Stimulation of c‐MYC transcriptional activity and acetylation by recruitment of the cofactor CBP

Vervoorts, Jörg; Lüscher-Firzlaff, Juliane; Rottmann, Sabine; Lilischkis, Richard; Walsemann, Gesa; Dohmann, Karen; Austen, Matthias; Lüscher, Bernhard

doi:10.1038/sj.embor.embor821

Cited by 237 publications

(221 citation statements)

References 38 publications

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“…It is unknown if Sam68 acetylation contributes in any way to the tumor cell phenotype. Increased acetylation of other proteins such as Rb and Myc is thought to contribute to cell proliferation by stimulating gene expression (Chan et al, 2001;Vervoorts et al, 2003). Although the true biological relevance of Sam68 acetylation in the tumor cell lines remains to be determined, we observed a positive correlation between acetylation and the ability to bind poly(U) RNA (Figure 3).…”

Section: Discussionsupporting

confidence: 51%

The RNA binding protein Sam68 is acetylated in tumor cell lines, and its acetylation correlates with enhanced RNA binding activity

2004

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Section: Discussionsupporting

confidence: 51%

The RNA binding protein Sam68 is acetylated in tumor cell lines, and its acetylation correlates with enhanced RNA binding activity

2004

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“…6C). We also measured c-Myc-dependent transcriptional activity using a c-Myc-sensitive luciferase reporter vector (33). In agreement with the inhibition of c-Myc protein expression observed in RhoE-induced cells, RhoE similarly reduced c-Myc function (Fig.…”

Section: Rhoe Does Not Alter the Dynamics Of Mtor/raptorsupporting

confidence: 50%

RhoE Inhibits 4E-BP1 Phosphorylation and eIF4E Function Impairing Cap-dependent Translation

Villalonga

Mattos

Ridley

2009

Journal of Biological Chemistry

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The Rho GTPase family member RhoE inhibits RhoA/ROCK signaling to promote actin stress fiber and focal adhesion disassembly. We have previously reported that RhoE also inhibits cell cycle progression and Ras-induced transformation, specifically preventing cyclin D1 translation. Here we investigate the molecular mechanisms underlying those observations. RhoE inhibits the phosphorylation of the translational repressor 4E-BP1 in response to extracellular stimuli. However, RhoE does not affect the activation of mTOR, the major kinase regulating 4E-BP1 phosphorylation, as indicated by the phosphorylation levels of the mTOR substrate S6K, the dynamics of mTOR/Raptor association, and the observation that RhoE, as opposed to rapamycin, does not impair cellular growth. Interestingly, RhoE prevents the release of the eukaryotic initiation factor eIF4E from 4E-BP1, inhibiting cap-dependent translation. Accordingly, RhoE also inhibits the expression and the transcriptional activity of the eIF4E target c-Myc. Consistent with its crucial role in cell proliferation, we show that eIF4E can rescue both cell cycle progression and Ras-induced transformation in RhoE-expressing cells, indicating that the inhibition of eIF4E function is critical to mediate the anti-proliferative effects of RhoE.Rnd proteins (Rnd1, Rnd2, and RhoE/Rnd3) constitute a separate subfamily within the Rho family of small GTPases that have attracted recent attention because of their atypical features (1). Despite their high level of sequence similarity with RhoA, -B, and -C, Rnd proteins are remarkably different at both biochemical and functional levels. For instance, Rnd proteins do not cycle between an active form and an inactive form. Instead, they are thought to be constitutively GTP bound because of their extremely low GTPase activity and their increased affinity for GTP over GDP. Moreover, both Rnd1 and RhoE/Rnd3 induce opposite effects to those induced by RhoA on the actin cytoskeleton, promoting the disassembly of actin stress fibers and the loss of focal adhesions (2, 3).

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“…Myc/Max complexes isolated from F-buffer extracts are capable to bind to DNA and the interaction with the coactivators CBP/p300 is preserved (Sommer et al, 1998;Vervoorts et al, 2003). The monoclonal antibody (mAb) 6A10, which recognizes an N-terminal epitope in c-Myc (Sommer et al, 1998), and the Mad1-specific mAb 5C9 for control (Sommer et al, 1997) were covalently linked to Affi-gel 10 and used for immunopurifications.…”

Section: Identification Of Novel Myc-associated Proteinsmentioning

confidence: 99%

“…The N-terminal transactivation domain of c-Myc interacts with TRRAP, a large protein that functions in complexes containing histone acetyltransferases (HATs) like GCN5 and TIP60 (McMahon et al, 2000;Park et al, 2001;Frank et al, 2003). The coactivator CBP/p300 represents a third HAT that, however, binds to a C-terminal region of c-Myc (Vervoorts et al, 2003). These HAT enzymes function at least in part by acetylating core histones, a mechanism that has been linked to chromatin opening and gene activation (Sterner and Berger, 2000;Strahl and Allis, 2000;Jenuwein and Allis, 2001).…”

Section: Introductionmentioning

confidence: 99%

PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation

et al. 2005

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Stimulation of c‐MYC transcriptional activity and acetylation by recruitment of the cofactor CBP

Cited by 237 publications

References 38 publications

The RNA binding protein Sam68 is acetylated in tumor cell lines, and its acetylation correlates with enhanced RNA binding activity

The RNA binding protein Sam68 is acetylated in tumor cell lines, and its acetylation correlates with enhanced RNA binding activity

RhoE Inhibits 4E-BP1 Phosphorylation and eIF4E Function Impairing Cap-dependent Translation

PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation

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