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    Srsf2 serine and arginine-rich splicing factor 2 [ Mus musculus (house mouse) ]

    Gene ID: 20382, updated on 18-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    PARP inhibition leads to synthetic lethality with key splicing-factor mutations in myelodysplastic syndromes.

    PARP inhibition leads to synthetic lethality with key splicing-factor mutations in myelodysplastic syndromes.
    Zhang F, Sun J, Zhang L, Li R, Wang Y, Geng H, Shen C, Li L, Chen L.,

    08/22/2024
    A mitochondrial surveillance mechanism activated by SRSF2 mutations in hematologic malignancies.

    A mitochondrial surveillance mechanism activated by SRSF2 mutations in hematologic malignancies.
    Liu X, Devadiga SA, Stanley RF, Morrow RM, Janssen KA, Quesnel-Vallières M, Pomp O, Moverley AA, Li C, Skuli N, Carroll M, Huang J, Wallace DC, Lynch KW, Abdel-Wahab O, Klein PS., Free PMC Article

    07/11/2024
    SRSF2 mutation reduces polycythemia and impairs hematopoietic progenitor functions in JAK2V617F-driven myeloproliferative neoplasm.

    SRSF2 mutation reduces polycythemia and impairs hematopoietic progenitor functions in JAK2V617F-driven myeloproliferative neoplasm.
    Yang Y, Abbas S, Sayem MA, Dutta A, Mohi G., Free PMC Article

    12/1/2023
    SRSF2-P95H decreases JAK/STAT signaling in hematopoietic cells and delays myelofibrosis development in mice.

    SRSF2-P95H decreases JAK/STAT signaling in hematopoietic cells and delays myelofibrosis development in mice.
    Willekens C, Laplane L, Dagher T, Benlabiod C, Papadopoulos N, Lacout C, Rameau P, Catelain C, Alfaro A, Edmond V, Signolle N, Marchand V, Droin N, Hoogenboezem R, Schneider RK, Penson A, Abdel-Wahab O, Giraudier S, Pasquier F, Marty C, Plo I, Villeval JL, Constantinescu SN, Porteu F, Vainchenker W, Solary E.

    06/13/2023
    SRSF2 in Sertoli cells is essential for testicular development and spermatogenesis in mice.

    SRSF2 in Sertoli cells is essential for testicular development and spermatogenesis in mice.
    Xie X, Sun L, Duan Y, Lv Z, Yao X, Wang C, Chen X, Tian S, Yan L, Shao Y, Luo H, Liu J.

    04/14/2023
    RUNX1 deficiency cooperates with SRSF2 mutation to induce multilineage hematopoietic defects characteristic of MDS.

    RUNX1 deficiency cooperates with SRSF2 mutation to induce multilineage hematopoietic defects characteristic of MDS.
    Huang YJ, Chen JY, Yan M, Davis AG, Miyauchi S, Chen L, Hao Y, Katz S, Bejar R, Abdel-Wahab O, Fu XD, Zhang DE., Free PMC Article

    12/24/2022
    Srsf2[P95H/+] co-operates with loss of TET2 to promote myeloid bias and initiate a chronic myelomonocytic leukemia-like disease in mice.

    Srsf2(P95H/+) co-operates with loss of TET2 to promote myeloid bias and initiate a chronic myelomonocytic leukemia-like disease in mice.
    Xu JJ, Chalk AM, Wall M, Langdon WY, Smeets MF, Walkley CR.

    12/10/2022
    Genome-wide screening identifies cell-cycle control as a synthetic lethal pathway with SRSF2P95H mutation.

    Genome-wide screening identifies cell-cycle control as a synthetic lethal pathway with SRSF2P95H mutation.
    Xu JJ, Chalk AM, Nikolic I, Simpson KJ, Smeets MF, Walkley CR., Free PMC Article

    04/9/2022
    Loss of SRSF2 triggers hepatic progenitor cell activation and tumor development in mice.

