Evidence map›Paper›PMID 31896577›Full record

ArticleThe Journal of biological chemistry2020

RNase L promotes the formation of unique ribonucleoprotein granules distinct from stress granules.

James M Burke, Evan T Lester, Devin Tauber, Roy Parker

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

70 citing papers in PubMed, 90 citations in OpenAlex.

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  12. Nonsense-mediated decay controls a negative feedback loop in innate immune sensing.Proceedings of the National Academy of Sciences of the United States of America · 2026
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10 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

James M BurkeDepartment of Biochemistry, University of Colorado, Boulder, Colorado 80303. Electronic address: james.m.burke@colorado.edu.
Evan T LesterDepartment of Biochemistry, University of Colorado, Boulder, Colorado 80303.
Devin TauberDepartment of Biochemistry, University of Colorado, Boulder, Colorado 80303.
Roy ParkerDepartment of Biochemistry, University of Colorado, Boulder, Colorado 80303; Howard Hughes Medical Institute, University of Colorado, Boulder, Colorado 80303.
University of Colorado Boulder · US

Funding

Determining the specificity and biological functions of widespread host mRNA degradation by RNase LF32AI145112 · NIAID · UNIVERSITY OF COLORADO · PI BURKE, JAMES M · 2019 to 2021
$200k
The Role of RNA in Tau AggregationF30AG063468 · NIA · UNIVERSITY OF COLORADO · PI LESTER, EVAN T · 2019 to 2022
$154k
Howard Hughes Medical InstituteNIAID NIH HHS F32 AI145112NIA NIH HHS F30 AG063468
6 · The paper itself

Abstract

Stress granules (SGs) are ribonucleoprotein (RNP) assemblies that form in eukaryotic cells as a result of limited translation in response to stress. SGs form during viral infection and are thought to promote the antiviral response because many viruses encode inhibitors of SG assembly. However, the antiviral endoribonuclease RNase L also alters SG formation, whereby only small punctate SG-like bodies that we term RNase L-dependent bodies (RLBs) form during RNase L activation. How RLBs relate to SGs and their mode of biogenesis is unknown. Herein, using immunofluorescence, live-cell imaging, and MS-based analyses, we demonstrate that RLBs represent a unique RNP granule with a protein and RNA composition distinct from that of SGs in response to dsRNA lipofection in human cells. We found that RLBs are also generated independently of SGs and the canonical dsRNA-induced SG biogenesis pathway, because RLBs did not require protein kinase R, phosphorylation of eukaryotic translation initiation factor 2 subunit 1 (eIF2α), the SG assembly G3BP paralogs, or release of mRNAs from ribosomes via translation elongation. Unlike the transient interactions between SGs and P-bodies, RLBs and P-bodies extensively and stably interacted. However, despite both RLBs and P-bodies exhibiting liquid-like properties, they remained distinct condensates. Taken together, these observations reveal that RNase L promotes the formation of a unique RNP complex that may have roles during the RNase L-mediated antiviral response.

Indexed as

A549 CellsCell LineCytoplasmic GranulesEndoribonucleasesHEK293 CellsHumansRibonucleoproteins2-5A-dependent ribonucleaseEndoribonucleasesRibonucleoproteinsdouble-stranded RNA (dsRNA)innate immunitylipid dropletprocessing body (P-body)Protein kinase R (PKR)Ribonuclease L (RNase L)RNA degradationRNA turnoverstress granule

Identifiers

PMID31896577
PMCPMC7008361
OpenAlexW2997447385

What OpenQuestion holds

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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.