E1A-mediated inhibition of myogenesis correlates with a direct physical interaction of E1A12S and basic helix-loop-helix proteins.

Taylor, Doris A.; Kraus, Virginia B.; Schwarz, John J.; Olson, Eric N.; Kraus, William E.

doi:10.1128/mcb.13.8.4714

Cited by 51 publications

(39 citation statements)

References 61 publications

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“…These include the TATA-box binding protein TBP (Song et al, 1995), Dr1, a transcriptional repressor (Kraus et al, 1994), YY1, a multifunctional transcription factor (Lewis et al, 1995), the bHLH protein myogenin (Taylor et al, 1993), and a factor necessary for cardiac myocyte-speci®c gene expression (Bishopric et al, 1997).…”

Section: Expression Of Prb Is Necessary But Not Sufficient To Restorementioning

confidence: 99%

The retinoblastoma gene family members pRB and p107 coactivate the AP-1-dependent mouse tissue factor promoter in fibroblasts

et al. 2000

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Serum-stimulation of quiescent mouse ®broblasts results in transcriptional activation of tissue factor (TF), the cellular initiator of blood coagulation. This requires the rapid entry of c-Fos into speci®c AP-1 DNA-binding complexes and can be strongly inhibited by the adenovirus E1A 12S gene product. In this study, we utilized a panel of E1A mutants de®cient in cellular protein binding to analyse the molecular basis for E1A inhibition of a minimal, c-Fos-dependent TF promoter/ reporter construct in mouse AKR-2B ®broblasts. Mutations which impaired binding of the retinoblastoma tumor suppressor protein family members pRB, p107, and p130 relieved E1A-mediated inhibition of transcription in response to serum-stimulation or c-Fos overexpression. Inhibition was restricted to the G 0 to G 1 transition, consistent with the speci®city of E1A for hypophosphorylated forms of RB proteins. Although E1A mutants de®cient in CBP/p300 binding retained the ability to inhibit TF transcription, deletion of the aminoterminal portion of the CBP/p300 interaction domain was required to permit rescue of TF promoter activity by coexpression of pRB. Moreover, ectopic p107 could e ectively substitute for pRB in relieving E1A-mediated repression. In primary mouse embryo ®broblasts, activity of the minimal AP-1-dependent TF promoter was suppressed in Rb 7/7 cells compared to parallel Rb +/7 and Rb +/+ transfectants. Ectopic expression of either pRB or p107 markedly enhanced TF promoter activity in Rb 7/7 ®broblasts. Collectively, these data imply that pRB and p107 can cooperate with c-Fos to activate TF gene transcription in ®broblasts and suggest a requirement for another, as yet unidenti®ed, E1A-binding protein. Oncogene (2000) 19, 3352 ± 3362.

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Section: Expression Of Prb Is Necessary But Not Sufficient To Restorementioning

confidence: 99%

The retinoblastoma gene family members pRB and p107 coactivate the AP-1-dependent mouse tissue factor promoter in fibroblasts

et al. 2000

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“…The expression vector, phIIB, obtained from D. Reinberg, was similarly used to obtain TFIIB, which was purified using phosphocellulose chromatography (46). The GST-E1A (13 S; 289 amino acid residues) fusion protein was expressed in BL21 cells containing the pGEX-E1A (obtained from T. Shenk) and was purified by binding to glutathione agarose, elution by glutathione, followed by dialysis into reaction buffer (47). All proteins were greater than 80% pure as evidenced by Coomassie staining of gels run on SDS-polyacrylamide gel electrophoresis.…”

Section: Methodsmentioning

confidence: 99%

Influence of HMG-1 and Adenovirus Oncoprotein E1A on Early Stages of Transcriptional Preinitiation Complex Assembly

Lü

Peterson

Dasgupta

et al. 2000

Journal of Biological Chemistry

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The TATA-binding protein (TBP) in the TFIID complex binds specifically to the TATA-box to initiate the stepwise assembly of the preinitiation complex (PIC) for RNA polymerase II transcription. Transcriptional activators and repressors compete with general transcription factors at each step to influence the course of the assembly. To investigate this process, the TBP⅐TATA complex was titrated with HMG-1 and the interaction monitored by electrophoretic mobility shift assays. The titration produced a ternary HMG-1⅐TBP⅐TATA complex, which exhibits increased mobility relative to the TBP⅐TATA complex. The addition of increasing levels of TFIIB to this complex results in the formation of the TFIIB⅐TBP⅐TATA complex. However, in the reverse titration, with very high mole ratios of HMG-1 present, TFIIB is not dissociated off and a complex is formed that contains all factors. The simultaneous addition of E1A to a mixture of TBP and TATA; or HMG-1, TBP, and TATA; or TFIIB, TBP, and TATA inhibits complex formation. On the other hand, E1A added to the pre-established complexes shows a significantly reduced capability to disrupt the complex. In add-back experiments with all complexes, increased levels of TBP re-established the complexes, indicating that the primary target for E1A in all complexes is TBP.

