Evidence map›Paper›PMID 26949256›Full record

ArticleeLife2016

SOX2 O-GlcNAcylation alters its protein-protein interactions and genomic occupancy to modulate gene expression in pluripotent cells.

Samuel A Myers, Sailaja Peddada, Nilanjana Chatterjee, Tara Friedrich, Kiichrio Tomoda, Gregor Krings, Sean Thomas, Jason Maynard, Michael Broeker, Matthew Thomson and 4 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
17.8field-weighted citation impact, top 1% 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

50 citing papers in PubMed, 84 citations in OpenAlex.

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  11. Glycosylation in Stem Cell Biology.Handbook of experimental pharmacology · 2025
    Review
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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

14 authors at 2 institutions in 2 countries.

Samuel A MyersDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, United States.
Sailaja PeddadaDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.
Nilanjana ChatterjeeDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.
Tara FriedrichGladstone Institute University of California, San Francisco, San Francisco, United States.
Kiichrio TomodaGladstone Institute University of California, San Francisco, San Francisco, United States.
Gregor KringsDepartment of Pathology, University of California, San Francisco, San Francisco, United States.
Sean ThomasGladstone Institute University of California, San Francisco, San Francisco, United States.
Jason MaynardDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, United States.
Michael BroekerCenter for Systems and Synthetic Biology, University of California, San Francisco, San Francisco, United States.
Matthew ThomsonCenter for Systems and Synthetic Biology, University of California, San Francisco, San Francisco, United States.
Katherine PollardGladstone Institute University of California, San Francisco, San Francisco, United States.
Shinya YamanakaGladstone Institute University of California, San Francisco, San Francisco, United States.
Alma L BurlingameDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, United States.
Barbara PanningDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, United States.ORCID http://orcid.org/0000-0002-8301-1172
University of California, San Francisco · USGladstone Institutes · US

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008284 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KORTEMME, TANJA · 1988 to 2022
$10.1M
BMI Bioinformatics Training GrantsT32GM067547 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI HERNANDEZ, RYAN D. · 2003 to 2022
$6.6M
Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
Quantitative models for controlling collective cell fate selection in stem cellsDP5OD012194 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI THOMSON, MATTHEW W. · 2012 to 2016
$1.8M
Role of SOX2 O-GIcNAcylation in pluripotencyR01GM114871 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI PANNING, BARBARA · 2016 to 2019
$1.3M
Investigation of the Tip60-p400 complex role in embryonic stem cell self-renR01GM085186 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI PANNING, BARBARA · 2009 to 2012
$1.2M
PURCHASE OF LTQ FT-ICR HYBRID MASS SPECTROMETER: (HEI) PROTEOMICSS10RR019934 · NCRR · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI BURLINGAME, ALMA L · 2004 to 2004
$1.0M
Howard Hughes Medical InstituteNCRR NIH HHS 1S10RR019934NCRR NIH HHS S10 RR019934NIGMS NIH HHS P41 GM103481NIGMS NIH HHS P41GM103481NIGMS NIH HHS R01 GM085186NIGMS NIH HHS R01GM085186NIGMS NIH HHS R01 GM114871NIGMS NIH HHS T32 GM008284NIGMS NIH HHS T32 GM067547NIH HHS DP5 OD012194
6 · The paper itself

Abstract

The transcription factor SOX2 is central in establishing and maintaining pluripotency. The processes that modulate SOX2 activity to promote pluripotency are not well understood. Here, we show SOX2 is O-GlcNAc modified in its transactivation domain during reprogramming and in mouse embryonic stem cells (mESCs). Upon induction of differentiation SOX2 O-GlcNAcylation at serine 248 is decreased. Replacing wild type with an O-GlcNAc-deficient SOX2 (S248A) increases reprogramming efficiency. ESCs with O-GlcNAc-deficient SOX2 exhibit alterations in gene expression. This change correlates with altered protein-protein interactions and genomic occupancy of the O-GlcNAc-deficient SOX2 compared to wild type. In addition, SOX2 O-GlcNAcylation impairs the SOX2-PARP1 interaction, which has been shown to regulate ESC self-renewal. These findings show that SOX2 activity is modulated by O-GlcNAc, and provide a novel regulatory mechanism for this crucial pluripotency transcription factor.

Indexed as

Gene Expression RegulationProtein Processing, Post-TranslationalAcetylglucosamineAnimalsCell DifferentiationMicePluripotent Stem CellsProtein BindingSOXB1 Transcription FactorsAcetylglucosamineSox2 protein, mouseSOXB1 Transcription Factorsbiochemistrydevelopmental biologyelectron transfer dissociationembryonic stem cellsmouseO-GlcNAcpluripotencySOX2stem cellstranscription factors

Identifiers

PMID26949256
PMCPMC4841768
OpenAlexW2301431651

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.