Evidence map›Paper›PMID 30026585›Full record

ArticleNature communications2018

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 and 17 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
4.5field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

62 citing papers in PubMed, 105 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Sirtuins in Women's Health.Pharmaceuticals (Basel, Switzerland) · 2025
    Review
  7. Article
  8. Review
  9. Article
  10. Osteoblast-CD4Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Role of NEL‑like molecule‑1 in osteogenesis/chondrogenesis (Review).International journal of molecular medicine · 2025
    Review

2 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

27 authors at 4 institutions in 2 countries.

Masatoshi FukudaDepartment of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.ORCID http://orcid.org/0000-0002-5692-3969
Tatsuya YoshizawaDepartment of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan. yoshizaw@kumamoto-u.ac.jp.
Md Fazlul KarimDepartment of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Shihab U SobuzDepartment of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Wataru KorogiDepartment of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Daiki KobayasiDepartment of Tumor Genetics and Biology, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Hiroki OkanishiDepartment of Tumor Genetics and Biology, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Masayoshi TasakiDepartment of Morphological and Physiological Sciences, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Katsuhiko OnoDepartment of Microbiology, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Tomohiro SawaDepartment of Microbiology, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Yoshifumi SatoDepartment of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Mami ChirifuDepartment of Structural Biology, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Takeshi MasudaDepartment of Pharmaceutical Microbiology, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Teruya NakamuraDepartment of Structural Biology, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Hironori TanoueDepartment of Molecular Genetics, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Kazuhisa NakashimaDepartment of Pharmacology, Tsurumi University School of Dental Medicine, Yokohama, 230-8501, Japan.
Yoshihiro KobashigawaDepartment of Analytical and Biophysical Chemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Hiroshi MoriokaDepartment of Analytical and Biophysical Chemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Eva BoberDepartment of Cardiac Development and Remodeling, Max-Planck-Institute for Heart and Lung Research, Ludwigstr. 43, 61231, Bad Nauheim, Germany.
Sumio OhtsukiDepartment of Pharmaceutical Microbiology, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.ORCID http://orcid.org/0000-0003-4634-7133
Yuriko YamagataDepartment of Structural Biology, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.ORCID http://orcid.org/0000-0003-0007-4985
Yukio AndoDepartment of Neurology, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Yuichi OikeDepartment of Molecular Genetics, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Norie ArakiDepartment of Tumor Genetics and Biology, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Shu TakedaDepartment of Physiology and Cell Biology, Tokyo Medical and Dental University, Tokyo, 113-8519, Japan.
Hiroshi MizutaDepartment of Orthopaedic Surgery, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Kazuya YamagataDepartment of Medical Biochemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, 860-8556, Japan.
Kumamoto University · JPMax Planck Institute for Heart and Lung Research · DETokyo Medical and Dental University · JPTsurumi University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SP7/Osterix (OSX) is a master regulatory transcription factor that activates a variety of genes during differentiation of osteoblasts. However, the influence of post-translational modifications on the regulation of its transactivation activity is largely unknown. Here, we report that sirtuins, which are NAD(+)-dependent deacylases, regulate lysine deacylation-mediated transactivation of OSX. Germline Sirt7 knockout mice develop severe osteopenia characterized by decreased bone formation and an increase of osteoclasts. Similarly, osteoblast-specific Sirt7 knockout mice showed attenuated bone formation. Interaction of SIRT7 with OSX leads to the activation of transactivation by OSX without altering its protein expression. Deacylation of lysine (K) 368 in the C-terminal region of OSX by SIRT7 promote its N-terminal transactivation activity. In addition, SIRT7-mediated deacylation of K368 also facilitates depropionylation of OSX by SIRT1, thereby increasing OSX transactivation activity. In conclusion, our findings suggest that SIRT7 has a critical role in bone formation by regulating acylation of OSX.

Indexed as

Transcriptional ActivationAcylationAnimalsBone DensityBone Diseases, MetabolicCell DifferentiationCell LineFemaleLysineMaleMiceMice, Inbred C57BLMice, KnockoutOsteoblastsOsteoclastsOsteogenesisLysineSirt7 protein, mouseSirtuinsSp7 protein, mouseSp7 Transcription Factor

Identifiers

PMID30026585
PMCPMC6053369
OpenAlexW2883591283

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.