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
- In most animals and fungi, centromere identity and function depend on the Scm3/Holliday junction recognition protein (HJURP) chaperone, which deposits CENPA at centromeres. However, Scm3/HJURP orthologs appeared to be missing in insects, nematodes, many vertebrates, and other metazoans, suggesting radical chaperone replacement in these lineages. Here, we combine remote homology detection, AlphaFold-based structural modeling, and functional genetics in zebrafish and to identify previously unknown Scm3/HJURP orthologs that localize to centromeres and whose loss causes catastrophic mitotic failure. We further show that CAL1, long considered a functional analog, is instead a highly diverged Scm3/HJURP ortholog. Despite rapid primary-sequence divergence, predicted and known structures reveal a broadly conserved CENPA-H4-binding scm3 fold across fungi, vertebrates, nematodes, insects, and most metazoans. Our work demonstrates how rapid divergence can obscure the broad conservation of essential centromere machinery and provides a generalizable strategy for unmasking missing orthologs. - Source: PubMed
Publication date: 2026/07/01
Hollis Jeremy AStonick Jason ATopalidou IriniYoung Janet MMoens Cecilia BLehrbach Nicolas JCampbell Melody GMalik Harmit S - The centromere is the chromosomal site of kinetochore assembly, defined by the histone H3 variant CENP-A. In each cell cycle, the assembly and maintenance of CENP-A is functionally critical for chromosome segregation. In Drosophila male meiosis, CID (fly CENP-A) is assembled in two phases: prophase of meiosis I and postmeiosis II. Here, we investigate the dynamics of the assembly components CAL1 and CENP-C in prophase I and determine the requirements for the second assembly phase. In early prophase I, CENP-C functions with CAL1 to maintain the centromere. In late prophase I, CAL1 is undetectable at centromeres and CENP-C is not critical for centromere maintenance. Instead, CENP-C is crucial for meiotic kinetochore recruitment and function. This CENP-C pool also functions in CID assembly postmeiosis II, which is independent of CAL1. In addition to different functional pools of CENP-C, distinct pools of the CID protein persist in the male germline, and the synthesis of each pool is uncoupled from its cell cycle deposition timing. - Source: PubMed
Publication date: 2026/06/30
Keegan Rachel SMalkeyeva DinaWeever Meg BDunleavy Elaine M - Centromeres are specialized chromatin structures essential for equal chromosome segregation. The human centromeres are organized on a portion of homogeneously repeated DNA sequence and contains nucleosomes including centromere specific histone H3 variant CENP-A. Histone modifications around the CENP-A dense region are also thought to have important roles in centromere function. Here, we used human artificial chromosome (HAC) system based on synthetic centromeric repeat DNA to enable structural and chromatin analysis at ∼2-kb resolution within defined centromere core domains. Analysis using this HAC centromere showed that the CENP-A dense regions span approximately 18-50 kb in size and coexisted with euchromatic histone modifications in an interdependent manner. We further found that when DNA replication reduced CENP-A density, a heterochromatin modification H3K9me3 transiently accumulated in the CENP-A-dense regions. This accumulation was suppressed by the CENP-A deposition factor HJURP and the histone acetyltransferase KAT7, suggesting that CENP-A assembly and euchromatic modifications interdependently antagonize heterochromatin accumulation. The synthetic centromere DNA generated in this study elucidates the epigenetic landscape within the centromere core regions and provides a more precise framework for understanding the dynamic balance between CENP-A assembly and histone modifications. - Source: PubMed
Ohzeki JunichiroWatanabe AkikoLee Jia XianMinami ChiharuKugou KazutoYamazaki KyotaroShirasawa KentaIsobe SachikoEndo YusukeKazuki Yasuhiro - Cell cycle-dependent maintenance of centromere protein A (CENP-A) levels and its spatiotemporal assembly are essential for centromere propagation. CENP-A synthesis peaks in late G2, while its assembly occurs during late telophase/early G1. We have previously shown that phosphorylation of CENP-A at Ser68 by CDK1-cyclin B during mitosis impairs its binding to holiday junction recognition protein (HJURP) and facilitates DCAF11-dependent polyubiquitination and degradation. However, the mechanisms governing CENP-A stability remain elusive. Here, we demonstrate that spindlin interactor and repressor of chromatin binding (SPINDOC), as an M-phase-specific maintenance factor for CENP-A assembly, binds and stabilizes CENP-A by antagonizing DCAF11-dependent polyubiquitination. In addition, SPINDOC bridges CENP-A to HJURP, ensuring that CENP-A is poised for subsequent deposition at centromeres. Interestingly, SPINDOC promotes liver cancer development in vitro and in vivo, and alterations in its levels disrupt CENP-A homeostasis, resulting in chromosomal instability. Together, this study identifies SPINDOC as a mitotic molecular counter of newly synthesized CENP-A, coordinating its spatiotemporal assembly by presenting it to HJURP. - Source: PubMed
Publication date: 2026/06/22
Zhang ZixuZhang XuechunLiu YutingWang KehuiChen ZhenZhang ShengHuang LiMa ZihanShao ChangrongHan YuqinYu ZhouliangZhang XiaodongHuang ZanLin HaiyanLi Guohong - During meiosis, chromosomes face a paradox: the machinery that ensures reductional chromosome segregation also destabilizes centromeres by dismantling kinetochores, risking chromosome missegregation. Here we show how cells resolve this crisis through an unexpected activity of the telomere bouquet. We demonstrate that the bouquet transfers heterochromatin components to pericentromeres, which in turn recruit the Aurora B kinase to direct centromere reassembly. The heterochromatin protein Swi6 relocates from telomeres to centromeres, enabling Haspin kinase-dependent phosphorylation of histone H3 and consequent enrichment of the chromosomal passenger complex, which includes the Aurora B kinase. Aurora B then phosphorylates core centromere proteins, including CenpA and CenpC, to promote kinetochore reassembly. Phosphomimetic mutants of CenpA or CenpC bypass the telomere-heterochromatin-Haspin pathway, demonstrating that Aurora B-mediated phosphorylation is sufficient for reassembly. This function is conserved in mitotically proliferating cells subjected to centromere dismantlement. Our findings establish a safeguarded system that couples meiotic nuclear architecture to centromere identity and reveal a fundamental role for the Aurora B kinase in centromere assembly, beyond its canonical function in correcting kinetochore-spindle attachment errors. - Source: PubMed
Publication date: 2026/06/08
Hou HaitongMorales Ana LopezLiu YingCooper Julia Promisel