Evidence map›Paper›PMID 28457890›Full record

ArticleStem cell reports2017

Context-Dependent Functions of NANOG Phosphorylation in Pluripotency and Reprogramming.

Arven Saunders, Dan Li, Francesco Faiola, Xin Huang, Miguel Fidalgo, Diana Guallar, Junjun Ding, Fan Yang, Yang Xu, Hongwei Zhou and 1 more

Open access · goldAbstract read
In one paragraph

Article in Stem cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

11 citing papers in PubMed, 20 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

11 authors at 3 institutions in 1 country.

Arven SaundersThe Black Family Stem Cell Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; The Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; Department of Cell, Developmental, and Regenerative Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Dan LiThe Black Family Stem Cell Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; The Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; Department of Cell, Developmental, and Regenerative Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Francesco FaiolaThe Black Family Stem Cell Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; Department of Cell, Developmental, and Regenerative Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Xin HuangThe Black Family Stem Cell Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; Department of Cell, Developmental, and Regenerative Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Miguel FidalgoThe Black Family Stem Cell Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; Department of Cell, Developmental, and Regenerative Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Diana GuallarThe Black Family Stem Cell Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; Department of Cell, Developmental, and Regenerative Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Junjun DingThe Black Family Stem Cell Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; Department of Cell, Developmental, and Regenerative Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Fan YangThe Black Family Stem Cell Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; Department of Cell, Developmental, and Regenerative Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Yang XuDivision of Biological Sciences, University of California, San Diego, La Jolla, CA 92093, USA.
Hongwei ZhouThe Black Family Stem Cell Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; Department of Cell, Developmental, and Regenerative Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Jianlong WangThe Black Family Stem Cell Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; The Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; Department of Cell, Developmental, and Regenerative Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA. Electronic address: jianlong.wang@mssm.edu.
Icahn School of Medicine at Mount Sinai · USThe Graduate Center, CUNY · USUniversity of California, San Diego · US

Funding

Interdisciplinary Training in Systems and Developmental Biology and Birth DefectsT32HD075735 · NICHD · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI JABS, ETHYLIN WANG · 2013 to 2022
$1.8M
Oct4 and epigenetic regulation of stem cell pluripotencyR01GM095942 · NIGMS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI WANG, JIANLONG · 2011 to 2015
$1.6M
Catalytic Activity Independent Functions of TET Proteins in PluripotencyR21HD087722 · NICHD · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI WANG, JIANLONG · 2016 to 2017
$466k
NICHD NIH HHS R21 HD087722NICHD NIH HHS T32 HD075735NIGMS NIH HHS R01 GM095942
6 · The paper itself

Abstract

The core pluripotency transcription factor NANOG is critical for embryonic stem cell (ESC) self-renewal and somatic cell reprogramming. Although NANOG is phosphorylated at multiple residues, the role of NANOG phosphorylation in ESC self-renewal is incompletely understood, and no information exists regarding its functions during reprogramming. Here we report our findings that NANOG phosphorylation is beneficial, although nonessential, for ESC self-renewal, and that loss of phosphorylation enhances NANOG activity in reprogramming. Mutation of serine 65 in NANOG to alanine (S65A) alone has the most significant impact on increasing NANOG reprogramming capacity. Mechanistically, we find that pluripotency regulators (ESRRB, OCT4, SALL4, DAX1, and TET1) are transcriptionally primed and preferentially associated with NANOG S65A at the protein level due to presumed structural alterations in the N-terminal domain of NANOG. These results demonstrate that a single phosphorylation site serves as a critical interface for controlling context-dependent NANOG functions in pluripotency and reprogramming.

Indexed as

Cellular ReprogrammingMutation, MissenseProtein Processing, Post-TranslationalAnimalsCell LineCells, CulturedDAX-1 Orphan Nuclear ReceptorDNA-Binding ProteinsEmbryonic Stem CellsInduced Pluripotent Stem CellsMiceNanog Homeobox ProteinOctamer Transcription Factor-3PhosphorylationProtein DomainsProto-Oncogene ProteinsDAX-1 Orphan Nuclear ReceptorDNA-Binding ProteinsEsrrb protein, mouseNanog Homeobox ProteinNanog protein, mouseNr0b1 protein, mouseOctamer Transcription Factor-3Pou5f1 protein, mouseProto-Oncogene ProteinsReceptors, EstrogenSall4 protein, mouseTET1 protein, mouseTranscription FactorsiPSCphospho-NANOGpluripotencypost-translational modificationreprogrammingself-renewalserine to alanine mutation

Identifiers

PMID28457890
PMCPMC5425684
OpenAlexW2608155867

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.