    Loss of SRSF2 triggers hepatic progenitor cell activation and tumor development in mice.
    Zhang C, Shen L, Yuan W, Liu Y, Guo R, Luo Y, Zhan Z, Xie Z, Wu G, Wu W, Feng Y., Free PMC Article

    06/12/2021
    In a new conditional murine Srsf2(P95H) model, where the P95H mutation is expressed physiologically and heterozygously from its endogenous locus after Cre activation, the mutation must occur in the hemopoietic stem-cell-containing populations to promote myelomonocytic bias and expansion with transcriptional and RNA splicing changes. With age, nontransplanted mutant animals develop progressive, transplantablable disease.

    Srsf2(P95H) initiates myeloid bias and myelodysplastic/myeloproliferative syndrome from hemopoietic stem cells.
    Smeets MF, Tan SY, Xu JJ, Anande G, Unnikrishnan A, Chalk AM, Taylor SR, Pimanda JE, Wall M, Purton LE, Walkley CR.

    07/20/2019
    Mutant Srsf2 leads to a compromised Hematopoietic stem cell function by causing abnormal RNA splicing and expression, contributing to the deregulated hematopoiesis that recapitulates the Myelodysplastic syndromes phenotypes, possibly as a result of additional genetic and/or environmental insults.

    Physiological Srsf2 P95H expression causes impaired hematopoietic stem cell functions and aberrant RNA splicing in mice.
    Kon A, Yamazaki S, Nannya Y, Kataoka K, Ota Y, Nakagawa MM, Yoshida K, Shiozawa Y, Morita M, Yoshizato T, Sanada M, Nakayama M, Koseki H, Nakauchi H, Ogawa S., Free PMC Article

    02/9/2019
    Posttranslational modification of SR proteins underlies the regulation of their mRNA export activities and distinguishes pluripotent from differentiated cells.

    Cellular differentiation state modulates the mRNA export activity of SR proteins.
    Botti V, McNicoll F, Steiner MC, Richter FM, Solovyeva A, Wegener M, Schwich OD, Poser I, Zarnack K, Wittig I, Neugebauer KM, Müller-McNicoll M., Free PMC Article

    09/16/2017
    Mice expressing Srsf2 mutation Srsf2P95H, which commonly occurs in individuals with MDS and AML, 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.

    Modulation of splicing catalysis for therapeutic targeting of leukemia with mutations in genes encoding spliceosomal proteins.
    Lee SC, Dvinge H, Kim E, Cho H, Micol JB, Chung YR, Durham BH, Yoshimi A, Kim YJ, Thomas M, Lobry C, Chen CW, Pastore A, Taylor J, Wang X, Krivtsov A, Armstrong SA, Palacino J, Buonamici S, Smith PG, Bradley RK, Abdel-Wahab O., Free PMC Article

    08/12/2017
    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.

    Liver-Specific Deletion of SRSF2 Caused Acute Liver Failure and Early Death in Mice.
    Cheng Y, Luo C, Wu W, Xie Z, Fu X, Feng Y., Free PMC Article

    05/27/2017
    Depletion of SRSF2 enhances reovirus replication and cytopathic effect, suggesting that T1L mu2 modulation of splicing benefits the virus.

    A Cytoplasmic RNA Virus Alters the Function of the Cell Splicing Protein SRSF2.
    Rivera-Serrano EE, Fritch EJ, Scholl EH, Sherry B., Free PMC Article

    05/20/2017
    HIV-1-Tat Protein Inhibits SC35-mediated Tau Exon 10 Inclusion through Up-regulation of DYRK1A Kinase.

    HIV-1-Tat Protein Inhibits SC35-mediated Tau Exon 10 Inclusion through Up-regulation of DYRK1A Kinase.
    Kadri F, Pacifici M, Wilk A, Parker-Struckhoff A, Del Valle L, Hauser KF, Knapp PE, Parsons C, Jeansonne D, Lassak A, Peruzzi F., Free PMC Article

    04/23/2016
    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.

