Evidence map›Paper›PMID 31837288›Full record

ArticleDevelopmental biology2020

Clueless forms dynamic, insulin-responsive bliss particles sensitive to stress.

K M Sheard, S A Thibault-Sennett, A Sen, F Shewmaker, R T Cox

Open access · hybridAbstract read
In one paragraph

Article in Developmental biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

11 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
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 1 institution in 1 country.

K M SheardDepartment of Biochemistry and Molecular Biology, Uniformed Services University, Bethesda, MD, 20814, USA.
S A Thibault-SennettDepartment of Biochemistry and Molecular Biology, Uniformed Services University, Bethesda, MD, 20814, USA.
A SenDepartment of Biochemistry and Molecular Biology, Uniformed Services University, Bethesda, MD, 20814, USA.
F ShewmakerDepartment of Pharmacology and Molecular Therapeutics, Uniformed Services University, Bethesda, MD, 20814, USA.
R T CoxDepartment of Biochemistry and Molecular Biology, Uniformed Services University, Bethesda, MD, 20814, USA. Electronic address: rachel.cox@usuhs.edu.
Uniformed Services University of the Health Sciences · US

Funding

Using naturally-occurring fungal prions as models of neurodegenerative protein misfoldingR35GM119790 · NIGMS · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI FENG, YUANYI · 2016 to 2020
$1.4M
Clu forms a dynamic new ribonucleoprotein particle directly involved in mitochondrial functionR01GM127938 · NIGMS · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI COX, RACHEL TAFEL · 2019 to 2022
$1.3M
Elucidating the mechanism of mitochondrial quality control in DrosophilaR21NS085730 · NINDS · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI COX, RACHEL TAFEL · 2015 to 2016
$428k
NIGMS NIH HHS R01 GM127938NIGMS NIH HHS R35 GM119790NINDS NIH HHS R21 NS085730
6 · The paper itself

Abstract

Drosophila Clueless (Clu) is a ribonucleoprotein that directly affects mitochondrial function. Loss of clu causes mitochondrial damage, and Clu associates with proteins on the mitochondrial outer membrane. Clu's subcellular pattern is diffuse throughout the cytoplasm, but Clu also forms large mitochondria-associated particles. Clu particles are reminiscent of ribonucleoprotein particles such as stress granules and processing bodies. Ribonucleoprotein particles play critical roles in the cell by regulating mRNAs spatially and temporally. Here, we show that Clu particles are unique, highly dynamic and rapidly disperse in response to stress in contrast to processing bodies and autophagosomes. In addition, Clu particle formation is dependent on diet as ovaries from starved females no longer contain Clu particles, and insulin signaling is necessary and sufficient for Clu particle formation. Oxidative stress also disperses particles. Since Clu particles are only present under optimal conditions, we have termed them "bliss particles". We also demonstrate that many aspects of Clu function are conserved in the yeast homolog Clu1p. These observations identify Clu particles as stress-sensitive cytoplasmic particles whose absence corresponds with altered cell stress and mitochondrial localization.

Indexed as

AnimalsCytoplasmDrosophilaDrosophila ProteinsFemaleInsulinMitochondriaMitochondrial MembranesNuclear ProteinsOocytesOvarian FollicleOxidative StressPeptide Initiation FactorsRibonucleoproteinsRNA, MessengerSaccharomyces cerevisiaeab protein, DrosophilaCLU1 protein, S cerevisiaeDrosophila ProteinsInsulinNuclear ProteinsPeptide Initiation FactorsRibonucleoproteinsRNA, MessengerSaccharomyces cerevisiae ProteinsCluelessDrosophilaInsulinMitochondriaRibonucleoprotein particle

Identifiers

PMID31837288
PMCPMC7080587
OpenAlexW2996440229

What OpenQuestion holds

Textmetadata
LicenceTDM
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.