Induction-independent Recruitment of CREB-binding Protein to the c-fos Serum Response Element through Interactions between the Bromodomain and Elk-1

Nissen, L. Johan; Gelly, Jean‐Christophe; Hipskind, Robert A.

doi:10.1074/jbc.m007824200

Cited by 51 publications

(49 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The transcriptional activity of Elk-1 is also tightly regulated by protein-protein interactions. The interaction of Elk-1 with the coactivators CBP and/or Sur2 positively impacts Elk-1-mediated transcription events (Janknecht and Nordheim, 1996;Boyer et al, 1999;Nissen et al, 2001;Stevens et al, 2002). On the other hand, the association of Elk-1 with ID-1 and the histone deacetylase mSin3A negatively regulates Elk-1 transcriptional activity Roberts et al, 2001;Yang et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

Akt negatively regulates translation of the ternary complex factor Elk-1

Figueroa

Vojtek

2003

Oncogene

View full text Add to dashboard Cite

Cross-talk between signaling pathways plays an important role in regulation of cell growth, differentiation, survival, and death. Here, we show that Akt regulates the Elk-1 transcription factor, independent of its negative regulation of Raf kinases. Using a constitutively active Mek1 to bypass the regulation of Raf by Akt, we find that the Elk-1 and Sap1a proteins are dramatically decreased in the presence of activated Akt. Akt catalytic activity is required. Also, Mek-dependent activation of a TCF (Elk-1/Sap-1a)-dependent c-fos reporter is decreased by activated Akt. Neither the level of Elk-1 mRNA nor the stability of the Elk-1 protein is altered by activated Akt. Instead, the rate of incorporation of labeled methionine into Elk-1 protein is decreased in the presence of Akt. In addition, the level of the Elk-1 protein but not GFP is significantly decreased in the presence of activated Akt, when GFP is expressed from an IRES element in a bicistronic message with Elk-1. We conclude that Akt negatively regulates translation of the Elk-1 mRNA. A coding region determinant that maps within the first 279 nts of the Elk-1 message is necessary and sufficient for Akt-mediated regulation of Elk-1.

show abstract

Section: Discussionmentioning

confidence: 99%

Akt negatively regulates translation of the ternary complex factor Elk-1

Figueroa

Vojtek

2003

Oncogene

View full text Add to dashboard Cite

show abstract

“…They interact with many transcription factors and coactivators, initially suggesting a structural role in promoter complexes (reviewed in ref. 28); p300 and CBP have been localized to c-fos and c-jun by ChIP (18,29) and through interactions with other proteins (30)(31)(32). A purely structural role was challenged following discovery of their acetyltransferase activity (33,34) with the catalytic domain required for transcription from chromatinized promoter constructs in vitro and in vivo (35,36).…”

Section: Discussionmentioning

confidence: 99%

Dynamic acetylation of all lysine-4 trimethylated histone H3 is evolutionarily conserved and mediated by p300/CBP

Crump

Hazzalin

Bowers

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

111

View full text Add to dashboard Cite

Histone modifications are reported to show different behaviors, associations, and functions in different genomic niches and organisms. We show here that rapid, continuous turnover of acetylation specifically targeted to all K4-trimethylated H3 tails (H3K4me3), but not to bulk histone H3 or H3 carrying other methylated lysines, is a common uniform characteristic of chromatin biology in higher eukaryotes, being precisely conserved in human, mouse, and Drosophila. Furthermore, dynamic acetylation targeted to H3K4me3 is mediated by the same lysine acetyltransferase, p300/cAMP response element binding (CREB)-binding protein (CBP), in both mouse and fly cells. RNA interference or chemical inhibition of p300/CBP using a newly discovered small molecule inhibitor, C646, blocks dynamic acetylation of H3K4me3 globally in mouse and fly cells, and locally across the promoter and start-site of inducible genes in the mouse, thereby disrupting RNA polymerase II association and the activation of these genes. Thus, rapid dynamic acetylation of all H3K4me3 mediated by p300/CBP is a general, evolutionarily conserved phenomenon playing an essential role in the induction of immediate-early (IE) genes. These studies indicate a more global function of p300/CBP in mediating rapid turnover of acetylation of all H3K4me3 across the nuclei of higher eukaryotes, rather than a tight promoter-restricted function targeted by complex formation with specific transcription factors.histone acetylation turnover | Trichostatin A | p300/CBP inhibitor

show abstract

“…Mutation of serine residues 63 and 73 in c-jun reduced CBP binding and transactivation in vitro (3). Phosphorylation of a number of ets family members has been shown to increase CBP/p300 recruitment (10,16,20,27,30). We previously demonstrated that phosphorylation of the AP-1 protein c-jun is a potent activator of MMP-9 expression, suggesting a novel mechanism by which this modification may recruit coactivator proteins (8).…”

mentioning

confidence: 99%

Extracellular Signals Regulate Rapid Coactivator Recruitment at AP-1 Sites by Altered Phosphorylation of both CREB Binding Protein and c-jun

Tsai

Salib

et al. 2008

Molecular and Cellular Biology

View full text Add to dashboard Cite

Retinoic acid (RA) inhibits matrix metalloproteinase 9 (MMP-9) expression due to AP-1 inhibition resulting from retinoic acid receptors (RARs) competing for limiting amounts of coactivator proteins. However, given the rapid kinetics of MMP-9 transcription, it seems unlikely that these interactions can be explained passively. Our previous studies indicated that coactivator and transcription factor phosphorylation may allow for rapid regulation of MMP-9 expression. In the present study we tested this hypothesis directly. CREB binding protein (CBP) and p300/CBP-associated factor (PCAF) were displaced from transcription factor binding sites on the MMP-9 promoter within minutes of RA treatment. The RAR interaction domains of CBP and PCAF were not required for this displacement. RA and epidermal growth factor had opposing effects on phosphorylation of CBP by extracellular signal-regulated kinase 1 that correlated with altered CBP occupancy of AP-1 sites and differential MMP-9 promoter activation. We identified a novel phosphorylation site in the CBP carboxyl terminus that mediated association with AP-1 sites in the MMP-9 promoter. Inhibition of c-jun phosphorylation displaced PCAF from AP-1 sites and reduced promoter activity. Phosphorylation deficient c-jun was less able to recruit PCAF to AP-1 sites. We also demonstrated novel interactions between coactivators and AP-1 proteins. We propose that extracellular signal-mediated coactivator exchange at AP-1 sites is mediated via protein kinase pathways.

show abstract

Induction-independent Recruitment of CREB-binding Protein to the c-fos Serum Response Element through Interactions between the Bromodomain and Elk-1

Cited by 51 publications

References 37 publications

Akt negatively regulates translation of the ternary complex factor Elk-1

Akt negatively regulates translation of the ternary complex factor Elk-1

Dynamic acetylation of all lysine-4 trimethylated histone H3 is evolutionarily conserved and mediated by p300/CBP

Extracellular Signals Regulate Rapid Coactivator Recruitment at AP-1 Sites by Altered Phosphorylation of both CREB Binding Protein and c-jun

Contact Info

Product

Resources

About