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Activating transcription factor 2

PDB rendering based on 1bhi.
Available structures
1bhi, 1t2k
Identifiers
Symbols ATF2; CREB2; CRE-BP1; HB16; MGC111558; TREB7
External IDs OMIM123811 MGI109349 HomoloGene31061 GeneCards: ATF2 Gene
RNA expression pattern
PBB GE ATF2 205446 s at tn.png
PBB GE ATF2 212984 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1386 11909
Ensembl ENSG00000115966 ENSMUSG00000027104
UniProt P15336 P70299
RefSeq (mRNA) NM_001880 NM_001025093
RefSeq (protein) NP_001871 NP_001020264
Location (UCSC) Chr 2:
175.65 - 175.74 Mb
Chr 2:
73.62 - 73.66 Mb
PubMed search [1] [2]

Activating transcription factor 2, also known as ATF2, is a protein which in humans is encoded by the ATF2 gene.[1]

Contents

Function

This gene encodes a transcription factor that is a member of the leucine zipper family of DNA binding proteins. This protein binds to the cAMP-responsive element (CRE), an octameric palindrome. The protein forms a homodimer or heterodimer with c-Jun and stimulates CRE-dependent transcription. The protein is also a histone acetyltransferase (HAT) that specifically acetylates histones H2B and H4 in vitro; thus it may represent a class of sequence-specific factors that activate transcription by direct effects on chromatin components. Additional transcript variants have been identified but their biological validity has not been determined.[1]

The gene atf2 is located at human chromosome 2q32.[2] The protein ATF-2 has 505 amino acids. Studies in mice indicate a role for ATF-2 in the development of nervous system and the skeleton.[3] ATF-2 is normally activated in response to signals that converge on stress-activated protein kinases p38 and JNK.[4] ATF-2 phosphorylation in response to treatment of cells with tumor promoter phorbol ester has been demonstrated.[5] Several studies implicate abnormal activation of ATF-2 in growth and progression of mammalian skin tumors.[6][7] ATF-2 may mediate oncogenesis caused by mutant Ras protein[8] and regulate maintenance of the aggressive cancer phenotype of some types of epithelial cells.

Interactions

Activating transcription factor 2 has been shown to interact with NCOA6,[9] RUVBL2,[10] CSNK2A2,[11] MAPK14,[12][13][14] Casein kinase 2, alpha 1,[11] JDP2,[15] MAPK8,[12][16][13][14] CREB binding protein,[17] C-jun,[18][19][20] Mothers against decapentaplegic homolog 3[21] and UBE2I.[22]

