Nature Communications (Jul 2018)
SIRT7 has a critical role in bone formation by regulating lysine acylation of SP7/Osterix
- Masatoshi Fukuda,
- Tatsuya Yoshizawa,
- Md. Fazlul Karim,
- Shihab U. Sobuz,
- Wataru Korogi,
- Daiki Kobayasi,
- Hiroki Okanishi,
- Masayoshi Tasaki,
- Katsuhiko Ono,
- Tomohiro Sawa,
- Yoshifumi Sato,
- Mami Chirifu,
- Takeshi Masuda,
- Teruya Nakamura,
- Hironori Tanoue,
- Kazuhisa Nakashima,
- Yoshihiro Kobashigawa,
- Hiroshi Morioka,
- Eva Bober,
- Sumio Ohtsuki,
- Yuriko Yamagata,
- Yukio Ando,
- Yuichi Oike,
- Norie Araki,
- Shu Takeda,
- Hiroshi Mizuta,
- Kazuya Yamagata
Affiliations
- Masatoshi Fukuda
- Department of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University
- Tatsuya Yoshizawa
- Department of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University
- Md. Fazlul Karim
- Department of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University
- Shihab U. Sobuz
- Department of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University
- Wataru Korogi
- Department of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University
- Daiki Kobayasi
- Department of Tumor Genetics and Biology, Faculty of Life Sciences, Kumamoto University
- Hiroki Okanishi
- Department of Tumor Genetics and Biology, Faculty of Life Sciences, Kumamoto University
- Masayoshi Tasaki
- Department of Morphological and Physiological Sciences, Faculty of Life Sciences, Kumamoto University
- Katsuhiko Ono
- Department of Microbiology, Faculty of Life Sciences, Kumamoto University
- Tomohiro Sawa
- Department of Microbiology, Faculty of Life Sciences, Kumamoto University
- Yoshifumi Sato
- Department of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University
- Mami Chirifu
- Department of Structural Biology, Faculty of Life Sciences, Kumamoto University
- Takeshi Masuda
- Department of Pharmaceutical Microbiology, Faculty of Life Sciences, Kumamoto University
- Teruya Nakamura
- Department of Structural Biology, Faculty of Life Sciences, Kumamoto University
- Hironori Tanoue
- Department of Molecular Genetics, Faculty of Life Sciences, Kumamoto University
- Kazuhisa Nakashima
- Department of Pharmacology, Tsurumi University School of Dental Medicine
- Yoshihiro Kobashigawa
- Department of Analytical and Biophysical Chemistry, Faculty of Life Sciences, Kumamoto University
- Hiroshi Morioka
- Department of Analytical and Biophysical Chemistry, Faculty of Life Sciences, Kumamoto University
- Eva Bober
- Department of Cardiac Development and Remodeling, Max-Planck-Institute for Heart and Lung Research
- Sumio Ohtsuki
- Department of Pharmaceutical Microbiology, Faculty of Life Sciences, Kumamoto University
- Yuriko Yamagata
- Department of Structural Biology, Faculty of Life Sciences, Kumamoto University
- Yukio Ando
- Department of Neurology, Faculty of Life Sciences, Kumamoto University
- Yuichi Oike
- Department of Molecular Genetics, Faculty of Life Sciences, Kumamoto University
- Norie Araki
- Department of Tumor Genetics and Biology, Faculty of Life Sciences, Kumamoto University
- Shu Takeda
- Department of Physiology and Cell Biology, Tokyo Medical and Dental University
- Hiroshi Mizuta
- Department of Orthopaedic Surgery, Faculty of Life Sciences, Kumamoto University
- Kazuya Yamagata
- Department of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University
- DOI
- https://doi.org/10.1038/s41467-018-05187-4
- Journal volume & issue
-
Vol. 9,
no. 1
pp. 1 – 14
Abstract
SP7/Osterix is a transcription factor involved in osteoblast differentiation. Here, the authors show that Sirtuin 7 activates Osterix posttranslationally by regulating its lysine acylation, and that mice lacking Sirtuin 7 in osteoblasts show reduced bone formation.
