ArticlePloS one2009
The C-terminal domain of CENP-C displays multiple and critical functions for mammalian centromere formation.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
44 citing papers in PubMed, 71 citations in OpenAlex.
- Optimized Genome-Wide Profiling of Centromeric Chromatin Complexes by ChIP-seq.Current protocols · 2026Article
- Models for the architecture of the human inner kinetochore on centromeric α-satellite CENP-A nucleosome arrays.Nature communications · 2026Article
- Centromeres drive and take a break.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025Review
- Interactions with multiple inner kinetochore proteins determine mitotic localization of FACT.The Journal of cell biology · 2025Article
- High-resolution analysis of human centromeric chromatin.Life science alliance · 2025Article
- Article
- CENP-A/CENP-B uncoupling in the evolutionary reshuffling of centromeres in equids.Genome biology · 2025Article
- Molecular evolution of the mammalian kinetochore complex.bioRxiv : the preprint server for biology · 2024Article
- Centromeric chromatin clearings demarcate the site of kinetochore formation.bioRxiv : the preprint server for biology · 2024Article
- Article
- Human centromere repositioning activates transcription and opens chromatin fibre structure.Nature communications · 2022Article
- Kinetochore Architecture Employs Diverse Linker Strategies Across Evolution.Frontiers in cell and developmental biology · 2022Review
- Intrinsic elasticity of nucleosomes is encoded by histone variants and calibrated by their binding partners.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Where is the right path heading from the centromere to spindle microtubules?Cell cycle (Georgetown, Tex.) · 2019Review
- MYC-containing amplicons in acute myeloid leukemia: genomic structures, evolution, and transcriptional consequences.Leukemia · 2018Article
- Reconstitution of a 26-Subunit Human Kinetochore Reveals Cooperative Microtubule Binding by CENP-OPQUR and NDC80.Molecular cell · 2018Article
- The Hidden Genomic and Transcriptomic Plasticity of Giant Marker Chromosomes in Cancer.Genetics · 2018Article
- Article
- The fission yeast nucleoporin Alm1 is required for proteasomal degradation of kinetochore components.The Journal of cell biology · 2017Article
- Molecular basis of CENP-C association with the CENP-A nucleosome at yeast centromeres.Genes & development · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
CENP-C is a fundamental component of functional centromeres. The elucidation of its structure-function relationship with centromeric DNA and other kinetochore proteins is critical to the understanding of centromere assembly. CENP-C carries two regions, the central and the C-terminal domains, both of which are important for the ability of CENP-C to associate with the centromeric DNA. However, while the central region is largely divergent in CENP-C homologues, the C-terminal moiety contains two regions that are highly conserved from yeast to humans, named Mif2p homology domains (blocks II and III). The activity of these two domains in human CENP-C is not well defined. In this study we performed a functional dissection of C-terminal CENP-C region analyzing the role of single Mif2p homology domains through in vivo and in vitro assays. By immunofluorescence and Chromatin immunoprecipitation assay (ChIP) we were able to elucidate the ability of the Mif2p homology domain II to target centromere and contact alpha satellite DNA. We also investigate the interactions with other conserved inner kinetochore proteins by means of coimmunoprecipitation and bimolecular fluorescence complementation on cell nuclei. We found that the C-terminal region of CENP-C (Mif2p homology domain III) displays multiple activities ranging from the ability to form higher order structures like homo-dimers and homo-oligomers, to mediate interaction with CENP-A and histone H3. Overall, our findings support a model in which the Mif2p homology domains of CENP-C, by virtue of their ability to establish multiple contacts with DNA and centromere proteins, play a critical role in the structuring of kinethocore chromatin.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.