See also

References

  1. ^ a b "Entrez Gene: ATF2 activating transcription factor 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1386.  
  2. ^ Ozawa K, Sudo T, Soeda E, Yoshida MC, Ishii S (1991). "Assignment of the human CREB2 (CRE-BP1) gene to 2q32". Genomics 10 (4): 1103–4. doi:10.1016/0888-7543(91)90210-6. PMID 1833307.  
  3. ^ Reimold AM, Grusby MJ, Kosaras B, et al. (1996). "Chondrodysplasia and neurological abnormalities in ATF-2-deficient mice". Nature 379 (6562): 262–5. doi:10.1038/379262a0. PMID 8538792.  
  4. ^ Gupta S, Campbell D, Dérijard B, Davis RJ (1995). "Transcription factor ATF2 regulation by the JNK signal transduction pathway". Science 267 (5196): 389–93. doi:0.1126/science.7824938. PMID 7824938.  
  5. ^ Yamasaki T, Takahashi A, Pan J, Yamaguchi N, Yokoyama KK (March 2009). "Phosphorylation of Activation Transcription Factor-2 at Serine 121 by Protein Kinase C Controls c-Jun-mediated Activation of Transcription". J. Biol. Chem. 284 (13): 8567–81. doi:10.1074/jbc.M808719200. PMID 19176525.  
  6. ^ Leslie MC, Bar-Eli M (2005). "Regulation of gene expression in melanoma: new approaches for treatment". J. Cell. Biochem. 94 (1): 25–38. doi:10.1002/jcb.20296. PMID 15523674.  
  7. ^ Papassava P, Gorgoulis VG, Papaevangeliou D, Vlahopoulos S, van Dam H, Zoumpourlis V (2004). "Overexpression of activating transcription factor-2 is required for tumor growth and progression in mouse skin tumors". Cancer Res. 64 (23): 8573–84. doi:10.1158/0008-5472.CAN-03-0955. PMID 15574764.  
  8. ^ Vlahopoulos SA, Logotheti S, Mikas D, Giarika A, Gorgoulis V, Zoumpourlis V (2008-03-17). "The role of ATF-2 in oncogenesis". Bioessays 30 (4): 314–327. doi:10.1002/bies.20734. PMID 18348191.  
  9. ^ Hong, SunHwa; Choi Hyun Mi, Park Min Jung, Kim Young Hee, Choi Yoon Ha, Kim Hyung Hoi, Choi Young Hyun, Cheong JaeHun (Apr. 2004). "Activation and interaction of ATF2 with the coactivator ASC-2 are responsive for granulocytic differentiation by retinoic acid". J. Biol. Chem. (United States) 279 (17): 16996–7003. doi:10.1074/jbc.M311752200. ISSN 0021-9258. PMID 14734562.  
  10. ^ Cho, S G; Bhoumik A, Broday L, Ivanov V, Rosenstein B, Ronai Z (Dec. 2001). "TIP49b, a regulator of activating transcription factor 2 response to stress and DNA damage". Mol. Cell. Biol. (United States) 21 (24): 8398–413. doi:10.1128/MCB.21.24.8398-8413.2001. ISSN 0270-7306. PMID 11713276.  
  11. ^ a b Yamaguchi, Y; Wada T, Suzuki F, Takagi T, Hasegawa J, Handa H (Aug. 1998). "Casein kinase II interacts with the bZIP domains of several transcription factors". Nucleic Acids Res. (ENGLAND) 26 (16): 3854–61. ISSN 0305-1048. PMID 9685505.  
  12. ^ a b Raingeaud, J; Gupta S, Rogers J S, Dickens M, Han J, Ulevitch R J, Davis R J (Mar. 1995). "Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine". J. Biol. Chem. (UNITED STATES) 270 (13): 7420–6. ISSN 0021-9258. PMID 7535770.  
  13. ^ a b Chen, Z; Cobb M H (May. 2001). "Regulation of stress-responsive mitogen-activated protein (MAP) kinase pathways by TAO2". J. Biol. Chem. (United States) 276 (19): 16070–5. doi:10.1074/jbc.M100681200. ISSN 0021-9258. PMID 11279118.  
  14. ^ a b Tournier, C; Whitmarsh A J, Cavanagh J, Barrett T, Davis R J (Jul. 1997). "Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 94 (14): 7337–42. ISSN 0027-8424. PMID 9207092.  
  15. ^ Murata, Takehide; Shinozuka Yoriko, Obata Yuichi, Yokoyama Kazunari K (May. 2008). "Phosphorylation of two eukaryotic transcription factors, Jun dimerization protein 2 and activation transcription factor 2, in Escherichia coli by Jun N-terminal kinase 1". Anal. Biochem. (United States) 376 (1): 115–21. doi:10.1016/j.ab.2008.01.038. PMID 18307971.  
  16. ^ Fuchs, S Y; Xie B, Adler V, Fried V A, Davis R J, Ronai Z (Dec. 1997). "c-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factors". J. Biol. Chem. (UNITED STATES) 272 (51): 32163–8. ISSN 0021-9258. PMID 9405416.  
  17. ^ Sano, Y; Tokitou F, Dai P, Maekawa T, Yamamoto T, Ishii S (Oct. 1998). "CBP alleviates the intramolecular inhibition of ATF-2 function". J. Biol. Chem. (UNITED STATES) 273 (44): 29098–105. ISSN 0021-9258. PMID 9786917.  
  18. ^ Newell, C L; Deisseroth A B, Lopez-Berestein G (Jul. 1994). "Interaction of nuclear proteins with an AP-1/CRE-like promoter sequence in the human TNF-alpha gene". J. Leukoc. Biol. (UNITED STATES) 56 (1): 27–35. ISSN 0741-5400. PMID 8027667.  
  19. ^ Kara, C J; Liou H C, Ivashkiv L B, Glimcher L H (Apr. 1990). "A cDNA for a human cyclic AMP response element-binding protein which is distinct from CREB and expressed preferentially in brain". Mol. Cell. Biol. (UNITED STATES) 10 (4): 1347–57. ISSN 0270-7306. PMID 2320002.  
  20. ^ Hai, T; Curran T (May. 1991). "Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 88 (9): 3720–4. ISSN 0027-8424. PMID 1827203.  
  21. ^ Sano, Y; Harada J, Tashiro S, Gotoh-Mandeville R, Maekawa T, Ishii S (Mar. 1999). "ATF-2 is a common nuclear target of Smad and TAK1 pathways in transforming growth factor-beta signaling". J. Biol. Chem. (UNITED STATES) 274 (13): 8949–57. ISSN 0021-9258. PMID 10085140.  
  22. ^ Firestein, R; Feuerstein N (Mar. 1998). "Association of activating transcription factor 2 (ATF2) with the ubiquitin-conjugating enzyme hUBC9. Implication of the ubiquitin/proteasome pathway in regulation of ATF2 in T cells". J. Biol. Chem. (UNITED STATES) 273 (10): 5892–902. ISSN 0021-9258. PMID 9488727.  

