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Interaction and kinetic assays unveiled how SRSF1 and the single RRM-containing SRSF3 are phosphorylated by SRPK2, another member of the SRPK family.
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SRSF1 regulates lung cancer cell radioresistance through modulating PTPMT1 splicing. Reduced SRSF1 favors the production of short isoforms of PTPMT1 upon ionizing radiation, which in turn promotes phosphorylation of AMPK, thereby inducing DNA double-strand break to sensitize cancer cells to irradiation.
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Results identify for the first time that the phosphorylation state of SRSF1 is linked to different phases in pediatric ALL. The Tyr-19 phosphorylation of SRSF1 disrupts its subcellular localization and promotes proliferation in leukemia cells by driving cell-cycle progression.
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SRSF1 promotes vascular smooth muscle cell (VSMC) proliferation and injury-induced neointima formation. SRSF1 favors the induction of a truncated p53 isoform, Delta133p53, which has an equal proliferative effect and in turn transcriptionally activates Kruppel-like factor 5 (KLF5) via the Delta133p53-EGR1 complex, resulting in an accelerated cell-cycle progression and increased VSMC proliferation.
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repeat RNA-sequestration of SRSF1 triggers the NXF1-dependent nuclear export of C9ORF72 transcripts retaining expanded hexanucleotide repeats
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A -44 G to A "hot zone" putative functional noncoding variant of SRSF1 was found in an AML patient. It alters the binding activities of E2F6, ELF1, and ELK4, ELK4.
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We now show that the ability of SRPK1 to mobilize SRSF1 from speckles to the nucleoplasm is dependent on active CLK1. Diffusion from speckles is promoted by the formation of an SRPK1-CLK1 complex that facilitates dissociation of SRSF1 from CLK1 and enhances the phosphorylation of several serine-proline dipeptides in this SR protein
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Authors showed that Mir505-3p was capable of inhibiting tumor proliferation driven by SRSF1 in two neural tumor cell lines, Neuro-2a (N2a) and U251, exclusively in serum-reduced condition. Authors observed that the protein level of SRSF1 was gradually promoted by increasing concentration of serum.
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The present study suggested that the tumor suppressor miR30c may be involved in prostate cancer tumorigenesis, possibly via targeting ASF/SF2.
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It has been proposed that SF2/ASF has a protective role against JC virus reactivation in multiple sclerosis patients.
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Immune suppression of JC virus gene expression is mediated by SRSF1.
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ASF/SF2 is identified as a splicing regulator of cyclin T1, which contributes to the control of the subsequent transcription events.
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Findings suggest MALAT1 increases AKAP-9 expression by promoting SRPK1-catalyzed SRSF1 phosphorylation in CRC cells. These results reveal a novel molecular mechanism by which MALAT1 regulates AKAP-9 expression in CRC cells.
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high level of SF2, as a novel oncoprotein in RCC, was significantly associated with poor survival in a large cohort of RCC specimens. Taken together, our study presents a road map for the prediction and validation of miR-766-3p/SF2 axis and thus imparts a therapeutic way for further RCC progression.
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The authors found that RNA recognition motif 1 (RRM1) in SRSF1 binds PP1 and represses its catalytic function through an allosteric mechanism.
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We present a joint atomistic molecular dynamics (MD) and experimental study of two RRM-containing proteins bound with their single-stranded target RNAs, namely the Fox-1 and SRSF1 complexes.The simulations predict unanticipated specific participation of Arg142 at the protein-RNA interface of the SRFS1 complex, which is subsequently confirmed by NMR and ITC measurements
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Using NMR spectroscopy with two separately expressed domains of SRSF1, we showed that several residues in the RNA-binding motif 2 interact with the N-terminal region of the RS domain (RS1).
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Especially, in SRSF1 morphants, bone cartilage formation was reduced in the brain and Nkx-2.5 expression was dramatically reduced in the heart of SRSF1 morphants. In addition, a dramatic reduction in functional chordin RNA in SRSF1 morphants was observed suggesting that chordin is one of the targets of SRSF1. Thus, we concluded that SRSF1 is an essential factor for pattern formation including heart, cartilage and germ lay
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results strongly support SRSF1 as a prognostic biomarker in SCLC and provide a rationale for personalized therapy in SCLC
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NSrp70 acts as a new molecular counterpart for alternative splicing of target RNA, counteracting SRSF1 and SRSF2 splicing activity.
