ArticleThe Journal of cell biology2016
Diaphanous formin mDia2 regulates CENP-A levels at centromeres.
Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Nuclear envelope buffering of cytoskeletal force stabilizes chromosome interactions inbioRxiv : the preprint server for biology · 2026Article
- mDia formins form hetero-oligomers and cooperatively maintain murine hematopoiesis.PLoS genetics · 2023Article
- DIAPH3 deficiency links microtubules to mitotic errors, defective neurogenesis, and brain dysfunction.eLife · 2021Article
- Emerging Properties and Functions of Actin and Actin Filaments Inside the Nucleus.Cold Spring Harbor perspectives in biology · 2021Review
- DIAPH1 Promotes Laryngeal Squamous Cell Carcinoma Progression Through Cell Cycle Regulation.Frontiers in oncology · 2021Article
- Review
- Nuclear Actin Polymerized by mDia2 Confines Centromere Movement during CENP-A Loading.iScience · 2018Article
- Centrifugal Displacement of Nuclei Reveals Multiple LINC Complex Mechanisms for Homeostatic Nuclear Positioning.Current biology : CB · 2017Article
- Formin-mediated epigenetic maintenance of centromere identity.Small GTPases · 2017Review
- Silencing ofJournal of Cancer · 2017Article
- Lack of Diaph3 relaxes the spindle checkpoint causing the loss of neural progenitors.Nature communications · 2016Article
- Set Theory, Logic, and Probability: The Integration of Qualitative Reasoning into Teaching Statistics for Quantitative Biology.CBE life sciences education · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Centromeres of higher eukaryotes are epigenetically defined by centromere protein A (CENP-A), a centromere-specific histone H3 variant. The incorporation of new CENP-A into centromeres to maintain the epigenetic marker after genome replication in S phase occurs in G1 phase; however, how new CENP-A is loaded and stabilized remains poorly understood. Here, we identify the formin mDia2 as essential for stable replenishment of new CENP-A at centromeres. Quantitative imaging, pulse-chase analysis, and high-resolution ratiometric live-cell studies demonstrate that mDia2 and its nuclear localization are required to maintain CENP-A levels at centromeres. Depletion of mDia2 results in a prolonged centromere association of holiday junction recognition protein (HJURP), the chaperone required for CENP-A loading. A constitutively active form of mDia2 rescues the defect in new CENP-A loading caused by depletion of male germ cell Rac GTPase-activating protein (MgcRacGAP), a component of the small GTPase pathway essential for CENP-A maintenance. Thus, the formin mDia2 functions downstream of the MgcRacGAP-dependent pathway in regulating assembly of new CENP-A containing nucleosomes at centromeres.
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Registered trials
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