The c‐myc Promoter: Still MysterY and Challenge

Wierstra, Inken; Alves, Jürgen

doi:10.1016/s0065-230x(07)99004-1

Cited by 186 publications

(224 citation statements)

References 1,147 publications

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“…Deregulation of c-myc expression is tumorigenic, promoting genomic instability (Chung and Levens, 2005;Wierstra and Alves, 2008), and thus a tight control is essential in cells. FBPs regulate c-myc transcription through the general transcription factor, TFIIH (Wierstra and Alves, 2008). In this study, we examine the possibility that FBP-1 is a valid caspase substrate.…”

Section: Discussionmentioning

confidence: 99%

“…However, even slight fluctuations in these amounts have dramatic consequences on cell fate. Therefore, c-myc evidently requires tight control and represents a promising target of anticancer therapy (Liu et al, 2007;Wierstra and Alves, 2008).…”

Section: Introductionmentioning

confidence: 99%

“…FBP proteins comprise three domains: an NH 2 -terminal domain containing one classical nuclear localization signal sequence, a central domain constituting four regularly spaced K-homology motifs and a COOH-terminal domain containing two to four repeats of a tyrosine-rich motif (Chung and Levens, 2005). FBP binds through its four K-homology domains to FUSE of the c-myc promoter, leading to the upregulation of the c-Myc level (Wierstra and Alves, 2008). FBP expression patterns are parallel to those of c-Myc.…”

Section: Introductionmentioning

confidence: 99%

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Far upstream element-binding protein-1, a novel caspase substrate, acts as a cross-talker between apoptosis and the c-myc oncogene

et al. 2009

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Far upstream element-binding protein-1 (FBP-1) binds to an upstream element of the c-myc promoter and regulates the c-myc mRNA level. Earlier, FBP-1 was identified as a candidate substrate of caspase-7. Here, we report that FBP-1 is cleaved by executor caspases, both in vitro and during apoptosis. Cleavage occurs at the caspase consensus site (DQPD 74 ) located within the classical bipartite nuclear localization signal sequence. In cells subjected to apoptotic stimuli, the caspase-mediated cleavage of FBP-1 leads to its decreased presence in the nucleus, concomitant with the marked downregulation of c-Myc and its various target proteins. By contrast, cells transfected with a non-cleavable mutant of FBP-1 (D74A) maintain higher levels of c-Myc and are protected from apoptosis. On the basis of these results, we suggest that the oncogenic potential of c-Myc is 'switched off' after apoptosis induction as a consequence of the caspasemediated cleavage of FBP-1.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Far upstream element-binding protein-1, a novel caspase substrate, acts as a cross-talker between apoptosis and the c-myc oncogene

et al. 2009

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“…Baicalin (chemical structural formula: C21H18O11) is an active ingredient extracted from Scutellaria (Labiatae). Many studies have shown that baicalin can play an anti-tumor role through various means (Hoffman and Liebermann, 2008;Wierstra and Alves, 2008;Zhang et al, 2009). For example, the promotional effect of prostaglandin synthetase on tumor cells can be blocked by reducing cyclooxygenase-2 expression to inhibit prostaglandin E2 production.…”

Section: Introductionmentioning

confidence: 99%

Baicalin Induces Apoptosis in Leukemia HL-60/ADR Cells via Possible Down-regulation of the PI3K/Akt Signaling Pathway

Zheng

Hu²,

Chen³

et al. 2012

Asian Pacific Journal of Cancer Prevention

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“…In fact, deregulated c-myc gene expression due to shifting to an alternative first exon/promoter that harbors less efficient transcription elongation block may be related to the oncogenesis of Burkitt lymphoma (44). Overproduction of aromatase, a key enzyme in estrogen biosynthesis, occurs in the surrounding tissues of breast tumors due to transcriptional activation caused by switching from a weak physiological promoter to a strong promoter (45).…”

Section: Discussionmentioning

confidence: 99%

Loss of the Gata1 Gene IE Exon Leads to Variant Transcript Expression and the Production of a GATA1 Protein Lacking the N-terminal Domain

Kobayashi

Shimizu

Kikuchi

et al. 2010

Journal of Biological Chemistry

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GATA1 is essential for the differentiation of erythroid cells and megakaryocytes. The Gata1 gene is composed of multiple untranslated first exons and five common coding exons. The erythroid first exon (IE exon) is important for Gata1 gene expression in hematopoietic lineages. Because previous IE exon knockdown analyses resulted in embryonic lethality, less is understood about the contribution of the IE exon to adult hematopoiesis. Here, we achieved specific deletion of the floxed IE exon in adulthood using an inducible Cre expression system. In this conditional knock-out mouse line, the Gata1 mRNA level was significantly down-regulated in the megakaryocyte lineage, resulting in thrombocytopenia with a marked proliferation of megakaryocytes. By contrast, in the erythroid lineage, Gata1 mRNA was expressed abundantly utilizing alternative first exons. Especially, the IEb/c and newly identified IEd exons were transcribed at a level comparable with that of the IE exon in control mice. Surprisingly, in the IE-null mouse, these transcripts failed to produce full-length GATA1 protein, but instead yielded GATA1 lacking the N-terminal domain inefficiently. With low level expression of the short form of GATA1, IE-null mice showed severe anemia with skewed erythroid maturation. Notably, the hematological phenotypes of adult IE-null mice substantially differ from those observed in mice harboring conditional ablation of the entire Gata1 gene. The present study demonstrates that the IE exon is instrumental to adult erythropoiesis by regulating the proper level of transcription and selecting the correct transcription start site of the Gata1 gene.

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The c‐myc Promoter: Still MysterY and Challenge

Cited by 186 publications

References 1,147 publications

Far upstream element-binding protein-1, a novel caspase substrate, acts as a cross-talker between apoptosis and the c-myc oncogene

Far upstream element-binding protein-1, a novel caspase substrate, acts as a cross-talker between apoptosis and the c-myc oncogene

Baicalin Induces Apoptosis in Leukemia HL-60/ADR Cells via Possible Down-regulation of the PI3K/Akt Signaling Pathway

Loss of the Gata1 Gene IE Exon Leads to Variant Transcript Expression and the Production of a GATA1 Protein Lacking the N-terminal Domain

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