From Wikipedia, the free encyclopedia
(Redirected from E2F1 (gene))
E2F1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases E2F1, E2F-1, RBAP1, RBBP3, RBP3, E2F transcription factor 1
External IDs OMIM: 189971; MGI: 101941; HomoloGene: 3828; GeneCards: E2F1; OMA: E2F1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005225

NM_007891
NM_001291105

RefSeq (protein)

NP_005216

NP_001278034
NP_031917

Location (UCSC) Chr 20: 33.68 – 33.69 Mb Chr 2: 154.4 – 154.41 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Transcription factor E2F1 is a protein that in humans is encoded by the E2F1 gene. [5]

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. [6]

Transcription

E2F1 promoter[PAX8] => E2F1 [7]

Interactions

E2F1 has been shown to interact with:

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101412Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027490Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Neuman E, Sellers WR, McNeil JA, Lawrence JB, Kaelin WG (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.
  6. ^ "Entrez Gene: E2F1 E2F transcription factor 1".
  7. ^ Li CG, Nyman JE, Braithwaite AW, Eccles MR (December 2011). "PAX8 promotes tumor cell growth by transcriptionally regulating E2F1 and stabilizing RB protein". Oncogene. 30 (48): 4824–34. doi: 10.1038/onc.2011.190. PMC  3229668. PMID  21602887.
  8. ^ 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. 17 (7): 853–65. doi: 10.1038/sj.onc.1202163. PMID  9780002.
  9. ^ 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. 1 (1): 14–9. doi: 10.1038/8984. PMID  10559858. S2CID  8884226.
  10. ^ Yang R, Müller C, Huynh V, Fung YK, Yee AS, Koeffler HP (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. 19 (3): 2400–7. doi: 10.1128/mcb.19.3.2400. PMC  84032. PMID  10022926.
  11. ^ Xu M, Sheppard KA, Peng CY, Yee AS, 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. 14 (12): 8420–31. doi: 10.1128/MCB.14.12.8420. PMC  359381. PMID  7969176.
  12. ^ Vandel L, Kouzarides T (August 1999). "Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase". EMBO J. 18 (15): 4280–91. doi: 10.1093/emboj/18.15.4280. PMC  1171504. PMID  10428966.
  13. ^ Strachan GD, Jordan-Sciutto KL, Rallapalli R, Tuan RS, Hall DJ (February 2003). "The E2F-1 transcription factor is negatively regulated by its interaction with the MDMX protein". J. Cell. Biochem. 88 (3): 557–68. doi: 10.1002/jcb.10318. PMID  12532331. S2CID  38805122.
  14. ^ Kong HJ, Yu HJ, Hong S, Park MJ, Choi YH, An WG, Lee JW, Cheong J (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. 1 (13): 948–58. PMID  14638867.
  15. ^ 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. 273 (2): 720–8. doi: 10.1074/jbc.273.2.720. PMID  9422723.
  16. ^ Kuwako K, Taniura H, Yoshikawa K (January 2004). "Necdin-related MAGE proteins differentially interact with the E2F1 transcription factor and the p75 neurotrophin receptor". J. Biol. Chem. 279 (3): 1703–12. doi: 10.1074/jbc.M308454200. PMID  14593116.
  17. ^ 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. 19 (43): 5000–9. doi: 10.1038/sj.onc.1203843. PMID  11042687.
  18. ^ Darbinian N, Gallia GL, 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. 18 (46): 6398–402. doi: 10.1038/sj.onc.1203011. PMID  10597240.
  19. ^ Joshi B, Ko D, Ordonez-Ercan D, Chellappan SP (December 2003). "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. doi: 10.1016/j.bbrc.2003.10.148. PMID  14637159.
  20. ^ Fusaro G, Dasgupta P, Rastogi S, Joshi B, Chellappan S (November 2003). "Prohibitin induces the transcriptional activity of p53 and is exported from the nucleus upon apoptotic signaling". J. Biol. Chem. 278 (48): 47853–61. doi: 10.1074/jbc.M305171200. PMID  14500729.
