Evidence map›Paper›PMID 10662770›Full record

ArticleThe Journal of cell biology2000

Isolation of a ribonucleoprotein complex involved in mRNA localization in Drosophila oocytes.

J E Wilhelm, J Mansfield, N Hom-Booher, S Wang, C W Turck, T Hazelrigg, R D Vale

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
4.4field-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

55 citing papers in PubMed, 141 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. P-body-like condensates in the germline.Seminars in cell & developmental biology · 2024
    Review
  5. Article
  6. Review
  7. Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Review
  9. Translational repression of theRNA (New York, N.Y.) · 2017
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. mRNA localization and translational control in Drosophila oogenesis.Cold Spring Harbor perspectives in biology · 2012
    Review
  17. Review
  18. Article
  19. Article
  20. New insights into the regulation of RNP granule assembly in oocytes.International review of cell and molecular biology · 2012
    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

7 authors at 3 institutions in 1 country.

J E WilhelmDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, California 94143, USA.
J Mansfield
N Hom-Booher
S Wang
C W Turck
T Hazelrigg
R D Vale
Columbia University · USHoward Hughes Medical Institute · USUniversity of California, San Francisco · US

Funding

MICROTUBULE-BASED ORGANELLE TRANSPORTR01GM038499 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI VALE, RONALD D · 1988 to 2005
$1.2M
SUBCELLULAR RNA LOCALIZATION IN DROSOPHILA DEVELOPMENTR01GM048060 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI HAZELRIGG, TULLE · 1993 to 1996
–
SUBCELLULAR RNA LOCALIZATION IN DROSOPHILA DEVELOPMENTR55GM048060 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI HAZELRIGG, TULLE · 1992 to 1992
–
NIGMS NIH HHS GM48060NIGMS NIH HHS GM48499NIGMS NIH HHS R01 GM038499
6 · The paper itself

Abstract

Localization of bicoid (bcd) mRNA to the anterior and oskar (osk) mRNA to the posterior of the Drosophila oocyte is critical for embryonic patterning. Previous genetic studies implicated exuperantia (exu) in bcd mRNA localization, but its role in this process is not understood. We have biochemically isolated Exu and show that it is part of a large RNase-sensitive complex that contains at least seven other proteins. One of these proteins was identified as the cold shock domain RNA-binding protein Ypsilon Schachtel (Yps), which we show binds directly to Exu and colocalizes with Exu in both the oocyte and nurse cells of the Drosophila egg chamber. Surprisingly, the Exu-Yps complex contains osk mRNA. This biochemical result led us to reexamine the role of Exu in the localization of osk mRNA. We discovered that exu-null mutants are defective in osk mRNA localization in both nurse cells and the oocyte. Furthermore, both Exu/Yps particles and osk mRNA follow a similar temporal pattern of localization in which they transiently accumulate at the oocyte anterior and subsequently localize to the posterior pole. We propose that Exu is a core component of a large protein complex involved in localizing mRNAs both within nurse cells and the developing oocyte.

Indexed as

Drosophila ProteinsAmino Acid SequenceAnimalsBinding SitesDNA-Binding ProteinsDrosophila melanogasterEgg ProteinsFemaleHumansInsect ProteinsMolecular Sequence DataMutagenesisOocytesOogenesisRibonuclease, PancreaticRibonucleoproteinsDNA-Binding ProteinsDrosophila ProteinsEgg Proteinsexu protein, DrosophilaInsect Proteinsosk protein, DrosophilaRibonuclease, PancreaticRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerYPS protein, Drosophila

Identifiers

PMID10662770
PMCPMC2174796
OpenAlexW1984261859

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.