Evidence map›Paper›PMID 21570389›Full record

ArticleDevelopmental biology2011

Reversible response of protein localization and microtubule organization to nutrient stress during Drosophila early oogenesis.

Yuko Shimada, K Mahala Burn, Ryusuke Niwa, Lynn Cooley

Abstract read
In one paragraph

Article in Developmental biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

50 citing papers in PubMed, 74 citations in OpenAlex.

  1. Ovary-Derived Signals Align Protein Appetite with Oogenesis.bioRxiv : the preprint server for biology · 2026
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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

4 authors at 3 institutions in 2 countries.

Yuko ShimadaDepartment of Genetics, Yale School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA.
K Mahala Burn
Ryusuke Niwa
Lynn Cooley
University of Tsukuba · JPWhitney Museum of American Art · USYale University · US

Funding

OOCYTE DEVELOPMENT IN DROSOPHILAR01GM043301 · NIGMS · YALE UNIVERSITY · PI COOLEY, LYNN · 1990 to 2020
$10.7M
NIGMS NIH HHS GM043301NIGMS NIH HHS R01 GM043301
6 · The paper itself

Abstract

The maturation of animal oocytes is highly sensitive to nutrient availability. During Drosophila oogenesis, a prominent metabolic checkpoint occurs at the onset of yolk uptake (vitellogenesis): under nutrient stress, egg chambers degenerate by apoptosis. To investigate additional responses to nutrient deprivation, we studied the intercellular transport of cytoplasmic components between nurse cells and the oocyte during previtellogenic stages. Using GFP protein-traps, we showed that Ypsilon Schachtel (Yps), a putative RNA binding protein, moved into the oocyte by both microtubule (MT)-dependent and -independent mechanisms, and was retained in the oocyte in a MT-dependent manner. These data suggest that oocyte enrichment is accomplished by a combination of MT-dependent polarized transport and MT-independent flow coupled with MT-dependent trapping within the oocyte. Under nutrient stress, Yps and other components of the oskar ribonucleoprotein complex accumulated in large processing bodies in nurse cells, accompanied by MT reorganization. This response was detected as early as 2h after starvation, suggesting that young egg chambers rapidly respond to nutrient stress. Moreover, both Yps aggregation and MT reorganization were reversed with re-feeding of females or the addition of exogenous insulin to cultured egg chambers. Our results suggest that egg chambers rapidly mount a stress response by altering intercellular transport upon starvation. This response implies a mechanism for preserving young egg chambers so that egg production can rapidly resume when nutrient availability improves.

Indexed as

Animal Nutritional Physiological PhenomenaAnimalsDNA-Binding ProteinsDrosophilaDrosophila ProteinsFemaleFluorescenceImmunohistochemistryIn Situ HybridizationMicrotubulesModels, BiologicalOocytesOogenesisPhotobleachingProtein TransportStress, PhysiologicalDNA-Binding ProteinsDrosophila Proteinsosk protein, DrosophilaYPS protein, Drosophila

Identifiers

PMID21570389
PMCPMC3118931
OpenAlexW2050340957

What OpenQuestion holds

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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.