  21. ^ Wang S, Zhang B, Faller DV (June 2002). "Prohibitin requires Brg-1 and Brm for the repression of E2F and cell growth". EMBO J. 21 (12): 3019–28. doi: 10.1093/emboj/cdf302. PMC  126057. PMID  12065415.
  22. ^ 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. 19 (11): 7447–60. doi: 10.1128/mcb.19.11.7447. PMC  84738. PMID  10523633.
  23. ^ 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. 67 (12): 7641–7. doi: 10.1128/JVI.67.12.7641-7647.1993. PMC  238233. PMID  8230483.
  24. ^ Nicolas E, Ait-Si-Ali S, Trouche D (August 2001). "The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein". Nucleic Acids Res. 29 (15): 3131–6. doi: 10.1093/nar/29.15.3131. PMC  55834. PMID  11470869.
  25. ^ Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM (December 2002). "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation". J. Biol. Chem. 277 (52): 50860–6. doi: 10.1074/jbc.M203839200. PMID  12397079.
  26. ^ a b Choubey D, Li SJ, Datta B, Gutterman JU, Lengyel P (October 1996). "Inhibition of E2F-mediated transcription by p202". EMBO J. 15 (20): 5668–78. doi: 10.1002/j.1460-2075.1996.tb00951.x. PMC  452311. PMID  8896460.
  27. ^ Fajas L, Paul C, Zugasti O, Le Cam L, Polanowska J, Fabbrizio E, Medema R, Vignais ML, 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. 97 (14): 7738–43. Bibcode: 2000PNAS...97.7738F. doi: 10.1073/pnas.130198397. PMC  16614. PMID  10869426.
  28. ^ a b Wu CL, Zukerberg LR, Ngwu C, Harlow E, Lees JA (May 1995). "In vivo association of E2F and DP family proteins". Mol. Cell. Biol. 15 (5): 2536–46. doi: 10.1128/mcb.15.5.2536. PMC  230484. PMID  7739537.
  29. ^ Walsh M, Shue G, Spidoni K, Kapoor A (March 1995). "E2F-1 and a cyclin-like DNA repair enzyme, uracil-DNA glycosylase, provide evidence for an auto-regulatory mechanisms for transcription". J. Biol. Chem. 270 (10): 5289–98. doi: 10.1074/jbc.270.10.5289. PMID  7534293.
  30. ^ 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. 293 (5): 1005–15. doi: 10.1006/jmbi.1999.3213. PMID  10547281.
  31. ^ Lin SY, Black AR, Kostic D, Pajovic S, Hoover CN, Azizkhan JC (April 1996). "Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction". Mol. Cell. Biol. 16 (4): 1668–75. doi: 10.1128/MCB.16.4.1668. PMC  231153. PMID  8657142.
  32. ^ Karlseder J, Rotheneder H, Wintersberger E (April 1996). "Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F". Mol. Cell. Biol. 16 (4): 1659–67. doi: 10.1128/mcb.16.4.1659. PMC  231152. PMID  8657141.
  33. ^ Sardet C, Vidal M, Cobrinik D, Geng Y, Onufryk C, Chen A, Weinberg RA (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. 92 (6): 2403–7. Bibcode: 1995PNAS...92.2403S. doi: 10.1073/pnas.92.6.2403. PMC  42492. PMID  7892279.
  34. ^ Helin K, Wu CL, Fattaey AR, Lees JA, Dynlacht BD, Ngwu C, Harlow E (October 1993). "Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative trans-activation". Genes Dev. 7 (10): 1850–61. doi: 10.1101/gad.7.10.1850. PMID  8405995.
  35. ^ Liu K, Lin FT, Ruppert JM, Lin WC (May 2003). "Regulation of E2F1 by BRCT domain-containing protein TopBP1". Mol. Cell. Biol. 23 (9): 3287–304. doi: 10.1128/mcb.23.9.3287-3304.2003. PMC  153207. PMID  12697828.
  36. ^ Yu X, Chini CC, He M, Mer G, Chen J (October 2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645): 639–42. Bibcode: 2003Sci...302..639Y. doi: 10.1126/science.1088753. PMID  14576433. S2CID  29407635.
  37. ^ Zhou F, Zhang L, Wang A, Song B, Gong K, Zhang L, Hu M, Zhang X, Zhao N, Gong Y (May 2008). "The association of GSK3 beta with E2F1 facilitates nerve growth factor-induced neural cell differentiation". J. Biol. Chem. 283 (21): 14506–15. 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.

