βTrCP regulates BMI1 protein turnover via ubiquitination and degradation

Sahasrabuddhe, Anagh A.; Dimri, Manjari; Bommi, Prashant V.; Dimri, Goberdhan P.

doi:10.4161/cc.10.8.15372

Cited by 46 publications

(47 citation statements)

References 39 publications

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“…As shown in Fig. 8B,C, the mRNA and protein levels of Bmi1 are not well correlated, suggesting that post-transcriptional regulation may also contribute to Bmi1 deregulation in cancer cells [45][46][47]. It has been reported that Bmi1 expression can be suppressed by microRNAs, such as miR-15a, miR-16, miR-128, miR-200c, miR-203, and miR-194, in various carcinomas, suggesting that the expression level of Bmi1 may be regulated in multiple ways [48][49][50][51].…”

Section: Discussionmentioning

confidence: 99%

Sp1 and c‐Myc regulate transcription of BMI1 in nasopharyngeal carcinoma

et al. 2013

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B-lymphoma mouse Moloney leukemia virus insertion region 1 (Bmi1), a member of the polycomb group, has elevated expression and is involved in the pathogenesis of various aggressive cancers, including nasopharyngeal carcinoma (NPC). To date, the mechanisms underlying the high expression of Bmi1 in NPC remain obscure. To gain new insights into the transcriptional regulation of BMI1, we cloned and characterized the promoter region of BMI1. Luciferase reporter assays demonstrated that the region from À783 to +375 showed significant promoter activity. With the use of a series of 5′-deletion and 3′-deletion promoter constructs in luciferase reporter assays, the +167/+232 and À536/À134 regions were found to be sufficient for full promoter activity. Transcriptional activity of the BMI1 promoter was dependent on the Sp1 binding site cluster (+181/ +214) as well as the E-box elements (À181), and was abolished after mutation of the two cis-elements. Electrophoretic mobility shift assays and chromatin immunoprecipitation assays demonstrated that Sp1 bound to the region from +181 to +214 within the BMI1 promoter. In addition, gain-of-function and loss-of-function analyses revealed that Sp1 augmented Bmi1 expression. Further investigations using immunohistochemistry and quantitative RT-PCR disclosed a significant positive correlation between the expression of Sp1 and Bmi1 in normal nasopharyngeal epithelial cells, NPC cells, and NPC tissue specimens. In addition, Myc, the known transcription factor for BMI1 in neuroblastomas, also activated the transcription of BMI1 through binding to the E-box element (À181) within its promoter, and showed a positive correlation with the mRNA level of BMI1 in NPC. In conclusion, these findings provide valuable mechanistic insights into the role of Sp1 and c-Myc in BMI1 transcription in NPC, and suggest that targeting of Sp1 or c-Myc may be a potential therapeutic strategy for NPC.

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Section: Discussionmentioning

confidence: 99%

Sp1 and c‐Myc regulate transcription of BMI1 in nasopharyngeal carcinoma

et al. 2013

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“…Luciferase assays were performed as described (23). ChIP assays were performed as described (28). Briefly, cells were treated with 1% formaldehyde for 20 min at room temperature.…”

Section: Methodsmentioning

confidence: 99%

A Positive Feedback Loop Regulates the Expression of Polycomb Group Protein BMI1 via WNT Signaling Pathway

Cho

Dimri

2013

Journal of Biological Chemistry

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Background: PcG protein BMI1 is transcriptionally regulated by Myc and is up-regulated in cancer cells. Results:The WNT pathway plays an important role in Myc regulation of BMI1. Conclusion: BMI1 up-regulates the WNT pathway, which in turn regulates expression of BMI1 via c-Myc. Significance: The study provides insights into the regulation of BMI1 and suggests that BMI1 expression may be targeted by WNT inhibitors in cancer cells.

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“…Real time-PCR (RT-PCR) was carried out using the QuantiFast SYBR Green RT-PCR Kit (Qiagen), and data were analyzed using Rotor-Gene Q software package (Corbett Life Science-Qiagen, Inc.) as described (21).…”

Section: Methodsmentioning

confidence: 99%

Fbxo45 Inhibits Calcium-sensitive Proteolysis of N-cadherin and Promotes Neuronal Differentiation

Chung

Sahasrabuddhe

et al. 2014

Journal of Biological Chemistry

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Background: Fbxo45 is an atypical E3 ligase that plays an important role in neuronal development. Results: Fbxo45 binds to N-cadherin intracellularly and prevents its degradation. Conclusion: By protecting N-cadherin from proteolysis, Fbxo45 plays a key role in promoting N-cadherin-mediated neuronal differentiation. Significance: This study reveals a novel mechanism of Fbxo45-mediated neuronal differentiation.

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βTrCP regulates BMI1 protein turnover via ubiquitination and degradation

Cited by 46 publications

References 39 publications

Sp1 and c‐Myc regulate transcription of BMI1 in nasopharyngeal carcinoma

Sp1 and c‐Myc regulate transcription of BMI1 in nasopharyngeal carcinoma

A Positive Feedback Loop Regulates the Expression of Polycomb Group Protein BMI1 via WNT Signaling Pathway

Fbxo45 Inhibits Calcium-sensitive Proteolysis of N-cadherin and Promotes Neuronal Differentiation

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