Somatic Mutations in Core Spliceosome Components Promote Tumorigenesis and Generate an Exploitable Vulnerability in Human Cancer - PubMed
- ️Sat Jan 01 2022
Review
Somatic Mutations in Core Spliceosome Components Promote Tumorigenesis and Generate an Exploitable Vulnerability in Human Cancer
Claudio Sette et al. Cancers (Basel). 2022.
Abstract
Alternative pre-mRNA processing enables the production of distinct mRNA and protein isoforms from a single gene, thus greatly expanding the coding potential of eukaryotic genomes and fine-tuning gene expression programs. Splicing is carried out by the spliceosome, a complex molecular machinery which assembles step-wise on mRNA precursors in the nucleus of eukaryotic cells. In the last decade, exome sequencing technologies have allowed the identification of point mutations in genes encoding splicing factors as a recurrent hallmark of human cancers, with higher incidence in hematological malignancies. These mutations lead to production of splicing factors that reduce the fidelity of the splicing process and yield splicing variants that are often advantageous for cancer cells. However, at the same time, these mutations increase the sensitivity of transformed cells to splicing inhibitors, thus offering a therapeutic opportunity for novel targeted strategies. Herein, we review the recent literature documenting cancer-associated mutations in components of the early spliceosome complex and discuss novel therapeutic strategies based on small-molecule spliceosome inhibitors that exhibit strong anti-tumor effects, particularly against cancer cells harboring mutations in spliceosomal components.
Keywords: alternative splicing; cancer; somatic mutations; spliceosome.
Conflict of interest statement
The authors declare no conflict of interest.
Figures

Pre-mRNA assembly by the spliceosome machine. The stepwise interaction of the spliceosomal snRNPs and RBPs in the removal of an intron from a pre-mRNA containing two exons (black).

U2AF35, U2AF65, and SF3B1 mutations in an individual with hematological malignancies. Schematic representation of U2AF35, U2AF65, and SF3B1 protein domains and recurrent somatic mutations identified in cancer patients within each domain. ZF, zinc finger; UHM, U2AF homology motif; RS, Arginine Serine domain; RRM, RNA-recognition motif; ULM, U2AF ligand motif; HD, HEAT (Huntingtin, Elongation factor 3, protein phosphatase 2A, Targets of rapamycin 1) Domain.

Splicing-based therapeutic strategies in cancer. (A) SF3B1 binding agents, including spliceostatin A, meayamycin, and Pladienolide B, interact with SF3B1, thus blocking its binding to the branch point. (B) PRMT5 inhibitors inhibit PRMT5-mediated symmetric demethylation of arginines’ (SDMA) on Sm (D1, B/B, D3) proteins, which is required for spliceosome assembly. (C) Indisulam links the E2 ubiquitin ligase complex to RBM39 through the adaptor DCAF15, thus leading to polyubiquitination of RBM39 and its proteasome-mediated degradation.
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