Evidence map›Paper›PMID 30279526›Full record

ArticleNature communications2018

LOTUS domain protein MARF1 binds CCR4-NOT deadenylase complex to post-transcriptionally regulate gene expression in oocytes.

Li Zhu, Suresh K Kandasamy, Susan E Liao, Ryuya Fukunaga

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

26 citing papers in PubMed, 42 citations in OpenAlex.

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  15. Aristolochic acid I exposure decreases oocyte quality.Frontiers in cell and developmental biology · 2022
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Li ZhuDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, 521 A Physiology Building, Baltimore, MD, 21205, USA.
Suresh K KandasamyDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, 521 A Physiology Building, Baltimore, MD, 21205, USA.
Susan E LiaoDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, 521 A Physiology Building, Baltimore, MD, 21205, USA.
Ryuya FukunagaDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, 521 A Physiology Building, Baltimore, MD, 21205, USA. fukunaga@jhmi.edu.ORCID http://orcid.org/0000-0002-5814-8206
Johns Hopkins University · US

Funding

Mechanism to regulate the length of small silencing RNAsR01GM116841 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FUKUNAGA, RYUYA · 2017 to 2021
$1.7M
Zeiss LSM780 Confocal Microscope for a Core FacilityS10OD016374 · OD · JOHNS HOPKINS UNIVERSITY · PI KUO, SCOT CHARLES · 2013 to 2013
$584k
American Heart Association (American Heart Association, Inc.) 15SDG23220028NIGMS NIH HHS R01 GM116841NIH HHS S10 OD016374U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R01GM116841
6 · The paper itself

Abstract

Post-transcriptional regulation of gene expression plays an essential role during oocyte maturation. Here we report that Drosophila MARF1 (Meiosis Regulator And mRNA Stability Factor 1), which consists of one RNA-recognition motif and six tandem LOTUS domains with unknown molecular function, is essential for oocyte maturation. When tethered to a reporter mRNA, MARF1 post-transcriptionally silences reporter expression by shortening reporter mRNA poly-A tail length and thereby reducing reporter protein level. This activity is mediated by the MARF1 LOTUS domain, which binds the CCR4-NOT deadenylase complex. MARF1 binds cyclin A mRNA and shortens its poly-A tail to reduce Cyclin A protein level during oocyte maturation. This study identifies MARF1 as a regulator in oocyte maturation and defines the conserved LOTUS domain as a post-transcriptional effector domain that recruits CCR4-NOT deadenylase complex to shorten target mRNA poly-A tails and suppress their translation.

Indexed as

RNA 3' End ProcessingAnimalsAnimals, Genetically ModifiedCyclin ADrosophilaDrosophila ProteinsFemaleFertilityMaleMeiosisMembrane ProteinsOocytesProtein TransportRibonucleasesCCR4 protein, DrosophilaCyclin ADrosophila ProteinsMarf protein, DrosophilaMembrane ProteinsRibonucleases

Identifiers

PMID30279526
PMCPMC6168497
OpenAlexW2893635239

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.