Essential role of autoactivation circuitry on Aurora B-mediated H2AX-pS121 in mitosis
Midori Shimada (),
Takahiro Goshima,
Hiromi Matsuo,
Yoshikazu Johmura,
Mayumi Haruta,
Kazuhiro Murata,
Hiromitsu Tanaka,
Masahito Ikawa,
Keiko Nakanishi and
Makoto Nakanishi ()
Additional contact information
Midori Shimada: Graduate School of Medical Sciences, Nagoya City University
Takahiro Goshima: Graduate School of Medical Sciences, Nagoya City University
Hiromi Matsuo: Graduate School of Medical Sciences, Nagoya City University
Yoshikazu Johmura: Graduate School of Medical Sciences, Nagoya City University
Mayumi Haruta: Graduate School of Medical Sciences, Nagoya City University
Kazuhiro Murata: Graduate School of Medical Sciences, Nagoya City University
Hiromitsu Tanaka: Faculty of Pharmaceutical Sciences, Nagasaki International University, Sasebo
Masahito Ikawa: Research Institute for Microbial Diseases, Osaka University, Suita
Keiko Nakanishi: Institute for Developmental Research, Aichi Human Service Center
Makoto Nakanishi: Graduate School of Medical Sciences, Nagoya City University
Nature Communications, 2016, vol. 7, issue 1, 1-11
Abstract:
Abstract Proper deposition and activation of Aurora B at the centromere is critical for faithful chromosome segregation in mammals. However, the mechanistic basis for abrupt Aurora B kinase activation at the centromere has not yet been fully understood. We demonstrate here that Aurora B-mediated phosphorylation of histone H2AX at serine 121 (H2AX-pS121) promotes Aurora B autophosphorylation and is essential for proper chromosome segregation. Aurora B-mediated H2AX-pS121 is specifically detected at the centromere during mitosis. H2AX depletion results in a severe defect in activation and deposition of Aurora B at this locus. A phosphomimic mutant of H2AX at S121 interacts with activated Aurora B more efficiently than wild-type in vitro. Taken together, these results propose a model in which Aurora B-mediated H2AX-pS121 probably provide a platform for Aurora B autoactivation circuitry at centromeres and thus play a pivotal role in proper chromosome segregation.
Date: 2016
References: Add references at CitEc
Citations:
Downloads: (external link)
https://www.nature.com/articles/ncomms12059 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12059
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/ncomms12059
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().