Evidence map›Paper›PMID 25512562›Full record

ArticleGenes & development2014

Histone acetyltransferase Enok regulates oocyte polarization by promoting expression of the actin nucleation factor spire.

Fu Huang, Ariel Paulson, Arnob Dutta, Swaminathan Venkatesh, Michaela Smolle, Susan M Abmayr, Jerry L Workman

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed, 42 citations in OpenAlex.

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  10. Tctp, a unique Ing5-binding partner, inhibits the chromatin binding of Enok inProceedings of the National Academy of Sciences of the United States of America · 2023
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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

7 authors at 2 institutions in 1 country.

Fu HuangStowers Institute for Medical Research, Kansas City, Missouri 64110, USA;
Ariel PaulsonStowers Institute for Medical Research, Kansas City, Missouri 64110, USA;
Arnob DuttaStowers Institute for Medical Research, Kansas City, Missouri 64110, USA;
Swaminathan VenkateshStowers Institute for Medical Research, Kansas City, Missouri 64110, USA;
Michaela SmolleStowers Institute for Medical Research, Kansas City, Missouri 64110, USA;
Susan M AbmayrStowers Institute for Medical Research, Kansas City, Missouri 64110, USA; Department of Anatomy and Cell Biology, University of Kansas Medical Center, Kansas City, Kansas 66160, USA jlw@stowers.org sma@stowers.org.
Jerry L WorkmanStowers Institute for Medical Research, Kansas City, Missouri 64110, USA; jlw@stowers.org sma@stowers.org.
Stowers Institute for Medical Research · USUniversity of Kansas Medical Center · US

Funding

Analysis of metazoan SAGA complex function in gene expressionR01GM099945 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI ABMAYR, SUSAN M, WORKMAN, JERRY L · 2012 to 2015
$1.2M
NIGMS NIH HHS GM099945NIGMS NIH HHS R01 GM099945
6 · The paper itself

Abstract

KAT6 histone acetyltransferases (HATs) are highly conserved in eukaryotes and have been shown to play important roles in transcriptional regulation. Here, we demonstrate that the Drosophila KAT6 Enok acetylates histone H3 Lys 23 (H3K23) in vitro and in vivo. Mutants lacking functional Enok exhibited defects in the localization of Oskar (Osk) to the posterior end of the oocyte, resulting in loss of germline formation and abdominal segments in the embryo. RNA sequencing (RNA-seq) analysis revealed that spire (spir) and maelstrom (mael), both required for the posterior localization of Osk in the oocyte, were down-regulated in enok mutants. Chromatin immunoprecipitation showed that Enok is localized to and acetylates H3K23 at the spir and mael genes. Furthermore, Gal4-driven expression of spir in the germline can largely rescue the defective Osk localization in enok mutant ovaries. Our results suggest that the Enok-mediated H3K23 acetylation (H3K23Ac) promotes the expression of spir, providing a specific mechanism linking oocyte polarization to histone modification.

Indexed as

Gene Expression Regulation, DevelopmentalAcetylationAnimalsChromatin ImmunoprecipitationDrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianFemaleHistone AcetyltransferasesHistonesMicrofilament ProteinsMutationOocytesOvaryProtein IsoformsDrosophila ProteinsEnok protein, DrosophilaHistone AcetyltransferasesHistonesmael protein, DrosophilaMicrofilament Proteinsosk protein, DrosophilaProtein Isoformsspir protein, Drosophilagerm plasmH3K23 acetylationOskar localization

Identifiers

PMID25512562
PMCPMC4265678
OpenAlexW2066926955

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.