Figure - available from: Cancer Cell International
This content is subject to copyright. Terms and conditions apply.
The diagram shows the schematic structure of the gene and protein of A-MYB, B-MYB and c-MYB. A The domain structures of A-MYB, B-MYB, and c-MYB. The MYB protein is diagrammed, with N-terminal on the left and C-terminal on the right. The labels at the bottom of the diagram indicate conserved domains. The MYB gene is located on chromosome 6q23.3 and encodes a transcription factor with an N-terminal DNA binding domain (DBD), a central transactivation domain (TAD), and a negative regulatory domain (NRD). Oncogenic activity requires the FAETL domain, the TPTPF domain conserved in the other MYB proteins, and the EVES domain that is involved in intra-molecular interactions and negative regulation. B MYB transcriptional elongation regulation model, and the effect of the interaction between ncRNAs and MYB on the occurrence and development of tumor cells
Source publication
MYB is often overexpressed in malignant tumors and plays a carcinogenic role in the initiation and development of cancer. Deletion of the MYB regulatory C-terminal domain may be a driving mutation leading to tumorigenesis, therefore, different tumor mechanisms produce similar MYB proteins. As MYB is a transcription factor, priority has been given t...
Similar publications
Premature leaf senescence has a profound influence on crop yield and quality. Here, a stable premature senescence mutant (GSm) was obtained from the common wheat (Triticum aestivum L.) cultivar Chang 6878 by mutagenesis with ethyl methanesulfonate. The differences between the GSm mutant and its wild-type (WT) were analyzed in terms of yield charact...
Citations
... When comparison differential expression of microRNAs in CML patients who responded to TKI therapy ("responders") versus those who did not ("non responders"), as well as between normal control bone marrow cells and CML patients' leukemic cells The goal is to identify microRNAs as predictive biomarkers of TKI sensitivity as well as to aid in the investigation of potential microRNA mediated TKI resistance mechanisms for therapeutic use [19]. MiRNA levels in the blood were shown to alter considerably in newly diagnosed CML patients before and throughout the first two weeks of Imatinib treatment, suggesting the possibility of identifying easily detectable biomarkers to track TKI response. ...
... These findings show that miRNA signatures could be used as biomarkers in CML research, allowing for CML staging and predicting patient response to TKI therapy [20]. MYB mRNA stability and translation efficiency are both affected by miR-150, MYB has been shown to be a top predicted target of miR-150, furthermore, miR-150 can target MYB in chronic myeloid leukemia (CML) and limit the production of a number of oncogenes, preventing CML cells from proliferating [19]. MYB is a confirmed target of miR-150. ...
The dysregulation of miRNA expression patterns is one of the many effects developments of cancer, miRNA has been found to express abnormally in hematological neoplasia such as chronic myeloid leukemia and solid malignancies. Resistance and the degree of response following tyrosine kinase inhibitor treatment are correlated with miRNA expression. Hence, in this study we tried to study the relationship of miRNA-150 between different breakpoint cluster region–Abelson (BCR- ABL) P210 transcript levels and the role miRNA- 150 between different levels of imatinib optimal response in chronic myeloid leukemia (CML). Our study included sixty chronic myeloid leukemia (CML) patients they were divided into two groups based on response to imatinib therapy, thirty samples of the optimal molecular response of chronic myeloid leukemia (CML) patients, and thirty samples of failure molecular response chronic myeloid leukemia (CML) patients. Thirty samples of apparently healthy volunteers were included and evaluated as control. According to the P210 BCR-ABL%, the results showed a significant difference (P= < 0.0001) between the responder and the failure response CML patients. Assessed the result of miRNA-150 showed a significant difference between both CML patients (P = < 0.0001), assessed miRNA-150 level among different response groups, and failure response of CML patients (P = 0.0002). A cutoff value of response vs. failure response (1.784) with high sensitivity can be a diagnostic value to differentiate between response and failure response. Changing gene expression with different amounts of miRNAs had an impact on drug-gene interactions, with consequences for cell growth and death. Gene expression of different levels miRNA-150 among of CML patients of imatinib therapy showed high expression in response patients than failure response patients. The gene expression level of miRNA-150 differs through different responses in CML patients.
... This is a novel observation and exposes a yet unidentified mode of dose-dependent differential actions of androgens in PCa. Posttranscriptional regulation of MYB via miRNA-mediated mechanisms has been demonstrated in multiple cancer cell types and during the cellular differentiation (32)(33)(34). Also, several miRNAs have been identified to exhibit aberrant expression in PCa and play a role in pathobiology and therapy resistance (35,36). ...
MYB, a proto-oncogene, is overexpressed in prostate cancer (PCa) and promotes its growth, aggressiveness, and resistance to androgen-deprivation therapy. Here, we examined the effect of androgen signaling on MYB expression and delineated the underlying molecular mechanisms. Paralleling a dichotomous effect on growth, low-dose androgen induced MYB expression at both transcript and protein levels whereas it was suppressed in high-dose androgen-treated PCa cells. Interestingly, treatment with both low- and high-dose androgen transcriptionally upregulated MYB by increasing the binding of androgen receptor (AR) to the MYB promoter. In a time-course assay, androgen induced MYB expression at early time points followed by a sharp decline in high-dose androgen-treated cells due to decreased stability of MYB mRNA. Additionally, profiling of MYB-targeted miRNAs demonstrated significant induction of miR-150 in high-dose androgen-treated PCa cells. We observed a differential binding of AR on miR-150 promoter with significantly greater occupancy recorded in high-dose androgen-treated cells compared to those treated with low-dose androgen. Functional inhibition of miR-150 relieved MYB suppression by high-dose androgen, while miR-150 mimic abolished MYB induction by low-dose androgen. Furthermore, MYB-silencing or miR-150 mimic transfection suppressed PCa cell growth induced by low-dose androgen, whereas miR-150 inhibition rescued PCa cells from growth repression by high-dose androgen. Similarly, we observed that MYB silencing suppressed the expression of androgen-responsive, cell cycle-related genes in low-dose androgen-treated cells, while miR-150 inhibition increased their expression in cells treated with high-dose androgen. Overall, these findings reveal novel androgen-mediated mechanisms of MYB regulation that support its biphasic growth control in PCa cells.
Decades ago, the viral myeloblastosis oncogene v-myb was identified as a gene responsible for the development of avian leukemia. However, the relevance of MYB proteins for human cancer diseases, in particular for solid tumors, remained basically unrecognized for a very long time. The human family of MYB transcription factors comprises MYB (c-MYB), MYBL2 (b-MYB), and MYBL1 (a-MYB), which are overexpressed in several cancers and are associated with cancer progression and resistance to anticancer drugs. In addition to overexpression, the presence of activated MYB-fusion proteins as tumor drivers was described in certain cancers. The identification of anticancer drug resistance mediated by MYB proteins and their underlying mechanisms are of great importance in understanding failures of current therapies and establishing new and more efficient therapy regimens. In addition, new drug candidates targeting MYB transcription factor activity and signaling have emerged as a promising class of potential anticancer therapeutics that could tackle MYB-dependent drug-resistant cancers in a more selective way. This review describes the correlation of MYB transcription factors with the formation and persistence of cancer resistance to various approved and investigational anticancer drugs.
