CCAAT/enhancer binding protein (C/EBP), epsilon, also known as CEBPE and CHOP, is a type of ccaat-enhancer-binding protein. CEBPE is its human gene.[1][2] It is pro-apoptotic.[3] The protein encoded by this gene is a bZIP transcription factor which can bind as a homodimer to certain DNA regulatory regions. It can also form heterodimers with the related protein CEBP-δ. The encoded protein may be essential for terminal differentiation and functional maturation of committed granulocyte progenitor cells. Mutations in this gene have been associated with specific granule deficiency, a rare congenital disorder. Multiple variants of this gene have been described, but the full-length nature of only one has been determined.[1] [edit] References - ^ a b "Entrez Gene: CEBPE CCAAT/enhancer binding protein (C/EBP), epsilon". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1053.
- ^ Antonson P, Stellan B, Yamanaka R, Xanthopoulos KG (July 1996). "A novel human CCAAT/enhancer binding protein gene, C/EBPepsilon, is expressed in cells of lymphoid and myeloid lineages and is localized on chromosome 14q11.2 close to the T-cell receptor alpha/delta locus". Genomics 35 (1): 30–8. doi:10.1006/geno.1996.0319. PMID 8661101.
- ^ Nakajima H, Watanabe N, Shibata F, Kitamura T, Ikeda Y, Handa M (May 2006). "N-terminal region of CCAAT/enhancer-binding protein epsilon is critical for cell cycle arrest, apoptosis, and functional maturation during myeloid differentiation". J. Biol. Chem. 281 (20): 14494–502. doi:10.1074/jbc.M600575200. PMID 16531405.
[edit] Further reading - Sladek FM, Darnell JE (1992). "Mechanisms of liver-specific gene expression.". Curr. Opin. Genet. Dev. 2 (2): 256–9. doi:10.1016/S0959-437X(05)80282-5. PMID 1638120.
- Gombart AF, Koeffler HP (2002). "Neutrophil specific granule deficiency and mutations in the gene encoding transcription factor C/EBP(epsilon).". Curr. Opin. Hematol. 9 (1): 36–42. doi:10.1097/00062752-200201000-00007. PMID 11753076.
- Williams SC, Cantwell CA, Johnson PF (1991). "A family of C/EBP-related proteins capable of forming covalently linked leucine zipper dimers in vitro.". Genes Dev. 5 (9): 1553–67. doi:10.1101/gad.5.9.1553. PMID 1884998.
- Antonson P, Stellan B, Yamanaka R, Xanthopoulos KG (1996). "A novel human CCAAT/enhancer binding protein gene, C/EBPepsilon, is expressed in cells of lymphoid and myeloid lineages and is localized on chromosome 14q11.2 close to the T-cell receptor alpha/delta locus.". Genomics 35 (1): 30–8. doi:10.1006/geno.1996.0319. PMID 8661101.
- Chumakov AM, Grillier I, Chumakova E, et al. (1997). "Cloning of the novel human myeloid-cell-specific C/EBP-epsilon transcription factor.". Mol. Cell. Biol. 17 (3): 1375–86. PMID 9032264.
- Yamanaka R, Kim GD, Radomska HS, et al. (1997). "CCAAT/enhancer binding protein epsilon is preferentially up-regulated during granulocytic differentiation and its functional versatility is determined by alternative use of promoters and differential splicing.". Proc. Natl. Acad. Sci. U.S.A. 94 (12): 6462–7. doi:10.1073/pnas.94.12.6462. PMID 9177240.
- Verbeek W, Gombart AF, Chumakov AM, et al. (1999). "C/EBPepsilon directly interacts with the DNA binding domain of c-myb and cooperatively activates transcription of myeloid promoters.". Blood 93 (10): 3327–37. PMID 10233885.
- Lekstrom-Himes JA, Dorman SE, Kopar P, et al. (1999). "Neutrophil-specific granule deficiency results from a novel mutation with loss of function of the transcription factor CCAAT/enhancer binding protein epsilon.". J. Exp. Med. 189 (11): 1847–52. doi:10.1084/jem.189.11.1847. PMID 10359588.
- Tavor S, Vuong PT, Park DJ, et al. (2002). "Macrophage functional maturation and cytokine production are impaired in C/EBP epsilon-deficient mice.". Blood 99 (5): 1794–801. doi:10.1182/blood.V99.5.1794. PMID 11861297.
