Evidence map›Paper›PMID 12215544›Full record

ArticleMolecular and cellular biology2002

Nuclear export and retention signals in the RS domain of SR proteins.

Demian Cazalla, Jun Zhu, Lisa Manche, Elisabeth Huber, Adrian R Krainer, Javier F Cáceres

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

99 citing papers in PubMed, 173 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Multiple types of nuclear localization signals inBiochemistry and biophysics reports · 2024
    Article
  6. Article
  7. Review
  8. Evidence Supporting a Role of Alternative Splicing Participates in Melon (International journal of molecular sciences · 2024
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Exploring the multifunctionality of SR proteins.Biochemical Society transactions · 2022
    Article
  15. Long Noncoding RNAInternational journal of molecular sciences · 2021
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

39 more citing papers are in PubMed but not listed here.

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 2 countries.

Demian CazallaMRC Human Genetics Unit, Western General Hospital, Edinburgh EH4 2XU, Scotland.
Jun Zhu
Lisa Manche
Elisabeth Huber
Adrian R Krainer
Javier F Cáceres
Cold Spring Harbor Laboratory · USWestern General Hospital · GB

Funding

Medical Research Council MC_U127584479
6 · The paper itself

Abstract

Splicing factors of the SR protein family share a modular structure consisting of one or two RNA recognition motifs (RRMs) and a C-terminal RS domain rich in arginine and serine residues. The RS domain, which is extensively phosphorylated, promotes protein-protein interactions and directs subcellular localization and-in certain situations-nucleocytoplasmic shuttling of individual SR proteins. We analyzed mutant versions of human SF2/ASF in which the natural RS repeats were replaced by RD or RE repeats and compared the splicing and subcellular localization properties of these proteins to those of SF2/ASF lacking the entire RS domain or possessing a minimal RS domain consisting of 10 consecutive RS dipeptides (RS10). In vitro splicing of a pre-mRNA that requires an RS domain could take place when the mutant RD, RE, or RS10 domain replaced the natural domain. The RS10 version of SF2/ASF shuttled between the nucleus and the cytoplasm in the same manner as the wild-type protein, suggesting that a tract of consecutive RS dipeptides, in conjunction with the RRMs of SF2/ASF, is necessary and sufficient to direct nucleocytoplasmic shuttling. However, the SR protein SC35 has two long stretches of RS repeats, yet it is not a shuttling protein. We demonstrate the presence of a dominant nuclear retention signal in the RS domain of SC35.

Indexed as

3T3 CellsActive Transport, Cell NucleusAnimalsCell NucleusCytoplasmHeLa CellsHeterogeneous-Nuclear RibonucleoproteinsHumansMiceMolecular Sequence DataMutagenesis, Site-DirectedNuclear ProteinsOrganellesPhosphorylationProtein Structure, TertiaryRibonucleoproteinsHeterogeneous-Nuclear RibonucleoproteinsNuclear ProteinsRibonucleoproteinsRNA-Binding ProteinsSerine-Arginine Splicing FactorsSRSF2 protein, humanSRSF2 protein, mouse

Identifiers

PMID12215544
PMCPMC134038
OpenAlexW2164019525

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.