Evidence map›Paper›PMID 32191872›Full record

ArticleMolecular cell2020

Ago2-Dependent Processing Allows miR-451 to Evade the Global MicroRNA Turnover Elicited during Erythropoiesis.

Dmitry A Kretov, Isha A Walawalkar, Alexandra Mora-Martin, Andrew M Shafik, Simon Moxon, Daniel Cifuentes

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.9field-weighted citation impact, top 4% 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

40 citing papers in PubMed, 75 citations in OpenAlex.

  1. Dicer-independent miR-451a is upregulated in periodontitis and potentiates inflammation by impairing macrophage polarization and SOCS activity.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Dmitry A KretovDepartment of Biochemistry, Boston University School of Medicine, Boston, MA, USA.
Isha A WalawalkarDepartment of Biochemistry, Boston University School of Medicine, Boston, MA, USA.
Alexandra Mora-MartinDepartment of Biochemistry, Boston University School of Medicine, Boston, MA, USA.
Andrew M ShafikDepartment of Biochemistry, Boston University School of Medicine, Boston, MA, USA.
Simon MoxonSchool of Biological Sciences, University of East Anglia, Norwich, UK.
Daniel CifuentesDepartment of Biochemistry, Boston University School of Medicine, Boston, MA, USA. Electronic address: dcb@bu.edu.
Boston University · USUniversity of East Anglia · GB

Funding

Analysis of non-canonical functions of microRNAsR01GM130935 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI CIFUENTES, DANIEL · 2019 to 2023
$1.9M
Analysis of the Molecular Machinery of microRNA-processing pathwaysR00HD071968 · NICHD · BOSTON UNIVERSITY MEDICAL CAMPUS · PI CIFUENTES, DANIEL · 2016 to 2018
$747k
NICHD NIH HHS R00 HD071968NIGMS NIH HHS R01 GM130935
6 · The paper itself

Abstract

MicroRNAs (miRNAs) are sequentially processed by two RNase III enzymes, Drosha and Dicer. miR-451 is the only known miRNA whose processing bypasses Dicer and instead relies on the slicer activity of Argonaute-2 (Ago2). miR-451 is highly conserved in vertebrates and regulates erythrocyte maturation, where it becomes the most abundant miRNA. However, the basis for the non-canonical biogenesis of miR-451 is unclear. Here, we show that Ago2 is less efficient than Dicer in processing pre-miRNAs, but this deficit is overcome when miR-144 represses Dicer in a negative-feedback loop during erythropoiesis. Loss of miR-144-mediated Dicer repression in zebrafish embryos and human cells leads to increased canonical miRNA production and impaired miR-451 maturation. Overexpression of Ago2 rescues some of the defects of miR-451 processing. Thus, the evolution of Ago2-dependent processing allows miR-451 to circumvent the global repression of canonical miRNAs elicited, in part, by the miR-144 targeting of Dicer during erythropoiesis.

Indexed as

AnimalsArgonaute ProteinsDEAD-box RNA HelicasesErythropoiesisGene Expression Regulation, DevelopmentalHumansMicroRNAsRibonuclease IIIRNA InterferenceZebrafishAGO2 protein, humanArgonaute ProteinsDEAD-box RNA HelicasesDICER1 protein, humanMicroRNAsMIRN144 microRNA, humanMIRN451 microRNA, humanRibonuclease IIIAgo2Ago2-dependentDicerDicer-independenterythropoiesismicroRNAmiR-144miR-451non-canonical microRNAzebrafish

Identifiers

PMID32191872
PMCPMC7201373
OpenAlexW3010880327

What OpenQuestion holds

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Registered trials

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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.