Evidence map›Paper›PMID 25533466›Full record

ArticleThe Journal of biological chemistry2015

The FBXL10/KDM2B scaffolding protein associates with novel polycomb repressive complex-1 to regulate adipogenesis.

Takeshi Inagaki, Satoshi Iwasaki, Yoshihiro Matsumura, Takeshi Kawamura, Toshiya Tanaka, Yohei Abe, Ayumu Yamasaki, Yuya Tsurutani, Ayano Yoshida, Yoko Chikaoka and 8 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

23 citing papers in PubMed, 49 citations in OpenAlex.

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  12. KDM2B Overexpression Facilitates LyticJournal of virology · 2021
    Article
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  14. Review
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  20. The critical role of histone lysine demethylase KDM2B in cancer.American journal of translational research · 2018
    Review
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

18 authors at 3 institutions in 2 countries.

Takeshi InagakiFrom the Division of Metabolic Medicine, the Translational Systems Biology and Medicine Initiative Center for Disease Biology and Integrative Medicine, University of Tokyo, Tokyo 153-8904, Japan, inagaki@lsbm.org.
Satoshi IwasakiFrom the Division of Metabolic Medicine.
Yoshihiro MatsumuraFrom the Division of Metabolic Medicine.
Takeshi Kawamurathe Translational Systems Biology and Medicine Initiative Center for Disease Biology and Integrative Medicine, University of Tokyo, Tokyo 153-8904, Japan, Laboratory for Systems Biology and Medicine.
Toshiya TanakaFrom the Division of Metabolic Medicine, the Translational Systems Biology and Medicine Initiative Center for Disease Biology and Integrative Medicine, University of Tokyo, Tokyo 153-8904, Japan, Laboratory for Systems Biology and Medicine.
Yohei AbeFrom the Division of Metabolic Medicine.
Ayumu YamasakiFrom the Division of Metabolic Medicine.
Yuya TsurutaniFrom the Division of Metabolic Medicine.
Ayano YoshidaFrom the Division of Metabolic Medicine, the Laboratory of Genome and Biosignals, Tokyo University of Pharmacy and Life Science, Tokyo 192-0392, Japan.
Yoko Chikaokathe Translational Systems Biology and Medicine Initiative Center for Disease Biology and Integrative Medicine, University of Tokyo, Tokyo 153-8904, Japan, Laboratory for Systems Biology and Medicine.
Kanako NakamuraFrom the Division of Metabolic Medicine, the Laboratory of Genome and Biosignals, Tokyo University of Pharmacy and Life Science, Tokyo 192-0392, Japan.
Kenta MagooriFrom the Division of Metabolic Medicine, the Translational Systems Biology and Medicine Initiative Center for Disease Biology and Integrative Medicine, University of Tokyo, Tokyo 153-8904, Japan.
Ryo NakakiGenome Science Division, Research Center for Advanced Science and Technology, University of Tokyo, Tokyo 153-8904, Japan.
Timothy F Osbornethe Metabolic Disease Program, Sanford-Burnham Medical Research Institute, Orlando, Florida 32827, and.
Kiyoko Fukamithe Laboratory of Genome and Biosignals, Tokyo University of Pharmacy and Life Science, Tokyo 192-0392, Japan.
Hiroyuki Aburatanithe Translational Systems Biology and Medicine Initiative Center for Disease Biology and Integrative Medicine, University of Tokyo, Tokyo 153-8904, Japan, Genome Science Division, Research Center for Advanced Science and Technology, University of Tokyo, Tokyo 153-8904, Japan.
Tatsuhiko KodamaLaboratory for Systems Biology and Medicine.
Juro SakaiFrom the Division of Metabolic Medicine, the Translational Systems Biology and Medicine Initiative Center for Disease Biology and Integrative Medicine, University of Tokyo, Tokyo 153-8904, Japan, jmsakai-tky@umin.ac.jp.
The University of Tokyo · JPSanford Burnham Prebys Medical Discovery Institute · USTokyo University of Pharmacy and Life Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polycomb repressive complex 1 (PRC1) plays an essential role in the epigenetic repression of gene expression during development and cellular differentiation via multiple effector mechanisms, including ubiquitination of H2A and chromatin compaction. However, whether it regulates the stepwise progression of adipogenesis is unknown. Here, we show that FBXL10/KDM2B is an anti-adipogenic factor that is up-regulated during the early phase of 3T3-L1 preadipocyte differentiation and in adipose tissue in a diet-induced model of obesity. Interestingly, inhibition of adipogenesis does not require the JmjC demethylase domain of FBXL10, but it does require the F-box and leucine-rich repeat domains, which we show recruit a noncanonical polycomb repressive complex 1 (PRC1) containing RING1B, SKP1, PCGF1, and BCOR. Knockdown of either RING1B or SKP1 prevented FBXL10-mediated repression of 3T3-L1 preadipocyte differentiation indicating that PRC1 formation mediates the inhibitory effect of FBXL10 on adipogenesis. Using ChIP-seq, we show that FBXL10 recruits RING1B to key specific genomic loci surrounding the key cell cycle and the adipogenic genes Cdk1, Uhrf1, Pparg1, and Pparg2 to repress adipogenesis. These results suggest that FBXL10 represses adipogenesis by targeting a noncanonical PRC1 complex to repress key genes (e.g. Pparg) that control conversion of pluripotent cells into the adipogenic lineage.

Indexed as

3T3-L1 CellsAdipocytesAdipogenesisAnimalsBiomarkersBlotting, WesternCell CycleCell Cycle ProteinsCell ProliferationChromatin ImmunoprecipitationF-Box ProteinsGene Expression ProfilingHistonesImmunoenzyme TechniquesImmunoprecipitationJumonji Domain-Containing Histone DemethylasesBiomarkersCell Cycle ProteinsF-Box ProteinsHistonesJumonji Domain-Containing Histone DemethylasesKdm2b protein, mouseLeucine-Rich Repeat ProteinsPolycomb Repressive Complex 1PPAR gammaProtein IsoformsProteinsRNA, MessengerRNA, Small Interfering3T3-L1 cellsAdipocyteAdipogenesisCell DifferentiationFBXL10/KDM2B/JHDM1BMitotic Clonal Expansion (MCE)Peroxisome Proliferator-activated Receptor (PPAR)PolycombPolycomb Repressive Complex 1 (PRC1)RING1B

Identifiers

PMID25533466
PMCPMC4326826
OpenAlexW2044115181

What OpenQuestion holds

Textmetadata
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.