Open Access Articles- Top Results for CREB1


SymbolsCREB1 ; CREB
External IDsOMIM123810 MGI88494 HomoloGene3223 ChEMBL: 5587 GeneCards: CREB1 Gene
RNA expression pattern
File:PBB GE CREB1 204313 s at tn.png
File:PBB GE CREB1 204312 x at tn.png
File:PBB GE CREB1 204314 s at tn.png
More reference expression data
RefSeq (mRNA)NM_004379NM_001037726
RefSeq (protein)NP_004370NP_001032815
Location (UCSC)Chr 2:
208.39 – 208.47 Mb
Chr 1:
64.53 – 64.6 Mb
PubMed search[1][2]

CAMP responsive element binding protein 1, also known as CREB-1, is a protein that in humans is encoded by the CREB1 gene.[1][2] This protein binds the cAMP response element, a DNA nucleotide sequence present in many viral and cellular promoters. The binding of CREB1 stimulates transcription.

This protein is a CREB transcription factor that is a member of the leucine zipper family of DNA-binding proteins. This protein binds as a homodimer to the cAMP-responsive element, an octameric palindrome. The protein is phosphorylated by several protein kinases, and induces transcription of genes in response to hormonal stimulation of the cAMP pathway. Alternate splicing of this gene results in two transcript variants encoding different isoforms.[3]

See also


CREB1 has been shown to interact with:


  1. ^ Hoeffler JP, Meyer TE, Yun Y, Jameson JL, Habener JF (December 1988). "Cyclic AMP-responsive DNA-binding protein: structure based on a cloned placental cDNA". Science 242 (4884): 1430–3. PMID 2974179. doi:10.1126/science.2974179. 
  2. ^ Taylor AK, Klisak I, Mohandas T, Sparkes RS, Li C, Gaynor R, Lusis AJ (July 1990). "Assignment of the human gene for CREB1 to chromosome 2q32.3-q34". Genomics 7 (3): 416–21. PMID 2142119. doi:10.1016/0888-7543(90)90176-U. 
  3. ^ "Entrez Gene: CREB1 cAMP responsive element binding protein 1". 
  4. ^ Chen Y, Zhuang S, Cassenaer S, Casteel DE, Gudi T, Boss GR, Pilz RB (June 2003). "Synergism between calcium and cyclic GMP in cyclic AMP response element-dependent transcriptional regulation requires cooperation between CREB and C/EBP-beta". Mol. Cell. Biol. 23 (12): 4066–82. PMC 156132. PMID 12773552. doi:10.1128/MCB.23.12.4066-4082.2003. 
  5. ^ Shi Y, Venkataraman SL, Dodson GE, Mabb AM, LeBlanc S, Tibbetts RS (April 2004). "Direct regulation of CREB transcriptional activity by ATM in response to genotoxic stress". Proc. Natl. Acad. Sci. U.S.A. 101 (16): 5898–903. PMC 395895. PMID 15073328. doi:10.1073/pnas.0307718101. 
  6. ^ Kim J, Jia L, Stallcup MR, Coetzee GA (February 2005). "The role of protein kinase A pathway and cAMP responsive element-binding protein in androgen receptor-mediated transcription at the prostate-specific antigen locus". J. Mol. Endocrinol. 34 (1): 107–18. PMID 15691881. doi:10.1677/jme.1.01701. 
  7. ^ Shimomura A, Ogawa Y, Kitani T, Fujisawa H, Hagiwara M (July 1996). "Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein". J. Biol. Chem. 271 (30): 17957–60. PMID 8663317. doi:10.1074/jbc.271.30.17957. 
  8. ^ Radhakrishnan I, Pérez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, Wright PE (December 1997). "Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions". Cell 91 (6): 741–52. PMID 9413984. doi:10.1016/S0092-8674(00)80463-8. 
  9. ^ Sano Y, Tokitou F, Dai P, Maekawa T, Yamamoto T, Ishii S (October 1998). "CBP alleviates the intramolecular inhibition of ATF-2 function". J. Biol. Chem. 273 (44): 29098–105. PMID 9786917. doi:10.1074/jbc.273.44.29098. 
  10. ^ Zor T, Mayr BM, Dyson HJ, Montminy MR, Wright PE (November 2002). "Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators". J. Biol. Chem. 277 (44): 42241–8. PMID 12196545. doi:10.1074/jbc.M207361200. 
  11. ^ a b Giebler HA, Lemasson I, Nyborg JK (July 2000). "p53 recruitment of CREB binding protein mediated through phosphorylated CREB: a novel pathway of tumor suppressor regulation". Mol. Cell. Biol. 20 (13): 4849–58. PMC 85936. PMID 10848610. doi:10.1128/MCB.20.13.4849-4858.2000. 
  12. ^ Zhang Q, Vo N, Goodman RH (July 2000). "Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB". Mol. Cell. Biol. 20 (14): 4970–8. PMC 85947. PMID 10866654. doi:10.1128/MCB.20.14.4970-4978.2000. 
  13. ^ Ernst P, Wang J, Huang M, Goodman RH, Korsmeyer SJ (April 2001). "MLL and CREB bind cooperatively to the nuclear coactivator CREB-binding protein". Mol. Cell. Biol. 21 (7): 2249–58. PMC 86859. PMID 11259575. doi:10.1128/MCB.21.7.2249-2258.2001. 
  14. ^ Ledo F, Kremer L, Mellström B, Naranjo JR (September 2002). "Ca2+-dependent block of CREB-CBP transcription by repressor DREAM". EMBO J. 21 (17): 4583–92. PMC 126180. PMID 12198160. doi:10.1093/emboj/cdf440. 
  15. ^ a b c Fimia GM, De Cesare D, Sassone-Corsi P (November 2000). "A family of LIM-only transcriptional coactivators: tissue-specific expression and selective activation of CREB and CREM". Mol. Cell. Biol. 20 (22): 8613–22. PMC 102166. PMID 11046156. doi:10.1128/MCB.20.22.8613-8622.2000. 
  16. ^ Gavaravarapu S, Kamine J (March 2000). "Tip60 inhibits activation of CREB protein by protein kinase A". Biochem. Biophys. Res. Commun. 269 (3): 758–66. PMID 10720489. doi:10.1006/bbrc.2000.2358. 
  17. ^ Deak M, Clifton AD, Lucocq LM, Alessi DR (August 1998). "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB". EMBO J. 17 (15): 4426–41. PMC 1170775. PMID 9687510. doi:10.1093/emboj/17.15.4426. 
  18. ^ Wang X, Li W, Williams M, Terada N, Alessi DR, Proud CG (August 2001). "Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase". EMBO J. 20 (16): 4370–9. PMC 125559. PMID 11500364. doi:10.1093/emboj/20.16.4370. 

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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