Evidence map›Paper›PMID 31289130›Full record

ArticleRNA (New York, N.Y.)2019

Sequestration of microRNA-mediated target repression by the Ago2-associated RNA-binding protein FAM120A.

Timothy J Kelly, Hiroshi I Suzuki, Jesse R Zamudio, Megumu Suzuki, Phillip A Sharp

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

23 citing papers in PubMed, 33 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

5 authors at 2 institutions in 1 country.

Timothy J Kelly *David H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Hiroshi I Suzuki *David H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.ORCID 0000-0003-4682-5086
Jesse R ZamudioDavid H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Megumu SuzukiDavid H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Phillip A SharpDavid H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.ORCID 0000-0003-1465-1691
Massachusetts Institute of Technology · USUniversity of California, Los Angeles · US

Funding

VIRUS PRODUCTION COREP30CA014051 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Jacqueline A. Lees · 1985 to 2026
$93.9M
REGULATION OF MRNA PROCESSINGR01GM034277 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SHARP, PHILLIP A · 1985 to 2021
$8.0M
Stress and Proliferation States Impact MicroRNA-Mediated Regulation in CancerR01CA133404 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SHARP, PHILLIP A · 2008 to 2017
$4.6M
Elucidating Nuclear Argonaute FunctionF32GM101872 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KELLY, TIMOTHY J · 2012 to 2013
$101k
NCI NIH HHS P30 CA014051NCI NIH HHS R01 CA133404NIGMS NIH HHS F32 GM101872NIGMS NIH HHS R01 GM034277
6 · The paper itself

Abstract

Argonaute (Ago) proteins interact with various binding partners and play a pivotal role in microRNA (miRNA)-mediated silencing pathways. By utilizing immunoprecipitation followed by mass spectrometry to determine cytoplasmic Ago2 protein complexes in mouse embryonic stem cells (mESCs), we identified a putative RNA-binding protein FAM120A (also known as OSSA/C9ORF10) as an Ago2 interacting protein. Individual nucleotide resolution cross-linking and immunoprecipitation (iCLIP) analysis revealed that FAM120A binds to homopolymeric tracts in 3'-UTRs of about 2000 mRNAs, particularly poly(G) sequences. Comparison of FAM120A iCLIP and Ago2 iCLIP reveals that greater than one-third of mRNAs bound by Ago2 in mESCs are co-bound by FAM120A. Furthermore, such FAM120A-bound Ago2 target genes are not subject to Ago2-mediated target degradation. Reporter assays suggest that the 3'-UTRs of several FAM120A-bound miRNA target genes are less sensitive to Ago2-mediated target repression than those of FAM120A-unbound miRNA targets and FAM120A modulates them via its G-rich target sites. These findings suggest that Ago2 may exist in multiple protein complexes with varying degrees of functionality.

Indexed as

3' Untranslated RegionsAnimalsArgonaute ProteinsCells, CulturedEmbryonic Stem CellsImmunoprecipitationMiceMicroRNAsNerve Tissue ProteinsRNA-Binding Proteins3' Untranslated RegionsAgo2 protein, mouseArgonaute ProteinsFam120a protein, mouseMicroRNAsNerve Tissue ProteinsRNA-Binding ProteinsAgo2FAM120AiCLIPmicroRNA

Identifiers

PMID31289130
PMCPMC6800481
OpenAlexW2959321860

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.