Evidence map›Paper›PMID 18282112›Full record

ArticlePLoS genetics2008

Motility screen identifies Drosophila IGF-II mRNA-binding protein--zipcode-binding protein acting in oogenesis and synaptogenesis.

Kristin L M Boylan, Sarah Mische, Mingang Li, Guillermo Marqués, Xavier Morin, William Chia, Thomas S Hays

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

30 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. N6-Methyladenosine Methylation of mRNA in Cell Senescence.Cellular and molecular neurobiology · 2023
    Review
  6. Article
  7. Tagged actin mRNA dysregulation in IGF2BP1[Formula: see text] mice.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
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  17. Article
  18. Review
  19. Article
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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

7 authors at 4 institutions in 3 countries.

Kristin L M BoylanDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota, United States of America.
Sarah Mische
Mingang Li
Guillermo Marqués
Xavier Morin
William Chia
Thomas S Hays
University of Minnesota · USInserm · FRNational University of Singapore · SGUniversity of Alabama at Birmingham · US

Funding

STRUCTURE AND FUNCTION OF CYTOPLASMIC DYNEINR01GM044757 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI HAYS, THOMAS S · 1990 to 2022
$5.7M
CELL POLARITY AND CYTOSKELETAL TRANSPORT IN DROSOPHILAR01GM053695 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI HAYS, THOMAS S · 1996 to 2006
$1.1M
Trafficking of BMP signals in neuronsR21NS051319 · NINDS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI MARQUES, GUILLERMO · 2006 to 2007
$354k
NIGMS NIH HHS GM53695NIGMS NIH HHS R01 GM044757NIGMS NIH HHS R01 GM053695NIGMS NIH HHS R01 GM44757NINDS NIH HHS R21 NS051319Wellcome Trust
6 · The paper itself

Abstract

The localization of specific mRNAs can establish local protein gradients that generate and control the development of cellular asymmetries. While all evidence underscores the importance of the cytoskeleton in the transport and localization of RNAs, we have limited knowledge of how these events are regulated. Using a visual screen for motile proteins in a collection of GFP protein trap lines, we identified the Drosophila IGF-II mRNA-binding protein (Imp), an ortholog of Xenopus Vg1 RNA binding protein and chicken zipcode-binding protein. In Drosophila, Imp is part of a large, RNase-sensitive complex that is enriched in two polarized cell types, the developing oocyte and the neuron. Using time-lapse confocal microscopy, we establish that both dynein and kinesin contribute to the transport of GFP-Imp particles, and that regulation of transport in egg chambers appears to differ from that in neurons. In Drosophila, loss-of-function Imp mutations are zygotic lethal, and mutants die late as pharate adults. Imp has a function in Drosophila oogenesis that is not essential, as well as functions that are essential during embryogenesis and later development. Germline clones of Imp mutations do not block maternal mRNA localization or oocyte development, but overexpression of a specific Imp isoform disrupts dorsal/ventral polarity. We report here that loss-of-function Imp mutations, as well as Imp overexpression, can alter synaptic terminal growth. Our data show that Imp is transported to the neuromuscular junction, where it may modulate the translation of mRNA targets. In oocytes, where Imp function is not essential, we implicate a specific Imp domain in the establishment of dorsoventral polarity.

Indexed as

Alternative SplicingAnimalsAnimals, Genetically ModifiedBase SequenceBiological Transport, ActiveBody PatterningDNA PrimersDrosophilaDrosophila ProteinsFemaleGene ExpressionGenes, InsectGreen Fluorescent ProteinsMaleMutationOogenesisDNA PrimersDrosophila ProteinsGreen Fluorescent ProteinsImp protein, DrosophilaRecombinant Fusion ProteinsRNA-Binding Proteins

Identifiers

PMID18282112
PMCPMC2242817
OpenAlexW1989624726

What OpenQuestion holds

Textmetadata
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.