From Wikipedia, the free encyclopedia
(Redirected from E2F1 (gene))
E2F1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases E2F1, E2F-1, RBAP1, RBBP3, RBP3, E2F transcription factor 1
External IDs OMIM: 189971; MGI: 101941; HomoloGene: 3828; GeneCards: E2F1; OMA: E2F1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005225

NM_007891
NM_001291105

RefSeq (protein)

NP_005216

NP_001278034
NP_031917

Location (UCSC) Chr 20: 33.68 – 33.69 Mb Chr 2: 154.4 – 154.41 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Transcription factor E2F1 is a protein that in humans is encoded by the E2F1 gene. [5]

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. [6]

Transcription

E2F1 promoter[PAX8] => E2F1 [7]

Interactions

E2F1 has been shown to interact with:

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101412Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027490Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Neuman E, Sellers WR, McNeil JA, Lawrence JB, Kaelin WG (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.
  6. ^ "Entrez Gene: E2F1 E2F transcription factor 1".
  7. ^ Li CG, Nyman JE, Braithwaite AW, Eccles MR (December 2011). "PAX8 promotes tumor cell growth by transcriptionally regulating E2F1 and stabilizing RB protein". Oncogene. 30 (48): 4824–34. doi: 10.1038/onc.2011.190. PMC  3229668. PMID  21602887.
  8. ^ 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. 17 (7): 853–65. doi: 10.1038/sj.onc.1202163. PMID  9780002.
  9. ^ 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. 1 (1): 14–9. doi: 10.1038/8984. PMID  10559858. S2CID  8884226.
  10. ^ Yang R, Müller C, Huynh V, Fung YK, Yee AS, Koeffler HP (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. 19 (3): 2400–7. doi: 10.1128/mcb.19.3.2400. PMC  84032. PMID  10022926.
  11. ^ Xu M, Sheppard KA, Peng CY, Yee AS, 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. 14 (12): 8420–31. doi: 10.1128/MCB.14.12.8420. PMC  359381. PMID  7969176.
  12. ^ Vandel L, Kouzarides T (August 1999). "Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase". EMBO J. 18 (15): 4280–91. doi: 10.1093/emboj/18.15.4280. PMC  1171504. PMID  10428966.
  13. ^ Strachan GD, Jordan-Sciutto KL, Rallapalli R, Tuan RS, Hall DJ (February 2003). "The E2F-1 transcription factor is negatively regulated by its interaction with the MDMX protein". J. Cell. Biochem. 88 (3): 557–68. doi: 10.1002/jcb.10318. PMID  12532331. S2CID  38805122.
  14. ^ Kong HJ, Yu HJ, Hong S, Park MJ, Choi YH, An WG, Lee JW, Cheong J (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. 1 (13): 948–58. PMID  14638867.
  15. ^ 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. 273 (2): 720–8. doi: 10.1074/jbc.273.2.720. PMID  9422723.
  16. ^ Kuwako K, Taniura H, Yoshikawa K (January 2004). "Necdin-related MAGE proteins differentially interact with the E2F1 transcription factor and the p75 neurotrophin receptor". J. Biol. Chem. 279 (3): 1703–12. doi: 10.1074/jbc.M308454200. PMID  14593116.
  17. ^ 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. 19 (43): 5000–9. doi: 10.1038/sj.onc.1203843. PMID  11042687.
  18. ^ Darbinian N, Gallia GL, 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. 18 (46): 6398–402. doi: 10.1038/sj.onc.1203011. PMID  10597240.
  19. ^ Joshi B, Ko D, Ordonez-Ercan D, Chellappan SP (December 2003). "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. doi: 10.1016/j.bbrc.2003.10.148. PMID  14637159.
  20. ^ Fusaro G, Dasgupta P, Rastogi S, Joshi B, Chellappan S (November 2003). "Prohibitin induces the transcriptional activity of p53 and is exported from the nucleus upon apoptotic signaling". J. Biol. Chem. 278 (48): 47853–61. doi: 10.1074/jbc.M305171200. PMID  14500729.