    SRSF2 Is Essential for Hematopoiesis, and Its Myelodysplastic Syndrome-Related Mutations Dysregulate Alternative Pre-mRNA Splicing.
    Komeno Y, Huang YJ, Qiu J, Lin L, Xu Y, Zhou Y, Chen L, Monterroza DD, Li H, DeKelver RC, Yan M, Fu XD, Zhang DE., Free PMC Article

    10/31/2015
    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-splicing of key hematopoietic regulators

    SRSF2 Mutations Contribute to Myelodysplasia by Mutant-Specific Effects on Exon Recognition.
    Kim E, Ilagan JO, Liang Y, Daubner GM, Lee SC, Ramakrishnan A, Li Y, Chung YR, Micol JB, Murphy ME, Cho H, Kim MK, Zebari AS, Aumann S, Park CY, Buonamici S, Smith PG, Deeg HJ, Lobry C, Aifantis I, Modis Y, Allain FH, Halene S, Bradley RK, Abdel-Wahab O., Free PMC Article

    07/25/2015
    Study reports that SRSF2 (also known as SC35, an SR-splicing factor) is part of the 7SK complex assembled at gene promoters and plays a direct role in transcription pause release.

    SR proteins collaborate with 7SK and promoter-associated nascent RNA to release paused polymerase.
    Ji X, Zhou Y, Pandit S, Huang J, Li H, Lin CY, Xiao R, Burge CB, Fu XD., Free PMC Article

    07/20/2013
    Specific effects on regulated splicing by SR proteins SRSF1 and SRSF2 depends on a complex set of relationships with multiple other SR proteins in mammalian genomes.

    Genome-wide analysis reveals SR protein cooperation and competition in regulated splicing.
    Pandit S, Zhou Y, Shiue L, Coutinho-Mansfield G, Li H, Qiu J, Huang J, Yeo GW, Ares M Jr, Fu XD., Free PMC Article

    07/6/2013
    Deficiency of the splicing factor Sfrs10 results in early embryonic lethality in mice and has no impact on full-length SMN/Smn splicing.

    Deficiency of the splicing factor Sfrs10 results in early embryonic lethality in mice and has no impact on full-length SMN/Smn splicing.
    Mende Y, Jakubik M, Riessland M, Schoenen F, Rossbach K, Kleinridders A, Köhler C, Buch T, Wirth B.

    09/27/2010
    splicing factor SC35 has an active role in transcriptional elongation

    The splicing factor SC35 has an active role in transcriptional elongation.
    Lin S, Coutinho-Mansfield G, Wang D, Pandit S, Fu XD., Free PMC Article

    01/21/2010
    intranuclear distribution of SC35 is dependent on GSK-3

    Glycogen synthase kinase-3 plays a crucial role in tau exon 10 splicing and intranuclear distribution of SC35. Implications for Alzheimer's disease.
    Hernández F, Pérez M, Lucas JJ, Mata AM, Bhat R, Avila J.

    01/21/2010
    These findings reveal the involvement of SC35 in specific pathways in regulating cell proliferation and genomic stability during mammalian organogenesis and suggest its potential function in tumorigenesis.

    Splicing regulator SC35 is essential for genomic stability and cell proliferation during mammalian organogenesis.
    Xiao R, Sun Y, Ding JH, Lin S, Rose DW, Rosenfeld MG, Fu XD, Li X., Free PMC Article

    01/21/2010
    This protein was more abundant in the nucleoplasm of mice fed genetically-modified soybeans than in control mice.

    Ultrastructural morphometrical and immunocytochemical analyses of hepatocyte nuclei from mice fed on genetically modified soybean.
    Malatesta M, Caporaloni C, Gavaudan S, Rocchi MB, Serafini S, Tiberi C, Gazzanelli G.

    01/21/2010
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