CREB-binding protein interaction

Gewinner C, Hart G, Zachara N, Cole R, Beisenherz-Huss C, 33. Groner B. The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5. J. Biol. 

Lorentz, O., Suit, E.R., Taylor, J.K., Boudreau, F., Traber, P.G. 1999. CREB-binding protein interacts with the homeodomain protein Cdx2 and enhances transcriptional activity. J. Biol. Chem. 274, 7196-7199. 

Chromatin remodeling, transcription factor modification by various enzyme activities, and the communication between the nuclear receptors and the basal transcription apparatus are accomplished by protein-protein interactions with one or more of a class of coregulator molecules. The number of these coregulator molecules now exceeds 100, not counting species variations and splice variants. The first of these to be described was the CREB-binding protein, CBP. CBP, through an amino terminal domain, binds to phosphorylated serine 137 of CREB and mediates transactivation in response to cAMP. It thus is described as a coactivator. CBP and... 

The detailed mechanisms involved in CREB phosphorylation were first established for the cAMP pathway. A first messenger that increases cAMP concentrations leads to activation of PKA and to translocation of the free catalytic subunit of the protein kinase into the nucleus, where it phosphorylates CREB on serine 133. Such phosphorylation then promotes the binding of CREB to a CREB-binding protein (CBP). CBP, upon binding CREB, interacts directly with the RNA polymerase II complex, which mediates the initiation of transcription. In most cases, such interactions lead to the activation of transcription, although it is possible that the expression of some genes may be repressed. 

Sakaguchi K, Herrera JE, Saito S, Mild T, Bustin M, Vassilev A, Anderson CW, Appella E (1998) DNA damage activates p53 through a phosphorylation-acetylation cascade. Genes Dev 12( 18) 2831-2841 Shikama N, Chan HM, Krstic-Demonacos M, Smith L, Lee CW, Cairns W, La Thangue NB (2000). Functional interaction between nucleosome assembly proteins and p300/CREB-binding protein family coactivators. Mol Cell Biol 20(23) 8933-8943... 

Shikama, N., Chan, H.M., Krstic-Demonacos, M., Smith, L., Lee, C.W., Cairns, W., and La Thangue, N.B. (2000) Functional interaction between nucleosome assembly proteins and p300/ CREB-binding protein family coactivators. Mol. Cell. Biol. 20, 8933-8943. 

Kretsovali, A., Agalioti, T., Spilianakis, C., Tzortzakaki, E., Merika, M., and Papamatheakis, J. (1998) Involvement of CREB binding protein in expression of major histocompatibility complex class II genes via interaction with the class II transactivator. Mol. Cell. Biol. 18(11),... 

Steffan JS, Kazantsev A, Spasic-Boskovic O, Greenwald M, Zhu YZ, Gohler H, et al. The Huntington s disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc Natl Acad Sri USA 2000 97(12) 6763—6768. 

Figure 31.24. Coactivator Structure. The pi60 family of coactivators includes a number of domains that can be recognized at the amino acid sequence level, including a basic helix-loop-helix domain that takes part in DNA binding, a PAS domain that participates in protein-protein interactions, a central domain that contacts the ligandbinding domain of the nuclear hormone receptors, and a domain that interacts with additional coactivators such as p300 and CREB-binding protein (CBP). (CREB stands for cyclic AMP-response element binding protein.) The nuclear hormone receptor interaction domain includes three Leu-X-X-Leu-Leu sequences.

Figure 31.32. Domain Structure of CREB-Binding Protein (CBP). The CREB-binding protein includes at least three types of protein-protein interaction domains in addition to a histone acetyltransferase domain that lies near the carboxyl terminus. The kinase-inducible interaction (KIX) domain interacts specifically with a region of CREB in its phosphorylated form.

Jaber, B.M., Mukopadhyay, R. and Smith, C.L. (2004) Estrogen receptor-a interaction with the CREB binding protein coactivator is regulated by the cellular environment. Journal of Molecular Endocrinology, 32, 307-323. 

Histone acetylase activity has been associated with a number of transcription factors and co-activators. The proteins ACTR (activator of the thyroid and retinoic acid receptor) and SRC-1 (steroid receptor co-activator) are involved in activation of transcription by several ligand-bound nuclear receptors, and both contain histone acetylase activity. TAF250, a component of TFIID, also contains histone acetylase activity, as does the co-activator p300/CBP (CREB binding protein), which interacts with the transcription factor CREB. 

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