ArticleProceedings of the National Academy of Sciences of the United States of America2021
Ccp1-Ndc80 switch at the N terminus of CENP-T regulates kinetochore assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Dbp7 interacts with RNA exosome component Dis3 to mediate CENP-A loading to centromeres.Genome biology · 2026Article
- The SUN-family protein Sad1 mediates heterochromatin spatial organization through interaction with histone H2A-H2B.Nature communications · 2024Article
- Fluorescence complementation-based FRET imaging reveals centromere assembly dynamics.Molecular biology of the cell · 2024Article
- Cell cycle control of kinetochore assembly.Nucleus (Austin, Tex.) · 2022Review
- Epidemiology of Δ8THC-Related Carcinogenesis in USA: A Panel Regression and Causal Inferential Study.International journal of environmental research and public health · 2022Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Kinetochores, a protein complex assembled on centromeres, mediate chromosome segregation. In most eukaryotes, centromeres are epigenetically specified by the histone H3 variant CENP-A. CENP-T, an inner kinetochore protein, serves as a platform for the assembly of the outer kinetochore Ndc80 complex during mitosis. How CENP-T is regulated through the cell cycle remains unclear. Ccp1 (counteracter of CENP-A loading protein 1) associates with centromeres during interphase but delocalizes from centromeres during mitosis. Here, we demonstrated that Ccp1 directly interacts with CENP-T. CENP-T is important for the association of Ccp1 with centromeres, whereas CENP-T centromeric localization depends on Mis16, a homolog of human RbAp48/46. We identified a Ccp1-interaction motif (CIM) at the N terminus of CENP-T, which is adjacent to the Ndc80 receptor motif. The CIM domain is required for Ccp1 centromeric localization, and the CIM domain-deleted mutant phenocopies
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