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“…Because E boxes bind proteins containing a bHLH domain, the E2-binding protein likely belongs to this family. Inhibitory bHLH proteins that compete with MyoD for DNA binding have been described and include MyoR (35), Mist1 (36), the mouse snail-related gene, Smuc (37), and the E1A͞E12 heterodimer (38). (22).…”

Section: Protein Binding To E2 In the Absence Of Myod Requires Usf Bomentioning

confidence: 99%

Muscle-regulated expression and determinants for neuromuscular junctional localization of the mouse RIα regulatory subunit of cAMP- dependent protein kinase

Barradeau

Imaizumi-Scherrer

Weiss

et al. 2001

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

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In skeletal muscle, transcription of the gene encoding the mouse type I␣ (RI␣) subunit of the cAMP-dependent protein kinase is initiated from the alternative noncoding first exons 1a and 1b. Here, we report that activity of the promoter upstream of exon 1a (Pa) depends on two adjacent E boxes (E1 and E2) in NIH 3T3-transfected fibroblasts as well as in intact muscle. Both basal activity and MyoD transactivation of the Pa promoter require binding of the upstream stimulating factors (USF) to E1. E2 binds either an unknown protein in a USF͞E1 complex-dependent manner or MyoD. Both E2-bound proteins seem to function as repressors, but with different strengths, of the USF transactivation potential. Previous work has shown localization of the RI␣ protein at the neuromuscular junction. Using DNA injection into muscle of plasmids encoding segments of RI␣ or RII␣ fused to green fluorescent protein, we demonstrate that anchoring at the neuromuscular junction is specific to RI␣ subunits and requires the amino-terminal residues 1-81. Mutagenesis of Phe-54 to Ala in the full-length RI␣-green fluorescent protein template abolishes localization, indicating that dimerization of RI␣ is essential for anchoring. Moreover, two other hydrophobic residues, Val-22 and Ile-27, are crucial for localization of RI␣ at the neuromuscular junction. These amino acids are involved in the interaction of the Caenorhabditis elegans type I␣ homologue RCE with AKAPCE and for in vitro binding of RI␣ to dual A-kinase anchoring protein 1. We also show enrichment of dual A-kinase anchoring protein 1 at the neuromuscular junction, suggesting that it could be responsible for RI␣ tethering at this site.S ubcellular localization is a crucial mechanism to achieve optimal activation and substrate specificity of the cAMPdependent protein kinase (PKA, EC 2.7.1.37). PKA type II targeting to subcellular structures and organelles or assembly in signaling complexes is a result of tethering of RII regulatory (R) subunits by members of the A-kinase anchoring protein (AKAP) family, a group of structurally divergent proteins possessing a conserved RII-binding site (1, 2).Although a large proportion of type I␣ R subunit (RI␣) is dispersed in the cytosol, it also is associated with the plasma membrane of human erythrocytes (3), recruited to the ''cap site'' of activated T lymphocytes (4) and sequestered along the fibrous sheath of mammalian spermatozoa (5). In addition, we have demonstrated previously the accumulation of RI␣ at the neuromuscular junction (NMJ) of skeletal muscle (6) and its association with microtubules (7). The high affinity RII-binding sites of certain AKAPs, named dual (D)-AKAPs, also sequester RI␣ in vitro but with a 25-500 lower affinity (8, 9). Thus, type I PKA also could be anchored in intact cells through specific AKAP-RI␣ interactions. In fact, Angelo and Rubin (10) have identified AKAP CE from Caenorhabditis elegans, which binds the R CE subunit. Because R CE is closely related to mammalian RI␣, AKAP CE is the first eukaryotic RI-specific teth...

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E1A-mediated inhibition of myogenesis correlates with a direct physical interaction of E1A12S and basic helix-loop-helix proteins.

Cited by 51 publications

References 61 publications

The retinoblastoma gene family members pRB and p107 coactivate the AP-1-dependent mouse tissue factor promoter in fibroblasts

The retinoblastoma gene family members pRB and p107 coactivate the AP-1-dependent mouse tissue factor promoter in fibroblasts

Influence of HMG-1 and Adenovirus Oncoprotein E1A on Early Stages of Transcriptional Preinitiation Complex Assembly

Muscle-regulated expression and determinants for neuromuscular junctional localization of the mouse RIα regulatory subunit of cAMP- dependent protein kinase

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