  21. ^ Wang S, Zhang B, Faller DV (June 2002). "Prohibitin requires Brg-1 and Brm for the repression of E2F and cell growth". EMBO J. 21 (12): 3019–28. doi: 10.1093/emboj/cdf302. PMC  126057. PMID  12065415.
  22. ^ 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. 19 (11): 7447–60. doi: 10.1128/mcb.19.11.7447. PMC  84738. PMID  10523633.
  23. ^ 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. 67 (12): 7641–7. doi: 10.1128/JVI.67.12.7641-7647.1993. PMC  238233. PMID  8230483.
  24. ^ Nicolas E, Ait-Si-Ali S, Trouche D (August 2001). "The histone deacetylase HDAC3 targets RbAp48 to the retinoblastoma protein". Nucleic Acids Res. 29 (15): 3131–6. doi: 10.1093/nar/29.15.3131. PMC  55834. PMID  11470869.
  25. ^ Pardo PS, Leung JK, Lucchesi JC, Pereira-Smith OM (December 2002). "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation". J. Biol. Chem. 277 (52): 50860–6. doi: 10.1074/jbc.M203839200. PMID  12397079.
  26. ^ a b Choubey D, Li SJ, Datta B, Gutterman JU, Lengyel P (October 1996). "Inhibition of E2F-mediated transcription by p202". EMBO J. 15 (20): 5668–78. doi: 10.1002/j.1460-2075.1996.tb00951.x. PMC  452311. PMID  8896460.
  27. ^ Fajas L, Paul C, Zugasti O, Le Cam L, Polanowska J, Fabbrizio E, Medema R, Vignais ML, 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. 97 (14): 7738–43. Bibcode: 2000PNAS...97.7738F. doi: 10.1073/pnas.130198397. PMC  16614. PMID  10869426.
  28. ^ a b Wu CL, Zukerberg LR, Ngwu C, Harlow E, Lees JA (May 1995). "In vivo association of E2F and DP family proteins". Mol. Cell. Biol. 15 (5): 2536–46. doi: 10.1128/mcb.15.5.2536. PMC  230484. PMID  7739537.
  29. ^ Walsh M, Shue G, Spidoni K, Kapoor A (March 1995). "E2F-1 and a cyclin-like DNA repair enzyme, uracil-DNA glycosylase, provide evidence for an auto-regulatory mechanisms for transcription". J. Biol. Chem. 270 (10): 5289–98. doi: 10.1074/jbc.270.10.5289. PMID  7534293.
  30. ^ 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. 293 (5): 1005–15. doi: 10.1006/jmbi.1999.3213. PMID  10547281.
  31. ^ Lin SY, Black AR, Kostic D, Pajovic S, Hoover CN, Azizkhan JC (April 1996). "Cell cycle-regulated association of E2F1 and Sp1 is related to their functional interaction". Mol. Cell. Biol. 16 (4): 1668–75. doi: 10.1128/MCB.16.4.1668. PMC  231153. PMID  8657142.
  32. ^ Karlseder J, Rotheneder H, Wintersberger E (April 1996). "Interaction of Sp1 with the growth- and cell cycle-regulated transcription factor E2F". Mol. Cell. Biol. 16 (4): 1659–67. doi: 10.1128/mcb.16.4.1659. PMC  231152. PMID  8657141.
  33. ^ Sardet C, Vidal M, Cobrinik D, Geng Y, Onufryk C, Chen A, Weinberg RA (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. 92 (6): 2403–7. Bibcode: 1995PNAS...92.2403S. doi: 10.1073/pnas.92.6.2403. PMC  42492. PMID  7892279.
  34. ^ Helin K, Wu CL, Fattaey AR, Lees JA, Dynlacht BD, Ngwu C, Harlow E (October 1993). "Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative trans-activation". Genes Dev. 7 (10): 1850–61. doi: 10.1101/gad.7.10.1850. PMID  8405995.
  35. ^ Liu K, Lin FT, Ruppert JM, Lin WC (May 2003). "Regulation of E2F1 by BRCT domain-containing protein TopBP1". Mol. Cell. Biol. 23 (9): 3287–304. doi: 10.1128/mcb.23.9.3287-3304.2003. PMC  153207. PMID  12697828.
  36. ^ Yu X, Chini CC, He M, Mer G, Chen J (October 2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645): 639–42. Bibcode: 2003Sci...302..639Y. doi: 10.1126/science.1088753. PMID  14576433. S2CID  29407635.
  37. ^ Zhou F, Zhang L, Wang A, Song B, Gong K, Zhang L, Hu M, Zhang X, Zhao N, Gong Y (May 2008). "The association of GSK3 beta with E2F1 facilitates nerve growth factor-induced neural cell differentiation". J. Biol. Chem. 283 (21): 14506–15. 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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