Evidence map›Paper›PMID 15611175›Full record

ArticleGenetics2004

The Drosophila U1-70K protein is required for viability, but its arginine-rich domain is dispensable.

Helen K Salz, Ricardo S Y Mancebo, Alexis A Nagengast, Olga Speck, Mitchell Psotka, Stephen M Mount

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

14 citing papers in PubMed, 28 citations in OpenAlex.

  1. Bourbon and Mycbp function with Otu to promote Sxl protein expression in theProceedings of the National Academy of Sciences of the United States of America · 2025
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  7. Xio is a component of theProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. Review
  9. spenito is required for sex determination in Drosophila melanogaster.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  10. Article
  11. Review
  12. Article
  13. Evolution of an RNP assembly system: a minimal SMN complex facilitates formation of UsnRNPs in Drosophila melanogaster.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  14. 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

6 authors at 3 institutions in 1 country.

Helen K SalzDepartment of Genetics, Case Western Reserve University, Cleveland, Ohio 44106-4955, USA. helen.salz@case.edu <helen.salz@case.edu>
Ricardo S Y Mancebo
Alexis A Nagengast
Olga Speck
Mitchell Psotka
Stephen M Mount
University of Maryland, College Park · USCase Western Reserve University · USColumbia University · US

Funding

TRAINING IN NORMAL AND ABNORMAL DEVELOPMENTT32HD007104 · NICHD · CASE WESTERN RESERVE UNIVERSITY · PI HARTE, PETER J. · 1985 to 2010
$3.5M
Regulation of Sex-lethal pre-mRNA splicing during Drosophila developmentR01GM061039 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI SALZ, HELEN KAREN · 2002 to 2010
$2.5M
NICHD NIH HHS HD07104NICHD NIH HHS T32 HD007104NIGMS NIH HHS GM37991NIGMS NIH HHS GM61039NIGMS NIH HHS R01 GM061039
6 · The paper itself

Abstract

The conserved spliceosomal U1-70K protein is thought to play a key role in RNA splicing by linking the U1 snRNP particle to regulatory RNA-binding proteins. Although these protein interactions are mediated by repeating units rich in arginines and serines (RS domains) in vitro, tests of this domain's importance in intact multicellular organisms have not been carried out. Here we report a comprehensive genetic analysis of U1-70K function in Drosophila. Consistent with the idea that U1-70K is an essential splicing factor, we find that loss of U1-70K function results in lethality during embryogenesis. Surprisingly, and contrary to the current view of U1-70K function, animals carrying a mutant U1-70K protein lacking the arginine-rich domain, which includes two embedded sets of RS dipeptide repeats, have no discernible mutant phenotype. Through double-mutant studies, however, we show that the U1-70K RS domain deletion no longer supports viability when combined with a viable mutation in another U1 snRNP component. Together our studies demonstrate that while the protein interactions mediated by the U1-70K RS domain are not essential for viability, they nevertheless contribute to an essential U1 snRNP function.

Indexed as

Amino Acid SequenceAnimalsAnimals, Genetically ModifiedArginineDrosophilaDrosophila ProteinsMolecular Sequence DataMutationProtein Structure, TertiaryRibonucleoprotein, U1 Small NuclearRNA-Binding ProteinsArginineDrosophila ProteinsRibonucleoprotein, U1 Small NuclearRNA-Binding Proteinssnf protein, DrosophilaSNRNP70 protein, humansnRNP-U1-70K protein, Drosophila

Identifiers

PMID15611175
PMCPMC1448718
OpenAlexW2161586678

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.