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SR proteins in cancer: function, regulation, and small inhibitor
Mingrong Bei1,2, Jianzhen Xu3
1Systems Biology Laboratory, Shantou University Medical College (SUMC), 22 Xinling Road, Shantou, 515041, China.
Cellular & Molecular Biology Letters
|May 22, 2024
Summary
Serine and arginine-rich (SR) proteins are crucial for RNA processing and gene expression. Their dysregulation contributes to cancer, but targeting them offers new therapeutic strategies.
Area of Science:
- Molecular Biology
- Cancer Biology
- RNA Biology
Background:
- Alternative splicing is essential for gene expression in metazoans.
- Serine and arginine-rich (SR) proteins regulate alternative splicing and other RNA processing events.
- SR protein dysregulation is linked to disrupted cell differentiation and cancer progression.
Purpose of the Study:
- To review the biological characteristics and functions of SR proteins in carcinogenesis.
- To summarize current inhibitors targeting SR proteins for cancer therapy.
Main Methods:
- Literature review of SR protein functions in RNA processing and cancer.
- Analysis of SR protein interactions with m6A regulators.
- Summary of existing SR protein inhibitors.
Main Results:
- SR proteins are multifunctional, involved in splicing, polyadenylation, degradation, and translation.
- SR proteins interact with m6A regulators, influencing RNA methylation.
- Dysfunctional SR proteins disrupt cell differentiation and promote cancer.
Conclusions:
- SR proteins play critical roles in normal cellular processes and cancer development.
- Targeting SR proteins presents a promising avenue for novel cancer therapeutics.
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