SFRS8 Blocking Peptide
- Known as:
- SFRS8 Blocking Peptide
- Catalog number:
- 33r-5508
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- SFRS8 Blocking Peptide
Related genes to: SFRS8 Blocking Peptide
- Gene:
- SFSWAP NIH gene
- Name:
- splicing factor SWAP
- Previous symbol:
- SFRS8
- Synonyms:
- SWAP
- Chromosome:
- 12q24.33
- Locus Type:
- gene with protein product
- Date approved:
- 1995-09-11
- Date modifiied:
- 2017-09-13
Related products to: SFRS8 Blocking Peptide
Related articles to: SFRS8 Blocking Peptide
- Dual-specificity protein kinase CLK4 plays a pivotal role in regulating alternative mRNA splicing, DNA repair, and various cellular processes through precise phosphorylation. In this study, we analyzed 3825 global human cellular phosphoproteome studies, identifying 430 qualitative profiles and 55 quantitative differential datasets featuring high-confidence Class-1 phosphosites (localization probability ≥ 75%; A-score ≥ 13). Notably, S136 and S138 emerged as predominant phosphorylation sites outside the kinase domain. These sites showed frequent detection and differential expression in liver, lung, and head and neck cancers, as documented in PhosphositePlus. We identified a high-confidence set of co-regulated phosphoproteins, including SQSTM1, SRRT, RPS6, TP53BP1, TNKS1BP1, THUMPD1, OTUD4, and TCEA1. These proteins link CLK4 to critical pathways, including RNA splicing, autophagy, DNA damage response, and cancer progression. Binary interactors, including SRRM2, Interacts with SPT6 1 (IWS1), RBBP6, ZC3H18, BUD13, and DYRK1A, further connect CLK4 to RNA processing and splicing. Predicted downstream substrates, such as CCNL2, CDK11B, PRDX6, YTHDC1, RBM15, SRRM1, SFSWAP, HNRNPU, and DOCK7, highlight CLK4's broad regulatory scope. Upstream kinases were also predicted for S136 and S138. Site-resolved analyses revealed tumor-specific dysregulation of CLK4 phosphorylation at key residues. Co-occurring phosphosite alterations and nearby somatic mutations suggest disrupted CLK4 regulation in cancer. Overall, this study provides a comprehensive phosphoproteomic resource that maps CLK4's co-regulatory networks, paving the way for mechanistic investigations and targeted cancer therapies. - Source: PubMed
Publication date: 2026/07/22
Pai ApoorvaDcunha LeonaGopalakrishnan Athira PerunellyUmmar SamseeraRajeev Athira CRaju Rajesh - Diffuse large B-cell lymphoma (DLBCL) remains a challenging disease with limited therapeutic options beyond standard immunochemotherapy. ETS transcription factors, including SPIB and SPI1, are implicated in lymphoma pathogenesis and can be targeted by the small molecule TK216, which disrupts ETS-DHX9 interactions. To explore mechanisms of resistance, we generated stable TK216-resistant clones from the ABC-DLBCL line U2932. Resistant clones exhibited a 4-5-fold increase in IC values and lost the ability to undergo G2-M arrest upon treatment. Transcriptomic and mutational analyses revealed three resistance patterns: (i) MDR1/ABCB1 overexpression, leading to multidrug efflux; (ii) Cluster A, enriched for proliferation, Wnt, and transcriptional programs, with mutations in ESR2, USP24, and SFSWAP; and (iii) Cluster B, characterized by actin/microtubule remodeling, altered metabolism, and mutations in SRSF11 and PATJ. Pharmacologic screening revealed an increased sensitivity of resistant cells to BCL2, MCL1, and XPO1 inhibitors, while also showing reduced sensitivity to aurora kinase and microtubule-targeting agents. Venetoclax and selinexor retained activity in resistant models, supporting their potential for rational combinations with TK216. These findings demonstrate that multiple, heterogeneous mechanisms drive resistance to ETS inhibition in DLBCL, highlighting therapeutic strategies to overcome it. - Source: PubMed
Spriano FilippoCascione LucianoTarantelli ChiaraSartori GiulioArribas Alberto JVelasova AdrianaNapoli SaraHavranek OndrejToretsky Jeffrey ABertoni Francesco - An elegant screening strategy unveils a molecular actor that connects widespread changes in mRNA processing with a nutrient-sensing protein modification. - Source: PubMed
Publication date: 2025/05/08
Hanover John A - O-GlcNAcylation is the reversible post-translational addition of β--acetylglucosamine to serine and threonine residues of nuclear and cytoplasmic proteins. It plays an important role in several cellular processes through the modification of thousands of protein substrates. O-GlcNAcylation in humans is mediated by a single essential enzyme, O-GlcNAc transferase (OGT). OGT, together with the sole O-GlcNAcase OGA, form an intricate feedback loop to maintain O-GlcNAc homeostasis in response to changes in cellular O-GlcNAc using a dynamic mechanism involving nuclear retention of its fourth intron. However, the molecular mechanism of this dynamic regulation remains unclear. Using an O-GlcNAc responsive GFP reporter cell line, we identify SFSWAP, a poorly characterized splicing factor, as a trans-acting factor regulating OGT intron detention. We show that SFSWAP is a global regulator of retained intron splicing and exon skipping that primarily acts as a negative regulator of splicing. In contrast, knockdown of SFSWAP leads to reduced inclusion of a 'decoy exon' present in the OGT retained intron which may mediate its role in OGT intron detention. Global analysis of decoy exon inclusion in SFSWAP and UPF1 double knockdown cells indicate altered patterns of decoy exon usage. Together, these data indicate a role for SFSWAP as a global negative regulator of pre-mRNA splicing and positive regulator of intron retention. - Source: PubMed
Publication date: 2025/04/23
Govindan AshwinConrad Nicholas K - O-GlcNAcylation is the reversible post-translational addition of β-N-acetylglucosamine to serine and threonine residues of nuclear and cytoplasmic proteins. It plays an important role in several cellular processes through the modification of thousands of protein substrates. O-GlcNAcylation in humans is mediated by a single essential enzyme, O-GlcNAc transferase (OGT). OGT, together with the sole O-GlcNAcase OGA, form an intricate feedback loop to maintain O-GlcNAc homeostasis in response to changes in cellular O-GlcNAc using a dynamic mechanism involving nuclear retention of its fourth intron. However, the molecular mechanism of this dynamic regulation remains unclear. Using an O-GlcNAc responsive GFP reporter cell line, we identify SFSWAP, a poorly characterized splicing factor, as a trans-acting factor regulating OGT intron detention. We show that SFSWAP is a global regulator of retained intron splicing and exon skipping that primarily acts as a negative regulator of splicing. In contrast, knockdown of SFSWAP leads to reduced inclusion of a 'decoy exon' present in the OGT retained intron which may mediate its role in OGT intron detention. Global analysis of decoy exon inclusion in SFSWAP and UPF1 double knockdown cells indicate altered patterns of decoy exon usage. Together, these data indicate a role for SFSWAP as a global negative regulator of pre-mRNA splicing and positive regulator of intron retention. - Source: PubMed
Publication date: 2025/01/30
Govindan AshwinConrad Nicholas K