

Further reading[edit]

  • Dupont E, Sansal I, Toru D, et al. (1997). "[Identification of NPDC-1, gene involved in the control of proliferation and differentiation of neural and glial precursors]". C. R. Seances Soc. Biol. Fil. 191 (1): 95–104. PMID 9181131. 
  • Stevens C, La Thangue NB (2005). "The emerging role of E2F-1 in the DNA damage response and checkpoint control.". DNA Repair (Amst.) 3 (8-9): 1071–9. doi:10.1016/j.dnarep.2004.03.034. PMID 15279795. 
  • Zhang Z, Wang H, Li M, et al. (2006). "Novel MDM2 p53-independent functions identified through RNA silencing technologies.". Ann. N. Y. Acad. Sci. 1058 (1): 205–14. doi:10.1196/annals.1359.030. PMID 16394138. 
  • Schild C, Wirth M, Reichert M, Schmid RM, Saur D, Schneider G (July 2009). "PI3K signaling maintains c-myc expression to regulate transcription of E2F1 in pancreatic cancer cells". Mol. Carcinog. 48 (12): 1149–58. doi:10.1002/mc.20569. PMID 19603422. 

External links[edit]

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