Evidence map›Paper›PMID 24948806›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2014

An amino terminal phosphorylation motif regulates intranuclear compartmentalization of Olig2 in neural progenitor cells.

Dimphna H Meijer, Yu Sun, Tao Liu, Michael F Kane, John A Alberta, Guillaume Adelmant, Robert Kupp, Jarrod A Marto, David H Rowitch, Yoshihiro Nakatani and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

17 citing papers in PubMed, 25 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

12 authors at 5 institutions in 1 country.

Dimphna H MeijerDepartment of Neurobiology, Harvard Medical School and Cancer Biology, Dana-Farber Cancer Institute, Boston, Massachusetts 02215.
Yu SunDepartment of Neurobiology, Harvard Medical School and Cancer Biology, Dana-Farber Cancer Institute, Boston, Massachusetts 02215.
Tao LiuDepartment of Biostatistics and Computational Biology, Dana-Farber Cancer Institute and Harvard School of Public Health, Boston, Massachusetts 02215.
Michael F KaneDepartment of Neurobiology, Harvard Medical School and Cancer Biology, Dana-Farber Cancer Institute, Boston, Massachusetts 02215.
John A AlbertaDepartment of Neurobiology, Harvard Medical School and Cancer Biology, Dana-Farber Cancer Institute, Boston, Massachusetts 02215.
Guillaume AdelmantDepartments of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Cancer Biology, Blais Proteomics Center, Dana-Farber Cancer Institute, Boston, Massachusetts 02215.
Robert KuppDepartment of Neurosurgery, Barrow Brain Tumor Research Center, Barrow Neurological Institute, St. Joseph's Hospital and Medical Center, Phoenix, Arizona 85013.
Jarrod A MartoDepartments of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Cancer Biology, Blais Proteomics Center, Dana-Farber Cancer Institute, Boston, Massachusetts 02215.
David H RowitchDepartments of Pediatrics and Neurological Surgery, Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, California 94143, and.
Yoshihiro NakataniDepartment of Neurobiology, Harvard Medical School and Cancer Biology, Dana-Farber Cancer Institute, Boston, Massachusetts 02215.
Charles D StilesDepartment of Neurobiology, Harvard Medical School and Cancer Biology, Dana-Farber Cancer Institute, Boston, Massachusetts 02215, Charles_stiles@dfci.harvard.edu Shwetal.Mehta@dignityhealth.org.
Shwetal MehtaDepartment of Neurosurgery, Barrow Brain Tumor Research Center, Barrow Neurological Institute, St. Joseph's Hospital and Medical Center, Phoenix, Arizona 85013 Charles_stiles@dfci.harvard.edu Shwetal.Mehta@dignityhealth.org.
Harvard University · USBarrow Neurological Institute · USDana-Farber Cancer Institute · USHoward Hughes Medical Institute · USSt. Joseph's Hospital and Medical Center · US

Funding

Transcriptional control of inhibitory synapse formationP01NS047572 · NINDS · DANA-FARBER CANCER INSTITUTE · PI STILES, CHARLES D · 2004 to 2013
$13.5M
OLIGODENDROCYTE LINEAGE GENE FUNCTION IN THE CNSR01NS040511 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ROWITCH, DAVID H · 2000 to 2014
$6.4M
OLIG2 Phosphorylation as a Drug Target for GliomaR01NS057727 · NINDS · DANA-FARBER CANCER INST · PI STILES, CHARLES D · 2007 to 2015
$3.9M
NINDS NIH HHS NS040511NINDS NIH HHS NS047572NINDS NIH HHS NS057727NINDS NIH HHS P01 NS047572NINDS NIH HHS R01 NS040511NINDS NIH HHS R01 NS057727
6 · The paper itself

Abstract

The bHLH transcription factor Olig2 is expressed in cycling neural progenitor cells but also in terminally differentiated, myelinating oligodendrocytes. Sustained expression of Olig2 is counterintuitive because all known functions of the protein in expansion of neural progenitors and specification of oligodendrocyte progenitors are completed with the formation of mature white matter. How are the biological functions of Olig2 suppressed in terminally differentiated oligodendrocytes? In previous studies, we have shown that a triple serine motif in the amino terminus of Olig2 is phosphorylated in cycling neural progenitors but not in their differentiated progeny. We now show that phosphorylation of the triple serine motif regulates intranuclear compartmentalization of murine Olig2. Phosphorylated Olig2 is preferentially localized to a transcriptionally active "open" chromatin compartment together with coregulator proteins essential for regulation of gene expression. Unphosphorylated Olig2, as seen in mature white matter, is localized mainly within a transcriptionally inactive, chromatin fraction characterized by condensed and inaccessible DNA. Of special note is the observation that the p53 tumor suppressor protein is confined to the open chromatin fraction. Proximity ligation assays show that phosphorylation brings Olig2 within 30 nm of p53 within the open chromatin compartment. The data thus shed light on previously noted promitogenic functions of phosphorylated Olig2, which reflect, at least in part, an oppositional relationship with p53 functions.

Indexed as

Amino Acid MotifsAnimalsBasic Helix-Loop-Helix ProteinsCell NucleusCells, CulturedFemaleMaleMiceMice, KnockoutNerve Tissue ProteinsNeural Stem CellsOligodendrocyte Transcription Factor 2PhosphorylationPregnancyBasic Helix-Loop-Helix ProteinsNerve Tissue ProteinsOlig2 protein, mouseOligodendrocyte Transcription Factor 2bHLHintranuclear localizationNuRD complexOlig2p53phosphorylation

Identifiers

PMID24948806
PMCPMC4061392
OpenAlexW2065105253

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.