Further reading

  • Denys H, Desmet R, Stragier M, et al. (1978). "Cystitis emphysematosa.". Acta urologica Belgica 45 (4): 327–31. PMID 602896.  
  • Kim SJ, Wagner S, Liu F, et al. (1992). "Retinoblastoma gene product activates expression of the human TGF-beta 2 gene through transcription factor ATF-2.". Nature 358 (6384): 331–4. doi:10.1038/358331a0. PMID 1641004.  
  • Hai T, Curran T (1991). "Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity.". Proc. Natl. Acad. Sci. U.S.A. 88 (9): 3720–4. doi:10.1073/pnas.88.9.3720. PMID 1827203.  
  • Hoeffler JP, Lustbader JW, Chen CY (1991). "Identification of multiple nuclear factors that interact with cyclic adenosine 3',5'-monophosphate response element-binding protein and activating transcription factor-2 by protein-protein interactions.". Mol. Endocrinol. 5 (2): 256–66. doi:10.1210/mend-5-2-256. PMID 1828107.  
  • Ozawa K, Sudo T, Soeda E, et al. (1991). "Assignment of the human CREB2 (CRE-BP1) gene to 2q32.". Genomics 10 (4): 1103–4. doi:10.1016/0888-7543(91)90210-6. PMID 1833307.  
  • Diep A, Li C, Klisak I, et al. (1992). "Assignment of the gene for cyclic AMP-response element binding protein 2 (CREB2) to human chromosome 2q24.1-q32.". Genomics 11 (4): 1161–3. doi:10.1016/0888-7543(91)90047-I. PMID 1838349.  
  • Kara CJ, Liou HC, Ivashkiv LB, Glimcher LH (1990). "A cDNA for a human cyclic AMP response element-binding protein which is distinct from CREB and expressed preferentially in brain.". Mol. Cell. Biol. 10 (4): 1347–57. PMID 2320002.  
  • Gonzalez GA, Yamamoto KK, Fischer WH, et al. (1989). "A cluster of phosphorylation sites on the cyclic AMP-regulated nuclear factor CREB predicted by its sequence.". Nature 337 (6209): 749–52. doi:10.1038/337749a0. PMID 2521922.  
  • Maekawa T, Sakura H, Kanei-Ishii C, et al. (1989). "Leucine zipper structure of the protein CRE-BP1 binding to the cyclic AMP response element in brain.". Embo J. 8 (7): 2023–8. PMID 2529117.  
  • Raingeaud J, Gupta S, Rogers JS, et al. (1995). "Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine.". J. Biol. Chem. 270 (13): 7420–6. doi:10.1074/jbc.270.13.7420. PMID 7535770.  
  • Livingstone C, Patel G, Jones N (1995). "ATF-2 contains a phosphorylation-dependent transcriptional activation domain.". Embo J. 14 (8): 1785–97. PMID 7737129.  
  • van Dam H, Wilhelm D, Herr I, et al. (1995). "ATF-2 is preferentially activated by stress-activated protein kinases to mediate c-jun induction in response to genotoxic agents.". Embo J. 14 (8): 1798–811. PMID 7737130.  
  • Zhou Q, Gedrich RW, Engel DA (1995). "Transcriptional repression of the c-fos gene by YY1 is mediated by a direct interaction with ATF/CREB.". J. Virol. 69 (7): 4323–30. PMID 7769693.  
  • Newell CL, Deisseroth AB, Lopez-Berestein G (1994). "Interaction of nuclear proteins with an AP-1/CRE-like promoter sequence in the human TNF-alpha gene.". J. Leukoc. Biol. 56 (1): 27–35. PMID 8027667.  
  • Nomura N, Zu YL, Maekawa T, et al. (1993). "Isolation and characterization of a novel member of the gene family encoding the cAMP response element-binding protein CRE-BP1.". J. Biol. Chem. 268 (6): 4259–66. PMID 8440710.  
  • Martin ML, Lieberman PM, Curran T (1996). "Fos-Jun dimerization promotes interaction of the basic region with TFIIE-34 and TFIIF.". Mol. Cell. Biol. 16 (5): 2110–8. PMID 8628277.  
  • Yang L, Lanier ER, Kraig E (1997). "Identification of a novel, spliced variant of CREB that is preferentially expressed in the thymus.". J. Immunol. 158 (6): 2522–5. PMID 9058782.  
  • Shuman JD, Cheong J, Coligan JE (1997). "ATF-2 and C/EBPalpha can form a heterodimeric DNA binding complex in vitro. Functional implications for transcriptional regulation.". J. Biol. Chem. 272 (19): 12793–800. doi:10.1074/jbc.272.19.12793. PMID 9139739.  
  • Fukunaga R, Hunter T (1997). "MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates.". Embo J. 16 (8): 1921–33. doi:10.1093/emboj/16.8.1921. PMID 9155018.  
  • Kumar S, McDonnell PC, Gum RJ, et al. (1997). "Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles.". Biochem. Biophys. Res. Commun. 235 (3): 533–8. doi:10.1006/bbrc.1997.6849. PMID 9207191.  
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