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    Aurora Kinase B, a novel regulator of TERF1 binding and telomeric integrity

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    Author
    Chan, FL; Vinod, B; Novy, K; Schittenhelm, RB; Huang, C; Udugama, M; Nunez-Iglesias, J; Lin, JI; Hii, L; Chan, J; ...
    Date
    2017-12-01
    Source Title
    Nucleic Acids Research
    Publisher
    OXFORD UNIV PRESS
    University of Melbourne Author/s
    Nunez-Iglesias, Juan
    Affiliation
    Medicine Dentistry & Health Sciences
    Metadata
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    Document Type
    Journal Article
    Citations
    Chan, F. L., Vinod, B., Novy, K., Schittenhelm, R. B., Huang, C., Udugama, M., Nunez-Iglesias, J., Lin, J. I., Hii, L., Chan, J., Pickett, H. A., Daly, R. J. & Wong, L. H. (2017). Aurora Kinase B, a novel regulator of TERF1 binding and telomeric integrity. NUCLEIC ACIDS RESEARCH, 45 (21), pp.12340-12353. https://doi.org/10.1093/nar/gkx904.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/255462
    DOI
    10.1093/nar/gkx904
    Abstract
    AURKB (Aurora Kinase B) is a serine/threonine kinase better known for its role at the mitotic kinetochore during chromosome segregation. Here, we demonstrate that AURKB localizes to the telomeres in mouse embryonic stem cells, where it interacts with the essential telomere protein TERF1. Loss of AURKB function affects TERF1 telomere binding and results in aberrant telomere structure. In vitro kinase experiments successfully identified Serine 404 on TERF1 as a putative AURKB target site. Importantly, in vivo overexpression of S404-TERF1 mutants results in fragile telomere formation. These findings demonstrate that AURKB is an important regulator of telomere structural integrity.

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