Evidence map›Paper›PMID 27250035›Full record

ArticleOncotarget2016

Osterix acetylation at K307 and K312 enhances its transcriptional activity and is required for osteoblast differentiation.

Jianlei Lu, Shuang Qu, Bing Yao, Yuexin Xu, Yucui Jin, Kaikai Shi, Yifang Shui, Shiyang Pan, Li Chen, Changyan Ma

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 40 citations in OpenAlex.

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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

10 authors at 3 institutions in 2 countries.

Jianlei LuDepartment of Developmental Genetics, Nanjing Medical University, Nanjing, P.R. China.
Shuang QuDepartment of Developmental Genetics, Nanjing Medical University, Nanjing, P.R. China.
Bing YaoDepartment of Developmental Genetics, Nanjing Medical University, Nanjing, P.R. China.
Yuexin XuDepartment of Developmental Genetics, Nanjing Medical University, Nanjing, P.R. China.
Yucui JinDepartment of Developmental Genetics, Nanjing Medical University, Nanjing, P.R. China.
Kaikai ShiDepartment of Developmental Genetics, Nanjing Medical University, Nanjing, P.R. China.
Yifang ShuiDepartment of Developmental Genetics, Nanjing Medical University, Nanjing, P.R. China.
Shiyang PanDepartment of Laboratory Medicine, the First Affiliated Hospital of Nanjing Medical University, Nanjing, P.R. China.
Li ChenMolecular Endocrinology Laboratory, Department of Endocrinology, Odense University Hospital, Odense C, Denmark.
Changyan MaDepartment of Developmental Genetics, Nanjing Medical University, Nanjing, P.R. China.
Nanjing Medical University · CNJiangsu Province Hospital · CNOdense University Hospital · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Osterix (Osx) is an essential transcription factor involved in osteoblast differentiation and bone formation. The precise molecular mechanisms of the regulation of Osx expression are not fully understood. In the present study, we found that in cells, both endogenous and exogenous Osx protein increased after treatment with histone deacetylase inhibitors Trichostatin A and hydroxamic acid. Meanwhile, the results of immunoprecipitation indicated that Osx was an acetylated protein and that the CREB binding protein (CBP), and less efficiently p300, acetylated Osx. The interaction and colocalization of CBP and Osx were demonstrated by Co-immunoprecipitation and immunofluorescence, respectively. In addition, K307 and K312 were identified as the acetylated sites of Osx. By contrast, HDAC4, a histone deacetylase (HDAC), was observed to interact and co-localize with Osx. HDAC4 was demonstrated to mediate the deacetylation of Osx. Moreover, we found that acetylation of Osx enhanced its stability, DNA binding ability and transcriptional activity. Finally, we demonstrated that acetylation of Osx was required for the osteogenic differentiation of C2C12 cells. Taken together, our results provide evidence that CBP-mediated acetylation and HDAC4-mediated deacetylation have critical roles in the modification of Osx, and thus are important in osteoblast differentiation.

Indexed as

AcetylationCell DifferentiationCell LineCREB-Binding ProteinHEK293 CellsHistone DeacetylasesHumansOsteoblastsOsteogenesisRepressor ProteinsSp7 Transcription FactorTransfectionViral Nonstructural ProteinsCREB-Binding ProteinCREBBP protein, humanHDAC4 protein, humanHistone DeacetylasesRepressor ProteinsSP7 protein, humanSp7 Transcription FactorViral Nonstructural ProteinsacetylationCBPosteoblast differentiationosterixPathology Section

Identifiers

PMID27250035
PMCPMC5122325
OpenAlexW2395166522

What OpenQuestion holds

Textmetadata
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.