ArticleThe Journal of biological chemistry2019
Holliday junction recognition protein interacts with and specifies the centromeric assembly of CENP-T.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Aurora B promotes the CENP-T-CENP-W interaction to guide accurate chromosome segregation in mitosis.Journal of molecular cell biology · 2024Article
- Organization of microtubule plus-end dynamics by phase separation in mitosis.Journal of molecular cell biology · 2024Article
- Genomic architecture of resistance to latania scale (H. lataniae) in kiwifruit (A. chinensis var. chinensis).BMC plant biology · 2023Article
- The expression, clinical relevance, and prognostic significance of HJURP in cholangiocarcinoma.Frontiers in oncology · 2022Article
- Diverse mechanisms of centromere specification.Current biology : CB · 2021Review
- Construction of a prognostic model with histone modification-related genes and identification of potential drugs in pancreatic cancer.Cancer cell international · 2021Article
- Mitotic motor CENP-E cooperates with PRC1 in temporal control of central spindle assembly.Journal of molecular cell biology · 2020Article
- Clinical Implications of Chromosomal Instability (CIN) and Kinetochore Abnormalities in Breast Cancers.Molecular diagnosis & therapy · 2019Review
- Mechanism of centromere recruitment of the CENP-A chaperone HJURP and its implications for centromere licensing.Nature communications · 2019Article
Corrections and comments
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Authors and funding
18 authors at 5 institutions in 2 countries.
Funding
Abstract
The centromere is an evolutionarily conserved eukaryotic protein machinery essential for precision segregation of the parental genome into two daughter cells during mitosis. Centromere protein A (CENP-A) organizes the functional centromere via a constitutive centromere-associated network composing the CENP-T complex. However, how CENP-T assembles onto the centromere remains elusive. Here we show that CENP-T binds directly to Holliday junction recognition protein (HJURP), an evolutionarily conserved chaperone involved in loading CENP-A. The binding interface of HJURP was mapped to the C terminus of CENP-T. Depletion of HJURP by CRISPR-elicited knockout minimized recruitment of CENP-T to the centromere, indicating the importance of HJURP in CEPN-T loading. Our immunofluorescence analyses indicate that HJURP recruits CENP-T to the centromere in S/G
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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.