Evidence map›Paper›PMID 27151441›Full record

ArticleMolecular cell2016

S6K1 Phosphorylation of H2B Mediates EZH2 Trimethylation of H3: A Determinant of Early Adipogenesis.

Sang Ah Yi, Sung Hee Um, Jaecheol Lee, Ji Hee Yoo, So Young Bang, Eun Kyung Park, Min Gyu Lee, Ki Hong Nam, Ye Ji Jeon, Jong Woo Park and 7 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing 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

58 citing papers in PubMed, 88 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors at 7 institutions in 3 countries.

Sang Ah YiResearch Center for Epigenome Regulation, School of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Sung Hee UmDepartment of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 16419, Republic of Korea; Department of Health Sciences and Technology, Samsung Advanced Institute for Health Sciences and Technology, Samsung Medical Center, Seoul 06351, Republic of Korea.
Jaecheol LeeDivision of Cardiology, Department of Medicine, Stanford University School of Medicine, 265 Campus Drive, Room G1120B, Stanford, CA 94305-5454, USA.
Ji Hee YooResearch Center for Epigenome Regulation, School of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea.
So Young BangResearch Center for Epigenome Regulation, School of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Eun Kyung ParkResearch Center for Epigenome Regulation, School of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Min Gyu LeeResearch Center for Epigenome Regulation, School of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Ki Hong NamResearch Center for Epigenome Regulation, School of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Ye Ji JeonResearch Center for Epigenome Regulation, School of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Jong Woo ParkResearch Center for Epigenome Regulation, School of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Jueng Soo YouDepartment of Biochemistry, School of Medicine, Konkuk University, Seoul 05029, Republic of Korea.
Sang-Jin LeeResearch Center for Cell Fate Control, College of Pharmacy, Sookmyung Women's University, Seoul 04310, Republic of Korea.
Gyu-Un BaeResearch Center for Cell Fate Control, College of Pharmacy, Sookmyung Women's University, Seoul 04310, Republic of Korea.
Jong Won RhieDepartment of Plastic Surgery, College of Medicine, Catholic University of Korea, Seoul 06591, Republic of Korea.
Sara C KozmaDivision of Hematology and Oncology, Department of Internal Medicine, College of Medicine, University of Cincinnati, Cincinnati, OH 45267, USA; Laboratory of Cancer Metabolism, Catalan Institute of Oncology (ICO), Bellvitge Biomedical Research Institute, Institut d'Investigació Biomèdica de Bellvitge (IDIBELL), 08908 Hospitalet de Llobregat, Barcelona, Spain.
George ThomasDivision of Hematology and Oncology, Department of Internal Medicine, College of Medicine, University of Cincinnati, Cincinnati, OH 45267, USA; Laboratory of Cancer Metabolism, Catalan Institute of Oncology (ICO), Bellvitge Biomedical Research Institute, Institut d'Investigació Biomèdica de Bellvitge (IDIBELL), 08908 Hospitalet de Llobregat, Barcelona, Spain; Unitat de Bioquímica, Dep. Ciències Fisiològiques II, Facultat de Medicina, Campus Universitari de Bellvitge - IDIBELL, Universitat de Barcelona, 08908 L'Hospitalet de Llobregat, Catalunya, Barcelona, Spain. Electronic address: gthomas@idibell.cat.
Jeung-Whan HanResearch Center for Epigenome Regulation, School of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea. Electronic address: jhhan551@skku.edu.
Sungkyunkwan University · KRInstitut Català d'Oncologia · ESSookmyung Women's University · KRCatholic University of Korea · KRKonkuk University · KRSamsung Medical Center · KRStanford University · US

Funding

The Function of rpL5 and rpL11 in induction of p53R01CA158768 · NCI · UNIVERSITY OF CINCINNATI · PI THOMAS, GEORGE · 2012 to 2017
$1.5M
NCI NIH HHS R01 CA158768
6 · The paper itself

Abstract

S6K1 has been implicated in a number of key metabolic responses, which contribute to obesity. Critical among these is the control of a transcriptional program required for the commitment of mesenchymal stem cells to the adipocytic lineage. However, in contrast to its role in the cytosol, the functions and targets of nuclear S6K1 are unknown. Here, we show that adipogenic stimuli trigger nuclear translocation of S6K1, leading to H2BS36 phosphorylation and recruitment of EZH2 to H3, which mediates H3K27 trimethylation. This blocks Wnt gene expression, inducing the upregulation of PPARγ and Cebpa and driving increased adipogenesis. Consistent with this finding, white adipose tissue from S6K1-deficient mice exhibits no detectable H2BS36 phosphorylation or H3K27 trimethylation, whereas both responses are highly elevated in obese humans or in mice fed a high-fat diet. These findings define an S6K1-dependent mechanism in early adipogenesis, contributing to the promotion of obesity.

Indexed as

AdipogenesisProtein Processing, Post-TranslationalAdipocytesAdipose TissueAdiposityAnimalsCCAAT-Enhancer-Binding ProteinsDisease Models, AnimalEnhancer of Zeste Homolog 2 ProteinEpigenesis, GeneticHeLa CellsHistonesHumansMaleMethylationMiceCCAAT-Enhancer-Binding ProteinsCEBPA protein, humanCEBPA protein, mouseEnhancer of Zeste Homolog 2 ProteinEZH2 protein, humanEzh2 protein, mouseHistonesPPAR gammaribosomal protein S6 kinase, 70kD, polypeptide 1Ribosomal Protein S6 Kinases, 70-kDaRibosomal Protein S6 Kinases, 90-kDaRps6ka1 protein, mouseWnt Proteins

Identifiers

PMID27151441
PMCPMC5325705
OpenAlexW2340171624

What OpenQuestion holds

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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.