Abstract
Background: SFRS1 is a member of the splicing factor protein family. Through a specific sequence of alteration, SRSF1 can move from the cytoplasm to the nucleus where it can work autonomously as a splicing activator, or as a silencer when interacting with other regulators. Alternative splicing (AS) is a fundamental biological process that ensures protein diversity. In fact, different proteins, produced by alternative splicing, can gain different and even antagonistic biological functions. Methods: Our review is based on English articles published in the MEDLINE/PubMed medical library between 2000 and 2021. We retrieved articles that were specifically related to SRSF1 and cancers, and we excluded other reviews and meta-analyses. We included in vitro studies, animal studies and clinical studies, evaluated using the Medical Education Research Study Quality Instrument (MERSQI) and the Newcastle–Ottawa Scale-Education (NOSE). Result: SRSF1 is related to various genes and plays a role in cell cycle, ubiquitin-mediated proteolysis, nucleotide excision repair, p53 pathway, apoptosis, DNA replication and RNA degradation. In most cases, SRSF1 carries out its cancer-related function via abnormal alternative splicing (AS). However, according to the most recent literature, SRSF1 may also be involved in mRNA translation and cancer chemoresistance or radio-sensitivity. Conclusion: Our results showed that SRSF1 plays a key clinical role in tumorigenesis and tumor progression in several types of cancer (such as Prostate, Lung, Breast, Colon, Glioblastoma), through various mechanisms of action and different cellular pathways. This review could be a starting point for several studies regarding the biology of and therapies for cancer.
Highlights
SRSF1 (Serine and Arginine Rich Splicing Factor 1), known as ASF, SF2, SF2P33 or SFRS1, is a member of the splicing factor protein family
Most of studies selected for the review were about lung cancer, followed by breast cancer, prostate cancer and glioblastoma multiforme
SRSF1 has been demonstrated to be overexpressed in a According to our review, SRSF1 has been demonstrated to be overexpressed in a wide range of cancer tissues and to take part in tumorigenesis and progression through different mechanisms
Summary
SRSF1 (Serine and Arginine Rich Splicing Factor 1), known as ASF, SF2, SF2P33 or SFRS1, is a member of the splicing factor protein family. Anczuków, O. et al observed that SRSF1 can work autonomously as a splicing activator, while it requires interaction with other splicing regulators to function as a silencer [3]. According to the study conducted by Ngo et al, SRSF1 2isof 14 initially phosphorylated by SRPK1 (SR protein-specific-kinase 1) on a precise serine residue contained in the SR domain [4]; due to its hypophosphorylation and through its Through a specific sequence of alteration, SRSF1 can move from the cytoplasm to the nucleus where it can work autonomously as a splicing activator, or as a silencer when interacting with other regulators. Different proteins, produced by alternative splicing, can gain different and even antagonistic biological functions
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