Ask about this productRelated genes to: RBM26 Blocking Peptide
- Gene:
- RBM26 NIH gene
- Name:
- RNA binding motif protein 26
- Previous symbol:
- C13orf10
- Synonyms:
- PRO1777, SE70-2, FLJ20957, ZC3H17, ARRS2, PPP1R132
- Chromosome:
- 13q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-01-24
- Date modifiied:
- 2014-11-19
Related products to: RBM26 Blocking Peptide
Related articles to: RBM26 Blocking Peptide
- - Source: PubMed
Publication date: 2026/03/14
Chowdhury Tamjid AQuinn Christopher C - Lynch syndrome (LS), the most common hereditary colorectal cancer (CRC), is caused by germline mutations in mismatch repair (MMR) genes, resulting in microsatellite instability-high (MSI-H) tumors. Lynch-like syndrome (LL) exhibits MSI-H and MMR deficiency, but lacks identifiable germline MMR mutations. Although LS/LL CRCs share clinical and molecular features, they are distinct from sporadic MSI-H (SM) CRCs, emphasizing the need for refined molecular classification. This study investigated the somatic alterations that distinguish LS/LL CRC from SM CRC. - Source: PubMed
Publication date: 2025/12/24
Ofuchi TakashiHirose KosukeHosoda KiyotakaIkehara TomohikoHiguchi SatoshiTsujimoto AkinoriWada AoiTamaoka YutaTsuda YasuoOtsu HajimeYonemura YusukeIwatsuki MasaakiMimori Koshi - - Source: PubMed
Publication date: 2025/12/08
He WenXu Rui - The functional diversity and mechanistic complexity of long non-coding RNAs (lncRNAs) exert various regulatory roles in cancer, and they have traditionally been annotated as non-coding genes. Currently, the coding potential of lncRNAs is gradually being revealed; however, their validation and mechanisms of action in cancer remain largely unknown. - Source: PubMed
Publication date: 2025/07/09
Wu QiJi Zhenling - The assembly of constitutive heterochromatin is a prerequisite for maintaining genome stability. However, the mechanism of heterochromatin formation has yet to be completely understood. Here, we demonstrate a crucial role of the nuclear poly(A)-binding protein (PABP) Pab2/PABPN1 in promoting constitutive heterochromatin formation in the fission yeast Schizosaccharomyces japonicus. Histone H3 Lys 9 di- and tri-methylation, hallmarks of heterochromatin, are significantly reduced at centromeres in the absence of Pab2. Pab2 forms nuclear condensates through its RNA-recognition motif (RRM) and the intrinsically disordered domain (IDR), both of which bind to centromeric non-coding RNAs. Intriguingly, two key heterochromatin factors, the histone H3 Lys9 methyltransferase Clr4 and the Mi2-type chromatin remodeler Mit1, associate with centromeres in a Pab2-dependent manner. Pab2 interacts with two putative RNA-binding proteins, the ZC3H3 ortholog Red5 and the RBM26·27 ortholog Rmn1, both essential for heterochromatin formation. Deletion of the Pab2 N-terminal region, which disrupts this interaction, largely abolishes Pab2 function, underscoring the importance of this complex. Pab2 also associates and colocalizes with Ppn1 (a PPP1R10 ortholog), a component of the cleavage and polyadenylation specificity factor (CPSF) complex, and ppn1 mutations disrupt constitutive heterochromatin. Notably, both Ppn1 and Rmn1 are able to interact with Clr4. Our findings reveal that Pab2 plays a pivotal role in heterochromatin assembly by forming nuclear condensates through its RRM/IDR, and Pab2 condensates facilitate the recruitment of Clr4 and Mit1 to centromeres, potentially through its binding proteins, Ppn1 and Rmn1. This study provides new insights into the mechanisms underlying heterochromatin formation and highlights the importance of RNA-binding proteins and phase separation in this process. - Source: PubMed
Publication date: 2025/03/31
Liu ZiyueSong XiuyiThillainadesan GobiSugiyama Tomoyasu