Ask about this productRelated genes to: RBBP6 antibody
- Gene:
- RBBP6 NIH gene
- Name:
- RB binding protein 6, ubiquitin ligase
- Previous symbol:
- -
- Synonyms:
- P2P-R, PACT, SNAMA
- Chromosome:
- 16p12.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-08-17
- Date modifiied:
- 2017-12-01
Related products to: RBBP6 antibody
Related articles to: RBBP6 antibody
- Accurate chromosome segregation during meiosis depends on precise homolog pairing. This process is driven by a series of specialized proteins that link chromosomes to cytoskeletal motors and coordinate chromosome movement for homolog recognition and alignment. Here, we identified RBPL-1, the Caenorhabditis elegans homolog of RBBP6, as a germline-expressed regulator essential for proper homolog pairing and associated nuclear reorganization. Depletion of RBPL-1 impaired the formation of clusters of the LINC complex and CHK-2 kinase within the nuclear periphery. Furthermore, we showed that RBPL-1 regulates the protein abundance of ZIM/HIM-8-family proteins and PLK-2 kinase, two critical mediators of homolog pairing. Notably, RBPL-1's role in homolog pairing is independent of the RING finger domain and Zn knuckle motif, which are proposed to mediate ubiquitination and alternative polyadenylation (APA)/mRNA processing respectively. Instead, we reveal that the evolutionarily conserved yet functionally enigmatic DWNN domain is essential for RBPL-1's function in homolog pairing. In summary, our findings demonstrate that RBPL-1 contributes to meiotic homolog pairing through its DWNN domain, by mediating nuclear reorganization and controlling the abundance of essential pairing factors. - Source: PubMed
Nan WencongLi PanfengLiu GuotengHe LeiZhang MeiyuGao HuiWang BinYu ZhouliangZhang HongtaoLi AngHong Ye - Radioactive iodine (RAI) resistance severely limits treatment efficacy in thyroid carcinoma (THCA), yet its molecular underpinnings remain incompletely elucidated. In the present study, we sought to reveal the molecular mechanism by which histone lysine methyltransferase 2B (KMT2B) regulated dipeptidyl peptidase 4 (DPP4)-mediated THCA resistance to RAI. - Source: PubMed
Publication date: 2026/04/21
Wang MeiqunWang ZhiYang HaifengZhou Tao - Multiple outbreaks of Ebola virus in West Africa have posed significant threats to global public health owing to its high pathogenicity and fatality rates. Current treatments for Ebola Virus Disease are limited, underscoring the imperative for novel antiviral therapies. VP30, a critical RNA synthesis factor, interacts with nucleoprotein (NP) to facilitate Ebola viral genome transcription and replication. Notably, the host ubiquitin-ligase retinoblastoma-binding protein 6 (RBBP6) binds to VP30 at the same interface as NP, thereby inhibiting VP30-NP interactions and indicating that targeting this interface could advance antiviral drug development. In this study, we engineered six peptide mutants through amino acid substitutions at key VP30 binding sites. These mutants were fused to DNA-binding protein from starved cells 4 (DPS4) to assemble nanoparticles, enabling surface display of the peptides. Antiviral effects were evaluated using minigenome and transcription and replication-competent virus-like particles (trVLPs) systems. Among the variants, RPL1 and NPL3 peptides exhibited relatively strong apparent affinities with the VP30 and potent antiviral activity by disrupting Ebola viral genome transcription and replication. To elucidate the binding details between the peptides and VP30, we determined crystal structures of complexes between RPL1 or NPL3 peptides and VP30 via X-ray crystallography. Concurrently, molecular dynamics (MD) simulations revealed the dynamic binding processes of these peptides to VP30. Structural analyses confirmed that the peptides bind to the VP30/NP interface and compete with NP. Our findings demonstrate that DPS4-fusion peptides effectively deliver peptides into cells as nanoparticles and inhibit VP30-NP interactions, presenting a novel antiviral strategy for Ebola virus. - Source: PubMed
Publication date: 2026/03/11
Wu FangHuang YuanweiLi RuiGao PeixuanLv PinpinWu GuanxianMa YanhongDing QiangZhong JinSu JiyanXu Wei - Environmental stresses induce RNA polymerase II (Pol II) to read through normal termination sites at mRNA genes using unknown mechanisms. We observe strong readthrough transcription downstream of thousands of genes after heat shock. Additionally, Pol II no longer pauses after the 3' ends of genes. Heat shock also increases phosphorylation of Tyr1 and Ser2 residues in the Pol II C-terminal domain (CTD) at the 3' ends of genes, which is attenuated at genes with readthrough transcription. Endonucleolytic cleavage of the nascent transcript, key to normal termination, is defective at readthrough genes after heat shock. However, CPSF73, the endonuclease responsible, remains present. Overexpressing an activator of CPSF73, RBBP6, during heat shock rescues the loss of cleavage and dampens readthrough transcription. Together, our results show that heat shock alters Pol II speed, CTD phosphorylation, and CPSF73 activity via RBBP6, contributing to a multifaceted mechanism that enables readthrough of termination sites during cellular stress. - Source: PubMed
Publication date: 2026/02/26
Walsh Kaitlyn EGoodrich James AKugel Jennifer F - Glioma is the most frequently diagnosed brain tumor in adults worldwide which is associated with unfavorable prognosis and survival time. However, the understanding of glioma progression remains limited. - Source: PubMed
Publication date: 2025/12/08
Liao YuxiangLiu BoZhang ZhipingZhang QianXiang MingyongJin Chen