The cooperation of B-Myb with the coactivator p300 is orchestrated by cyclins A and D1

Schubert, Stephan; Horstmann, Sebastian; Bartusel, Thorsten; Klempnauer, Karl‐Heinz

doi:10.1038/sj.onc.1207255

Cited by 28 publications

(34 citation statements)

References 69 publications

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“…This raises the interesting possibility that during RTK signaling, c-Myb functions in H3 positioning, acetylation, or both might be transiently altered, reflecting a constitutive function of v-Myb. One possibility is that such Myb-target genes do not depend on Myb binding to cis-regulatory sites on DNA but on interactions between Myb and other transcription factors that transmit Myb functions unrelated to H3 tail acetylation (Schubert et al 2004). Yet another possibility is that critical activities of Myb in proliferation might still require distinct Myb functions, such as p300 binding, but that these functions are nontranscriptional; such as, for example, during DNA replication (Beall et al 2002).…”

Section: Gain and Loss Of Functions Of V-mybmentioning

confidence: 99%

Histone H3 tail positioning and acetylation by the c-Myb but not the v-Myb DNA-binding SANT domain

Kowenz‐Leutz²,

Laumonnier³

et al. 2005

Genes Dev.

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Section: Gain and Loss Of Functions Of V-mybmentioning

confidence: 99%

Histone H3 tail positioning and acetylation by the c-Myb but not the v-Myb DNA-binding SANT domain

Kowenz‐Leutz²,

Laumonnier³

et al. 2005

Genes Dev.

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“…The column was washed with equilibration buffer and the bound protein was eluted using the same buffer supplemented with 2.5 mmol/L desthiobiotin. The protein was concentrated using centrifugal filter tubes (Merck Millipore, exclusion size 30 kDa) and stored at À80 C. To purify bacterial protein containing the KIX domain, a GST-p300 fusion protein (amino acids 1 to 672) was expressed using the plasmid pGex-p300#1 (35), as described previously (36). A construct encoding a GST-human CBP fusion protein (amino acids 1 to 692), pGex-CBP(1-692), was generated by PCR amplification of the corresponding part of human CBP and cloning into pGex-6P2.…”

Section: Expression and Purification Of Bacterial Proteinsmentioning

confidence: 99%

Naphthol AS-E Phosphate Inhibits the Activity of the Transcription Factor Myb by Blocking the Interaction with the KIX Domain of the Coactivator p300

Uttarkar

Dukare

Bopp

et al. 2015

Molecular Cancer Therapeutics

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The transcription factor c-Myb is highly expressed in hematopoietic progenitor cells and controls the transcription of genes important for lineage determination, cell proliferation, and differentiation. Deregulation of c-Myb has been implicated in the development of leukemia and certain other types of human cancer. c-Myb activity is highly dependent on the interaction of the c-Myb with the KIX domain of the coactivator p300, making the disruption of this interaction a reasonable strategy for the development of Myb inhibitors. Here, we have used bacterial Autodisplay to develop an in vitro binding assay that mimics the interaction of Myb and the KIX domain of p300. We have used this binding assay to investigate the potential of Naphthol AS-E phosphate, a compound known to bind to the KIX domain, to disrupt the interaction between Myb and p300. Our data show that Naphthol AS-E phosphate interferes with the Myb-KIX interaction in vitro and inhibits Myb activity in vivo. By using several human leukemia cell lines, we demonstrate that Naphthol AS-E phosphate suppresses the expression of Myb target genes and induces myeloid differentiation and apoptosis. Our work identifies Naphthol AS-E phosphate as the first low molecular weight compound that inhibits Myb activity by disrupting its interaction with p300, and suggests that inhibition of the Myb-KIX interaction might be a useful strategy for the treatment of leukemia and other tumors caused by deregulated c-Myb.

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“…GST fusion proteins were expressed and purified as described. 32 To detect GST-Pdcd4 by Western blotting, a Pdcd4 antiserum reacting with the C-terminus of human Pdcd4 (Acris, Herford, Germany) was used.…”

Section: Eukaryotic Expression Vectorsmentioning

confidence: 99%

Association of Tumor Suppressor Protein Pdcd4 With Ribosomes Is Mediated by Protein-Protein and Protein-RNA Interactions

et al. 2010

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The Pdcd4 (programmed cell death gene 4) gene has been implicated as a novel tumor suppressor gene in the development of several types of human cancer. The Pdcd4 protein is believed to act as a translation suppressor of mRNAs containing structured 5′ UTRs. Pdcd4 contains 2 copies of so-called MA3 domains that mediate tight interactions with the translation initiation factor eIF4A, resulting in the inhibition of the eIF4A helicase activity. The N-terminal part of Pdcd4, which has been less well characterized, binds RNA in vitro, but as yet, it has not been clear whether RNA binding by Pdcd4 plays a role in vivo. Here, the authors have identified 2 highly conserved clusters of basic amino acid residues that are essential for the RNA binding activity of Pdcd4. They also show that a substantial fraction of Pdcd4 is present, together with small ribosomal subunits, in translation preinitiation complexes. Using mutants that disrupt RNA binding or the Pdcd4-eIF4A interaction, they demonstrate that the ribosomal association of Pdcd4 is dependent on its RNA binding activity as well as on its ability to interact with eIF4A. Their work provides the first direct evidence for an essential role of the Pdcd4 RNA binding activity in vivo and suggests that RNA binding is required for recruiting Pdcd4 to the translation machinery.

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The cooperation of B-Myb with the coactivator p300 is orchestrated by cyclins A and D1

Cited by 28 publications

References 69 publications

Histone H3 tail positioning and acetylation by the c-Myb but not the v-Myb DNA-binding SANT domain

Histone H3 tail positioning and acetylation by the c-Myb but not the v-Myb DNA-binding SANT domain

Naphthol AS-E Phosphate Inhibits the Activity of the Transcription Factor Myb by Blocking the Interaction with the KIX Domain of the Coactivator p300

Association of Tumor Suppressor Protein Pdcd4 With Ribosomes Is Mediated by Protein-Protein and Protein-RNA Interactions

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