- Zhang P, Nelson E, Radomska HS, et al. (2002). "Induction of granulocytic differentiation by 2 pathways.". Blood 99 (12): 4406–12. doi:10.1182/blood.V99.12.4406. PMID 12036869.
- Kim J, Cantwell CA, Johnson PF, et al. (2002). "Transcriptional activity of CCAAT/enhancer-binding proteins is controlled by a conserved inhibitory domain that is a target for sumoylation.". J. Biol. Chem. 277 (41): 38037–44. doi:10.1074/jbc.M207235200. PMID 12161447.
- Du J, Stankiewicz MJ, Liu Y, et al. (2003). "Novel combinatorial interactions of GATA-1, PU.1, and C/EBPepsilon isoforms regulate transcription of the gene encoding eosinophil granule major basic protein.". J. Biol. Chem. 277 (45): 43481–94. doi:10.1074/jbc.M204777200. PMID 12202480.
- Truong BT, Lee YJ, Lodie TA, et al. (2003). "CCAAT/Enhancer binding proteins repress the leukemic phenotype of acute myeloid leukemia.". Blood 101 (3): 1141–8. doi:10.1182/blood-2002-05-1374. PMID 12393450.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
- Gombart AF, Kwok SH, Anderson KL, et al. (2003). "Regulation of neutrophil and eosinophil secondary granule gene expression by transcription factors C/EBP epsilon and PU.1.". Blood 101 (8): 3265–73. doi:10.1182/blood-2002-04-1039. PMID 12515729.
- Khanna-Gupta A, Zibello T, Sun H, et al. (2003). "Chromatin immunoprecipitation (ChIP) studies indicate a role for CCAAT enhancer binding proteins alpha and epsilon (C/EBP alpha and C/EBP epsilon ) and CDP/cut in myeloid maturation-induced lactoferrin gene expression.". Blood 101 (9): 3460–8. doi:10.1182/blood-2002-09-2767. PMID 12522000.
- Gery S, Gombart AF, Fung YK, Koeffler HP (2004). "C/EBPepsilon interacts with retinoblastoma and E2F1 during granulopoiesis.". Blood 103 (3): 828–35. doi:10.1182/blood-2003-01-0159. PMID 12947005.
- Gery S, Park DJ, Vuong PT, et al. (2005). "Retinoic acid regulates C/EBP homologous protein expression (CHOP), which negatively regulates myeloid target genes.". Blood 104 (13): 3911–7. doi:10.1182/blood-2003-10-3688. PMID 15308577.
[edit] External links This article incorporates text from the United States National Library of Medicine, which is in the public domain. | Transcription factors and intracellular receptors | | | (1) Basic domains | | | | Activating transcription factor ( AATF, 1, 2, 3, 4, 5, 6, 7) · AP-1 ( c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) · BACH ( 1, 2) · BATF · BLZF1 · C/EBP ( α, β, γ, δ, ε, ζ) · CREB ( 1, 3, L1) · CREM · DBP · DDIT3 · GABPA · HLF · MAF ( B, F, G, K) · NFE ( 2, L1, L2) · NFIL3 · NRL · NRF1 · XBP1 | | (1.2) Basic helix-loop-helix ( bHLH) | ATOH1 · AhR · AHRR · ARNT · ASCL1 · BHLHB2 · BMAL ( ARNTL, ARNTL2) · CLOCK · EPAS1 · HAND ( 1, 2) · HES ( 5, 6) · HEY ( 1, 2, L) · HES1 · HIF ( 1A, 3A) · ID ( 1, 2, 3, 4) · LYL1 · MXD4 · MYCL1 · MYCN · Myogenic regulatory factors ( MyoD, Myogenin, MYF5, MYF6) · Neurogenins · NeuroD ( 1, 2) · NPAS ( 1, 2, 3) · OLIG ( 1, 2) · Pho4 · Scleraxis · TAL ( 1, 2) · Twist · USF1 | | | | | | | (1.4) NF-1 | | | | (1.5) RF-X | | | | (1.6) Basic helix-span-helix (bHSH) | | | | | | (2) Zinc finger DNA-binding domains | | | | subfamily 1 ( Thyroid hormone ( α, β), CAR, FXR, LXR ( α, β), PPAR ( α, β/δ, γ), PXR, RAR ( α, β, γ), ROR ( α, β, γ), Rev-ErbA ( α, β), VDR) subfamily 2 ( COUP-TF ( I, II), Ear-2, HNF4 ( α, γ), PNR, RXR ( α, β, γ), Testicular receptor ( 2, 4), TLX) subfamily 3 ( Steroid hormone ( Androgen, Estrogen ( α, β), Glucocorticoid, Mineralocorticoid, Progesterone), Estrogen related ( α, β, γ)) subfamily 4 NUR ( NGFIB, NOR1, NURR1) · subfamily 5 ( LRH-1, SF1) · subfamily 6 ( GCNF) · subfamily 0 ( DAX1, SHP) | | | (2.2) Other Cys4 | | | | (2.3) Cys2His2 | General transcription factors ( TFIIA, TFIIB, TFIID, TFIIE, TFIIF ( 1, 2), TFIIH ( 1, 2, 4, 2I, 3A, 3C1, 3C2)) ATBF1 · BCL ( 6, 11A, 11B) · CTCF · E4F1 · EGR ( 2, 3) · ERV3 · GFI1 · GLI-Krüppel family ( 1, 2, 3, REST, S2, YY1) · HIC ( 1, 2) · HIVEP ( 1, 2, 3) · IKZF ( 1, 2, 3) · ILF ( 2, 3) · KLF ( 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 17) · MTF1 · MYT1 · OSR1 · SP ( 1, 2, 4, 7) · Zbtb7 ( 7A, 7B) · ZBTB ( 16, 17, 20, 32, 33, 40) · zinc finger ( 3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 423, 451, 452, 471, 593, 638, 649, 655) | | | (2.4) Cys6 | | | | (2.5) Alternating composition | | | | | | (3) Helix-turn-helix domains | | | | ARX · CDX ( 1, 2) · CRX · CUTL1 · DLX ( 3, 4, 5) · EMX2 · EN ( 1, 2) · FHL ( 1, 2, 3) · HESX1 · HHEX · HLX · Homeobox ( A1, A2, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) · HOPX · LMX ( 1A, 1B) · MEIS ( 1, 2) · MEOX2 · MNX1 · MSX ( 1, 2) · NANOG · NKX ( 2-1, 2-2, 2-3, 2-5, 3-1, 3-2) · PBX ( 1, 2, 3) · PHF ( 1, 3, 6, 8, 10, 16, 17, 20, 21A) · PITX ( 1, 2, 3) · POU domain ( PIT-1, BRN-3: A, B, C, Octamer transcription factor: 1, 2, 3/4, 6, 7, 11) · OTX ( 1, 2) · PDX1 · ZEB ( 1, 2) | | | (3.2) Paired box | | | | | E2F ( 1, 2, 3, 4, 5) · FOX proteins ( C1, C2, D3, E1, G1, H1, K2, L2, M1, N3, O1, O3, O4, P1, P2, P3) | | | | | | | (3.5) Tryptophan clusters | ELF ( 2, 4, 5) · EGF · ELK ( 1, 3, 4) · ERF · ERG · ETS ( 1, 2, SPIB) · ETV ( 1, 4, 5, 6) · FLI1 · Interferon regulatory factors ( 1, 2, 3, 4, 5, 6, 7, 8) · MYB · MYBL2 | | | (3.6) TEA domain | transcriptional enhancer factor ( 1, 2, 3, 4) | | | | | (4) β-Scaffold factors with minor groove contacts | | | | | | | | | | | (4.3) p53 | | | | | | | | | | | | | HMGB ( 1, 2, 3) · HNF ( 1A, 1B) · LEF1 · SOX ( 1, 2, 3, 4, 5, 6, 8, 9, 10, 11, 12, 13, 14, 15, 18, 21) · SRY · SSRP1 · TCF ( 3, 4) · TOX ( 1, 2, 3, 4) | | | (4.10) Cold-shock domain | | | | (4.11) Runt | | | | | | (0) Other transcription factors | | | (0.2) HMGI(Y) | | | | | | | | | | | | (0.6) Miscellaneous | ARID ( 1A, 1B, 2, 3A, 3B, 4A) · CAP · IFI ( 16, 35) · MLL ( 2, 3, T1) · MNDA · NFY ( A, B, C) · Rho/ Sigma | | | | |