Akt Phosphorylation of p300 at Ser-1834 Is Essential for Its Histone Acetyltransferase and Transcriptional Activity

Huang, Wei-Chien; Chen, Ching-Chow

doi:10.1128/mcb.25.15.6592-6602.2005

Cited by 250 publications

(257 citation statements)

References 51 publications

(59 reference statements)

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“…Growth factors also phosphorylated CBP via the MAPK pathway in the amino terminus of the coactivator (12,22,38). Recently, a separate p300 phosphorylation site at Ser1834 was shown to be a target of Akt induction of the ICAM-1 promoter (14). Transcription factor phosphorylation has also been shown to regulate coactivator binding.…”

Section: Discussionmentioning

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

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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.

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Section: Discussionmentioning

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

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“…Binding of transcription factors to the iNOS promoter DNA sequences was assayed, as described (25). Following exposure to US, nuclear extracts were prepared.…”

Section: Methodsmentioning

confidence: 99%

Ultrasound Induces Hypoxia-inducible Factor-1 Activation and Inducible Nitric-oxide Synthase Expression through the Integrin/Integrin-linked Kinase/Akt/Mammalian Target of Rapamycin Pathway in Osteoblasts

Tang

Tan

et al. 2007

Journal of Biological Chemistry

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It has been shown that ultrasound (US) stimulation accelerates fracture healing in the animal models and clinical studies. Nitric oxide (NO) is a crucial early mediator in mechanically induced bone formation. Here we found that US stimulation increased NO formation and the protein level of inducible nitric-oxide synthase (iNOS). US-mediated iNOS expression was attenuated by anti-integrinFracture healing is a complex physiological process comprising the coordinated participation of several cell types. Among all the means to influence fracture healing, ultrasound (US) 3 distinguishes itself by being non-invasive and easy to apply. Low intensity levels are used to accelerate fracture healing and are considered neither thermal nor destructive. It has been shown that low intensity US accelerates fracture healing in animal models (1, 2) and clinical studies (3, 4). It has been demonstrated that low intensity-pulsed US exposure increases nitric oxide (NO) and prostaglandin release (5, 6), stimulates collagen synthesis, and promotes bone formation (7). However, the mechanisms involved in osteoblasts to detect US stress and transduce the signal across the membrane for activating signaling pathways in metabolism, such as the induction of inducible nitric-oxide synthase (iNOS) and release of NO, remain poorly understood.Integrins are cell-surface adhesion receptors that regulate cell viability in response to cues derived from the extracellular matrix (8, 9). In the case of mesenchymal cells, encompassed by the extracellular matrix, matrix-derived mechanical stimuli can regulate their viability. In this latter scenario, integrins function as mechanoreceptors that detect mechanical stimuli originating from the extracellular matrix and convert them to chemical signaling pathways that regulate cell viability (10, 11). Mechanical stimuli can be transmitted through the direct or indirect interaction of integrins with associated lipid or protein-signaling molecules in the focal adhesion complex (12, 13). Integrinlinked kinase (ILK), a potential candidate signaling molecule, has been shown to be capable of regulating integrin-mediated signaling (14). ILK can interact with the cytoplasmic domain of ␤-integrin subunits and is activated by both integrin activation as well as growth factors and is an upstream regulator of Akt (15).Hypoxia-inducible factor-1 (HIF-1) is a heterodimeric transcription factor composed of the basic helix-loop-helix-PerArnt-Sim-domain, containing the proteins HIF-1␣ and arylhydrocarbon receptor nuclear translocator (HIF-1␤) (16). The availability of HIF-1 is determined primarily by HIF-1␣, which is regulated at the protein level in an oxygen-sensitive manner, in contrast to HIF-1␤, which is stably expressed (17,18). During normoxia, HIF-1␣ is efficiently degraded through the von HippelLindau-dependent ubiquitin-proteasome pathway (18). Under * This work was supported by the National Science Council of Taiwan (Grant NSC 95-2314-B-039-045) and China Medical University . The costs of publication of this arti...

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“…For this reason we determined whether p300 was associated with SV40 chromosomes. For this analysis we utilized antibody from Santa Cruz Biotechnology which has been successfully utilized for ChIP analysis previously (27) . Specificity of the p300 antibody for its epitope is shown in the Supplementary Data (SF11).…”

Section: Organization Of P300 On Transcribing Sv40 Chromosomesmentioning

confidence: 99%

Histone Hyperacetylation in the Coding Region of Chromatin Undergoing Transcription in SV40 Minichromosomes Is a Dynamic Process Regulated Directly by the Presence of RNA Polymerase II

Balakrishnan

Milavetz

2007

Journal of Molecular Biology

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SV40 chromosomes undergoing transcription operationally defined by the presence of RNA Polymerase II (RNAPII) were immune-selected with antibody to RNAPII and subjected to secondary chromatin immunoprecipitation with antibodies to hyperacetylated or unacetylated H4 or H3. Immune Selection Fragmentation and Immunoprecipitation (ISFIP) was used to determine the hyperacetylation status of histones independent of the location of the RNAPII and ReChromatin Immunoprecipitation (ReChIP) was used to determine their hyperacetylation status when associated with RNAPII. While hyperacetylated H4 and H3 were found in the coding regions regardless of the location of RNAPII, unacetylated H4 and H3 were only found at sites lacking RNAPII. The absence of unacetylated H4 and H3 at sites containing RNAPII was correlated with the specific association of the Histone Acetyl Transferase (HAT) p300 with the RNAPII. In contrast, the presence of unacetylated H4 and H3 at sites lacking RNAPII was shown to result from the action of a histone deacetylase (HDAC) based upon the effects of the inhibitor sodium butyrate. These results suggest that the extent of hyperacetylation of H4 and H3 during transcription alternates between hyperacetylation directed by an RNAPII associated HAT and deacetylation directed by an HDAC at other sites.

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Akt Phosphorylation of p300 at Ser-1834 Is Essential for Its Histone Acetyltransferase and Transcriptional Activity

Cited by 250 publications

References 51 publications

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

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

Ultrasound Induces Hypoxia-inducible Factor-1 Activation and Inducible Nitric-oxide Synthase Expression through the Integrin/Integrin-linked Kinase/Akt/Mammalian Target of Rapamycin Pathway in Osteoblasts

Histone Hyperacetylation in the Coding Region of Chromatin Undergoing Transcription in SV40 Minichromosomes Is a Dynamic Process Regulated Directly by the Presence of RNA Polymerase II

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