Evidence map›Paper›PMID 31844131›Full record

ArticleScientific reports2019

Protein components of ribonucleoprotein granules from Drosophila germ cells oligomerize and show distinct spatial organization during germline development.

Hieu D L Vo, Wahiduzzaman, Samuel J Tindell, Jimiao Zheng, Ming Gao, Alexey L Arkov

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

22 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
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  8. How germ granules promote germ cell fate.Nature reviews. Genetics · 2024
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Germ granules in development.Development (Cambridge, England) · 2023
    Article
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  16. Article
  17. Review
  18. Looking at the Pretty "Phase" of Membraneless Organelles: A View FromFrontiers in cell and developmental biology · 2022
    Review
  19. Article
  20. Article
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

6 authors at 2 institutions in 1 country.

Hieu D L VoDepartment of Biological Sciences, Murray State University, Murray, KY, 42071, USA.
WahiduzzamanDepartment of Biological Sciences, Murray State University, Murray, KY, 42071, USA.
Samuel J TindellDepartment of Biological Sciences, Murray State University, Murray, KY, 42071, USA.
Jimiao ZhengDepartment of Biological Sciences, Murray State University, Murray, KY, 42071, USA.
Ming GaoBiology Department, Indiana University Northwest, Gary, IN, 46408, USA.
Alexey L ArkovDepartment of Biological Sciences, Murray State University, Murray, KY, 42071, USA. aarkov@murraystate.edu.
Murray State University · USIndiana University Northwest · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The assembly of large RNA-protein granules occurs in germ cells of many animals and these germ granules have provided a paradigm to study structure-functional aspects of similar structures in different cells. Germ granules in Drosophila oocyte's posterior pole (polar granules) are composed of RNA, in the form of homotypic clusters, and proteins required for germline development. In the granules, Piwi protein Aubergine binds to a scaffold protein Tudor, which contains 11 Tudor domains. Using a super-resolution microscopy, we show that surprisingly, Aubergine and Tudor form distinct clusters within the same polar granules in early Drosophila embryos. These clusters partially overlap and, after germ cells form, they transition into spherical granules with the structural organization unexpected from these interacting proteins: Aubergine shell around the Tudor core. Consistent with the formation of distinct clusters, we show that Aubergine forms homo-oligomers and using all purified Tudor domains, we demonstrate that multiple domains, distributed along the entire Tudor structure, interact with Aubergine. Our data suggest that in polar granules, Aubergine and Tudor are assembled into distinct phases, partially mixed at their "interaction hubs", and that association of distinct protein clusters may be an evolutionarily conserved mechanism for the assembly of germ granules.

Indexed as

AnimalsCell LineCytoplasmic GranulesDrosophilaDrosophila ProteinsGerm CellsOocytesPeptide Initiation FactorsRibonucleoproteinsSf9 CellsTudor Domainaub protein, DrosophilaDrosophila ProteinsPeptide Initiation FactorsRibonucleoproteins

Identifiers

PMID31844131
PMCPMC6915754
OpenAlexW2995489786

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.