Ask about this productRelated genes to: CENPA antibody
- Gene:
- CENPA NIH gene
- Name:
- centromere protein A
- Previous symbol:
- -
- Synonyms:
- CENP-A, CenH3
- Chromosome:
- 2p23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1988-05-31
- Date modifiied:
- 2014-11-19
Related products to: CENPA antibody
Related articles to: CENPA antibody
- Centromeres are specialized chromosomal loci that ensure faithful chromosome segregation during mitosis, a function that depends on the precise localization of the histone H3 variant centromere protein A (CENP-A) within centromeric chromatin. CENP-A deposition is tightly regulated by assembly factors, including HJURP; however, the complete regulatory network remains incompletely defined. Using CENP-A immunoprecipitation coupled with mass spectrometry, we identified SET, a multifunctional chromatin-associated protein involved in transcription and nucleosome assembly, as one of the most enriched proteins in CENP-A immunoprecipitates, suggesting an association between SET and CENP-A. Here, we investigated this association and its functional significance. Reciprocal co-immunoprecipitation assays showed that SET associates with both CENP-A and HJURP. Immunofluorescence analysis revealed that SET localizes to centromeres and that SET depletion reduces centromeric CENP-A enrichment. Live-cell imaging further showed that SET depletion causes chromosome alignment defects and prolonged mitotic arrest. Together, these findings identify SET as a previously unrecognized regulator of the CENP-A-HJURP axis and suggest that SET supports proper CENP-A localization at centromeres and faithful mitotic progression. This study expands our understanding of the regulatory network that maintains centromere identity. - Source: PubMed
Wang YingHu ChengchengWang XinyangXiong FangyuanYao XuebiaoWang Zhikai - Centromeres ensure accurate chromosome segregation, and their identity is specified epigenetically by the histone H3 variant CENP-A. Although the structures of reconstituted CENP-A nucleosomes have provided important insights, how this epigenetic mark is structurally organized within native chromatin remains incompletely understood. Here, we combine cryogenic electron microscopy with chromatin immunoprecipitation (ChIP-CryoEM) to determine the structures of human CENP-A nucleosomes isolated directly from cells without crosslinking or stabilizing agents. We resolved two distinct cellular CENP-A nucleosome structures: a homotypic CENP-A nucleosome and a heterotypic CENP-A/H3 nucleosome, which have been proposed to represent centromeric and ectopic nucleosomes, respectively. Both cellular CENP-A nucleosomes assemble as histone octamers and wrap DNA in a left-handed superhelix, supporting an octameric model proposed for native CENP-A chromatin. In addition, the hallmark CENP-A-specific structural features previously characterized in vitro, including the shortened CENP-A N-terminal α-helix and the distinctive RG loop, are preserved in cellular CENP-A nucleosomes. These findings define the structural organization of CENP-A nucleosomes in cellular chromatin. - Source: PubMed
Publication date: 2026/09/29
Tanida EishoHatazawa SuguruOishi TakumiKobayashi YukiOgasawara MitsuoJaskiewicz Marta AHarada AkihitoFujii TakeruOhkawa YasuyukiTakizawa YoshimasaKurumizaka Hitoshi - Centromeres ensure faithful chromosome segregation, yet the satellite arrays typically underlying these loci exhibit remarkable variation in sequence, organization, and size across individuals and species. Recent advances in long-read genome assemblies and experimental model systems have begun to reveal that this diversity is not simply tolerated but can directly influence centromere function during female meiosis. Asymmetry between centromeric satellite arrays of homologous chromosomes can lead to asymmetries in kinetochore proteins and spindle interactions, biased chromosome orientation on the spindle, and ultimately non-Mendelian inheritance by centromere drive. Emerging evidence further suggests that centromeric satellite asymmetry can increase meiotic chromosome segregation errors and aneuploidy, particularly in the context of small arrays. In this review, we discuss recent progress linking centromeric satellite variation with meiotic chromosome behavior, centromere drive, and segregation fidelity. - Source: PubMed
Publication date: 2026/09/28
Kumar DeepanshuLampson Michael A - Hybrid incompatibility is associated with chromosome instability, DNA damage, and embryonic lethality, yet how cells respond to genome instability in hybrids is unclear. In inviable hybrids generated by fertilizing eggs with sperm, CENP-A is lost from paternal chromosomes, leading to elimination of two chromosome arms. Using hybrid egg extract reactions, we show that CENP-A is removed from chromosomes exposed to cytoplasm through an RNA polymerase II-dependent process associated with DNA damage. Topoisomerase II Binding Protein 1 (TOPBP1) localized to damaged acentric chromosomes during metaphase, and its depletion impaired chromosome alignment, increased DNA damage, and blocked CENP-A removal. Inhibition of DNA polymerase theta increased DNA damage while promoting CENP-A retention, indicating that DNA damage processing rather than damage itself promotes CENP-A loss. Together, our findings reveal separable roles for TOPBP1 in chromosome organization and centromere destabilization, showing how a protective genome surveillance pathway can instead drive chromosome instability in an inviable hybrid. - Source: PubMed
Publication date: 2026/09/18
Clark CordellTerui RikiChistol GheorgheHeald Rebecca - Systemic sclerosis (SSc) is a highly heterogeneous autoimmune disease in which early prognostic stratification is essential. We analysed the clinical and evolutionary associations of 12 SSc-related autoantibodies (Scl-70, CENP-A, CENP-B, RNApol-III, U3-RNP, Th/To, NOR90, U1-RNP, PM/Scl100, PM/Scl75, Ku, and Ro52) in patients with suspected or diagnosed SSc. - Source: PubMed
Publication date: 2026/09/22
López de Turiso Giner PFumanal Idocin LMartínez-Lostao LCorredor Sánchez LSáez Cómet LVelilla Marco J