Ask about this productRelated genes to: SF3A1 antibody
- Gene:
- SF3A1 NIH gene
- Name:
- splicing factor 3a subunit 1
- Previous symbol:
- -
- Synonyms:
- SF3a120, SAP114, PRPF21, Prp21
- Chromosome:
- 22q12.2
- Locus Type:
- gene with protein product
- Date approved:
- 2000-02-29
- Date modifiied:
- 2019-04-23
Related products to: SF3A1 antibody
Related articles to: SF3A1 antibody
- In recent years, RNA has emerged as a central player in gene regulation and cellular homeostasis, far beyond its canonical role as a mediator between DNA and proteins. Moreover, RNA-binding proteins orchestrate many of these processes not only through their folded domains but also via intrinsically disordered regions (IDRs). Particular attention has been given to arginine-glycine-rich motifs, which endow these regions with remarkable versatility, flexibility, and interaction adaptability. However, the dynamic nature of such regions represents a major challenge for both structural characterization and computational modeling of their interactions with RNA. In this study, we explore the applicability of supervised molecular dynamics (SuMD) to reconstruct, at atomic resolution, the recognition mechanisms between RNA and disordered protein regions while capturing the multistep nature of the binding process. By focusing on two experimentally resolved systems, SF3A1-UBL/U1-SL4 and FUS RRM/U1-SL3, we show that SuMD can reproduce association pathways involving both disordered and structured regions, capturing transient contacts and interaction hierarchies. We further extend the approach to a prospective system lacking an experimentally resolved complex structure, leading to a model that is consistent with experimental mutagenesis data. This approach provides new perspectives for understanding how IDRs recognize and modulate RNA and generating structural hypotheses for such complexes, paving the way for future applications in the rational design of RNA-protein-targeted therapeutics. - Source: PubMed
Publication date: 2026/05/07
Novello GianlucaDodaro AndreaStrascia Chiara CavastracciMenin SilviaSturlese MattiaSalmaso VeronicaMoro Stefano - - Source: PubMed
Publication date: 2026/04/27
Shuai XueqianSun YaoqiLi JialeGao YuanCheng ZhongpingLiu Shupeng - RNA dysregulation mediated by aberrant RNA-binding proteins (RBPs) is closely associated with tumorigenesis. However, the tumorigenic mechanisms of each RBP remained unclear. In this study, we demonstrate that downregulation of Splicing factor 3A1 (SF3A1) markedly suppressed the proliferation of colorectal cancer (CRC) cells, with minimal cytotoxicity observed in non-cancerous epithelial cells. The tumor-promoting function of SF3A1 was further validated in an HCT116 xenograft mouse model. Multiple apoptosis assays-including TdT-mediated dUTP nick end labeling (TUNEL) staining, poly-ADP-ribose polymerase (PARP) immunoblotting, and caspase-3/7 activity measurements-showed that SF3A1 inhibited apoptotic signaling in CRC cells. Transcriptome analysis, combined with RNA-immunoprecipitation (RIP), identified Syntaxin 12 (STX12) as a downstream effector of SF3A1. Knockdown of STX12 induced apoptosis in CRC cells but had no effect on the viability of non-cancerous HCEC-1CT epithelial cells. Furthermore, STX12 mRNA levels were significantly reduced following SF3A1 knockdown, indicating that SF3A1-mediated stabilization of STX12 contributes to apoptosis resistance in CRC cells. Collectively, our findings establish that SF3A1 promotes CRC progression by stabilizing STX12 mRNA and selectively inhibiting apoptosis in malignant cells, thereby identifying the SF3A1-STX12 regulatory axis as a novel and selective therapeutic target for CRC. - Source: PubMed
Publication date: 2026/01/24
Sasaki TakahiroKonishi HiroakiDokoshi TatsuyaSakatani AkiTanaka HirokiYamamoto KojiTakahashi KeitaroAndo KatsuyoshiUeno NobuhiroKashima ShinMoriichi KentaroTanabe HirokiOkumura ToshikatsuFujiya Mikihiro - Subcellular stress profoundly influences protein synthesis. However, both the nature of spatiotemporally restricted chemical cues and local protein responders to these cues remain elusive. Unlocking these mechanisms requires the ability to functionally map in living systems locale-specific stress responder proteins and interrogate how chemical modification of each responder impacts proteome synthesis. We resolved this problem by integrating precision localized electrophile generation and genetic code expansion tools. Upon examination of four distinct subcellular locales, only nuclear-targeted electrophile stress stalled translation. We discovered that NCBP1-a nuclear-resident protein with multifaceted roles in eukaryotic mRNA biogenesis-propagated this nuclear stress signal through a single cysteine (C436) from among its 19 conserved cysteines. This NCBP1(C436)-specific modification elicited alternative splicing of more than 250 genes. Mechanistically, global protein synthesis stall was choreographed by impaired association between electrophile-modified NCBP1(C436) and SF3A1, an essential component of spliceosome, triggering the production of alternatively spliced S6 kinase, whose expression was sufficient to dominantly inhibit protein translation. - Source: PubMed
Publication date: 2026/02/10
Chang DaluAssari MahdiSuwathep ChananyaSappakhaw KhomkritUttamapinant ChayasithLong Marcus J CAye Yimon - Maternal obesity is known to adversely affect fetal development, with placental transcriptional dysregulation being one of the key mechanisms. However, the effect of a maternal high-fat diet (HFD) on dynamic placental gene expression, particularly in the context of obesity propensity, remains poorly understood. This study aimed to investigate the impact of a maternal HFD on time-dependent placental transcriptome alterations, with a focus on identifying key dysregulated pathways during mid-to-late gestation in rats. - Source: PubMed
Publication date: 2026/01/28
Du XiaohanWei YuchenLe ZhiyinWang HongliangChen ZhaoyangYu HuanlingCai Xiaxia