Evidence map›Paper›PMID 26631469›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2015

Olig1 Acetylation and Nuclear Export Mediate Oligodendrocyte Development.

Jinxiang Dai, Kathryn K Bercury, Weilin Jin, Wendy B Macklin

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

39 citing papers in PubMed, 61 citations in OpenAlex.

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  11. Post-Translational Modifications During Brain Development.Advances in experimental medicine and biology · 2022
    Article
  12. Article
  13. Review
  14. PAK1 Positively Regulates Oligodendrocyte Morphology and Myelination.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. RNA-binding protein altered expression and mislocalization in MS.Neurology(R) neuroimmunology & neuroinflammation · 2020
    Article
  20. 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

4 authors at 2 institutions in 2 countries.

Jinxiang DaiDepartment of Cell and Developmental Biology, University of Colorado School of Medicine, Aurora, Colorado 80045.
Kathryn K BercuryDepartment of Cell and Developmental Biology, University of Colorado School of Medicine, Aurora, Colorado 80045.
Weilin JinInstitute of Bio-Nano-Science and Engineering, Department of Instrument Science and Engineering, School of Electronic Information and Electrical Engineering, and School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China.
Wendy B MacklinDepartment of Cell and Developmental Biology, University of Colorado School of Medicine, Aurora, Colorado 80045, Wendy.Macklin@ucdenver.edu.
University of Colorado Denver · USShanghai Jiao Tong University · CN

Funding

The role of mTOR signaling in oligodendrocyte differentiation and CNS myelinationR01NS082203 · NINDS · UNIVERSITY OF COLORADO DENVER · PI MACKLIN, WENDY B, WOOD, TERESA L · 2012 to 2016
$3.3M
GLIAL SURFACE MOLECULES INVOLVED IN NEURONAL DEVELOP-F32NS008223 · NINDS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI PECH, IRENE V · 1987 to 1988
–
NINDS NIH HHS NS08223NINDS NIH HHS R01 NS082203
6 · The paper itself

Abstract

The oligodendrocyte transcription factor Olig1 is critical for both oligodendrocyte development and remyelination in mice. Nuclear to cytoplasmic translocation of Olig1 protein occurs during brain development and in multiple sclerosis, but the detailed molecular mechanism of this translocation remains elusive. Here, we report that Olig1 acetylation and deacetylation drive its active translocation between the nucleus and the cytoplasm in both mouse and rat oligodendrocytes. We identified three functional nuclear export sequences (NES) localized in the basic helix-loop-helix domain and one specific acetylation site at Lys 150 (human Olig1) in NES1. Olig1 acetylation and deacetylation are regulated by the acetyltransferase CREB-binding protein and the histone deacetylases HDAC1, HDAC3, and HDAC10. Acetylation of Olig1 decreased its chromatin association, increased its interaction with inhibitor of DNA binding 2 and facilitated its retention in the cytoplasm of mature oligodendrocytes. These studies establish that acetylation of Olig1 regulates its chromatin dissociation and subsequent translocation to the cytoplasm and is required for its function in oligodendrocyte maturation.

Indexed as

Active Transport, Cell NucleusAge FactorsAnimalsAnimals, NewbornBasic Helix-Loop-Helix ProteinsCells, CulturedCREB-Binding ProteinEmbryo, MammalianFemaleGene Expression Regulation, DevelopmentalHistone AcetyltransferasesHistone DeacetylasesHumansMaleMiceMice, Inbred C57BLBasic Helix-Loop-Helix ProteinsCREB-Binding ProteinHistone AcetyltransferasesHistone DeacetylasesNes protein, mouseNestinOlig1 protein, mousep300-CBP-Associated Factorp300-CBP Transcription FactorsSox10 protein, mouseSOXE Transcription Factorsacetylationnuclear exportOlig1

Identifiers

PMID26631469
PMCPMC4666914
OpenAlexW2184415921

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.