serine/arginine-Rich Splicing Factor 2 Proteins (SRSF2)

Human serine/arginine-Rich Splicing Factor 2 (SRSF2) interaction partners

1. SRSF2 mutations were significantly related to the shorter OS in patients with myelodysplastic syndromes which may consider as an adverse prognostic risk factor. Whereas, analysis did not show any prognostic effect on overall-survival of chronic myelomonocytic leukemia patients with SRSF2 mutations.

2. SRSF2 is highly expressed in hepatocellular carcinoma and its expression increases with the degree of tumor differentiation and TNM (show ODZ1 Proteins) staging. It is related to lymph node metastasis and metastasis of tumor cells, and is positively related to serum alpha fetoprotein (show AFP Proteins) content, and affects the postoperative survival time of HCC (show FAM126A Proteins) patients.

3. We found that SON and SC35 (also known as SRSF2) localize to the central region of the speckle, whereas MALAT1 and small nuclear (sn)RNAs are enriched at the speckle periphery.

4. Through a serial mutagenesis, authors demonstrate that a 10 nt RNA sequence surrounding the branch-point (BP), is important for SRSF2-mediated inhibition of cassette exon inclusion through directly interacting with SRSF2.

5. The aberrantly spliced target genes and deregulated cellular pathways associated with the commonly mutated splicing factor (show SLU7 Proteins) genes in myelodysplastic syndromes (SF3B1 (show SF3B2 Proteins), SRSF2 and U2AF1 (show U2AF1 Proteins)) are being identified, illuminating the molecular mechanisms underlying the disease. (Review)

6. adverse prognostic impact of SRSF2 mutations on OS and AML (show RUNX1 Proteins) transformation in patients with de novo MDS (show PAFAH1B1 Proteins)

7. SRSF2 mutation is associated with chronic myelomonocytic leukemia.

8. Mutation in SRSF2 gene is associated with Uveal Melanoma.

9. Myelodysplastic syndrome -related P95 (show NBN Proteins) point mutants of SRSF2 lead to alternative splicing of CDC25C (show CDC25C Proteins) in a manner that is not dependent on the DNA damage response.

10. Findings identify SRSF2 as a key regulator of RNA splicing dysregulation in cancer, with possible clinical implications as a candidate prognostic factor in patients with HCC (show FAM126A Proteins).

Mouse (Murine) serine/arginine-Rich Splicing Factor 2 (SRSF2) interaction partners

1. Mice expressing Srsf2 mutation Srsf2P95H, which commonly occurs in individuals with MDS (show MECOM Proteins) and AML (show RUNX1 Proteins), in an inducible, hemizygous manner in hematopoietic cells rapidly succumbed to fatal bone marrow failure, demonstrating that Srsf2-mutated cells depend on the wild-type Srsf2 allele for survival.

2. Findings have shown that SRSF2 not only is involved in splicing regulation of a large number of transcripts but also activates transcription of metabolism-related genes and transcription factors.

3. Depletion of SRSF2 enhances reovirus replication and cytopathic effect, suggesting that T1L (show CERS6 Proteins) mu2 (show AP2M1 Proteins) modulation of splicing benefits the virus.

4. HIV-1-Tat (show TAT Proteins) Protein Inhibits SC35-mediated Tau Exon 10 Inclusion through Up-regulation of DYRK1A (show DYRK1A Proteins) Kinase.

5. The findings suggest that intact SRSF2 is essential for the functional integrity of the hematopoietic system and that its mutations likely contribute to development of myelodysplastic syndromes.

6. SRSF2 mutations alter SRSF2's normal sequence-specific RNA binding activity, thereby altering the recognition of specific exonic splicing enhancer motifs to drive recurrent mis (show AMH Proteins)-splicing of key hematopoietic regulators

7. Study reports that SRSF2 (also known as SC35, an SR-splicing factor (show SLU7 Proteins)) is part of the 7SK complex assembled at gene promoters and plays a direct role in transcription pause release.

8. Specific effects on regulated splicing by SR proteins SRSF1 (show SRSF1 Proteins) and SRSF2 depends on a complex set of relationships with multiple other SR proteins in mammalian genomes.

9. Deficiency of the splicing factor (show SLU7 Proteins) Sfrs10 results in early embryonic lethality in mice and has no impact on full-length SMN/Smn (show STMN1 Proteins) splicing.

10. Oct-4 distribution was examined relative to that of the unphosphorylated form of RNA polymerase II (Pol II) and splicing factor (SC 35) in the intranuclear entities such as perichromatin fibrils.