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RBM38 in cancer: role and mechanism
- Source :
- Cellular and molecular life sciences : CMLS. 78(1)
- Publication Year :
- 2020
-
Abstract
- Cancer is the second leading cause of death globally. Abnormity in gene expression regulation characterizes the trajectory of tumor development and progression. RNA-binding proteins (RBPs) are widely dysregulated, and thus implicated, in numerous human cancers. RBPs mainly regulate gene expression post-transcriptionally, but emerging studies suggest that many RBPs can impact transcription by acting on chromatin as transcription factors (TFs) or cofactors. Here, we review the evidence that RBM38, an intensively studied RBP, frequently plays a tumor-suppressive role in multiple human cancer types. Genetic studies in mice deficient in RBM38 on different p53 status also establish RBM38 as a tumor suppressor (TS). By uncovering a spectrum of transcripts bound by RBM38, we discuss the diversity in its mechanisms of action in distinct biological contexts. Examination of the genomic features and expression pattern of RBM38 in human tissues reveals that it is generally lost but rarely mutated, in cancers. By assessing future trends in the study of RBM38 in cancer, we signify the possibility of targeting RBM38 and its related pathways as therapeutic strategies against cancer.
- Subjects :
- RNA Stability
Computational biology
Biology
law.invention
03 medical and health sciences
Cellular and Molecular Neuroscience
Transcription (biology)
law
Neoplasms
Gene expression
P53 status
Humans
Gene Regulatory Networks
Molecular Biology
Transcription factor
Pharmacology
Regulation of gene expression
0303 health sciences
030302 biochemistry & molecular biology
RNA-Binding Proteins
Cell Biology
Chromatin
Gene Expression Regulation, Neoplastic
Mutation
Molecular Medicine
Suppressor
Tumor Suppressor Protein p53
Human cancer
Subjects
Details
- ISSN :
- 14209071
- Volume :
- 78
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Cellular and molecular life sciences : CMLS
- Accession number :
- edsair.doi.dedup.....ec4963c6c544a06755f117cf732c2041