Fig. 4: Domain architecture of SRSF2 and predicted protein structure. | Leukemia

Fig. 4: Domain architecture of SRSF2 and predicted protein structure.

From: The role of ASXL1, SRSF2, and EZH2 mutations in chromatin dysregulation of myelodysplastic neoplasia and acute myeloid leukemia

Fig. 4: Domain architecture of SRSF2 and predicted protein structure.

a Diagram of SRSF and the hotspot mutations at P95. P95H/L/R A proline-to-histidine, leucine, or arginine substitution at position 95. RRM RNA recognition motif, RS Arginine/serine-rich domain. b AlphaFold’s predicted structure for SRSF2, which indicates that P95 mutations, positioned right before the RS domain, could influence RNA-binding affinity. c Alternative splicing of EZH2 mRNA in association with wild-type SRSF2 and the Pro95 mutant. The Pro95 mutant induces poison exon insertion, resulting in a premature termination codon and subsequent degradation of the mRNA through nonsense-mediated decay. The mutant SRSF2 preferentially binds to an exonic splicing enhancer (ESE) motif (CCNG) within the poison exon, thereby promoting its inclusion.

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