Evidence map›Paper›PMID 9420331›Full record

ArticleGenes & development1998

A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm.

J F Cáceres, G R Screaton, A R Krainer

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 228 papers.

0numbers the graph read from it
0cells of the map it votes in
228citing papers in PubMed
–field-weighted citation impact
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

228 citing papers in PubMed, 486 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. The serine-arginine (SR) protein UmRrm75 from Ustilago maydis is a functional ortholog of yeast ScHrb1.International microbiology : the official journal of the Spanish Society for Microbiology · 2024
    Article
  11. Article
  12. SRSF1 interactome determined by proximity labeling reveals direct interaction with spliceosomal RNA helicase DDX23.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Oncogenic SRSF3 in health and diseases.International journal of biological sciences · 2023
    Review
  18. Article
  19. Article
  20. Article

168 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

3 authors at 2 institutions in 2 countries.

J F CáceresCold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724-2208, USA.
G R Screaton
A R Krainer
Cold Spring Harbor Laboratory · USJohn Radcliffe Hospital · GB

Funding

VIRAL TRANSACTIVATIONP01CA013106 · NCI · COLD SPRING HARBOR LABORATORY · PI William Richard McCombie · 1985 to 2026
$116.8M
NCI NIH HHS CA13106NCI NIH HHS P01 CA013106Wellcome Trust
6 · The paper itself

Abstract

The SR proteins constitute a large family of nuclear phosphoproteins required for constitutive pre-mRNA splicing. These factors also have global, concentration-dependent effects on alternative splicing regulation and this activity is antagonized by members of the hnRNP A/B family of proteins. We show here that whereas some human SR proteins are confined to the nucleus, three of them-SF2/ASF, SRp20, and 9G8-shuttle rapidly and continuously between the nucleus and the cytoplasm. By swapping the corresponding domains between shuttling and nonshuttling SR proteins, we show that the carboxy-terminal arginine/serine-rich (RS) domain is required for shuttling. This domain, however, is not sufficient to promote shuttling of an unrelated protein reporter, suggesting that stable RNA binding mediated by the RNA-recognition motifs may be required for shuttling. Consistent with such a requirement, a double point-mutation in RRM1 of SF2/ASF that impairs RNA binding prevents the protein from shuttling. In addition, we show that phosphorylation of the RS domain affects the shuttling properties of SR proteins. These findings show that different SR proteins have unique intracellular transport properties and suggest that the family members that shuttle may have roles not only in nuclear pre-mRNA splicing but also in mRNA transport, cytoplasmic events, and/or processes that involve communication between the nucleus and the cytoplasm.

Indexed as

Nucleocytoplasmic Transport Proteins3T3 CellsAnimalsBinding SitesBiological TransportCell NucleusCytoplasmHeLa CellsHeterogeneous-Nuclear RibonucleoproteinsHumansMiceNuclear ProteinsPhosphoproteinsPhosphorylationRibonucleoproteinsRNA-Binding ProteinsHeterogeneous-Nuclear RibonucleoproteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsPhosphoproteinsRibonucleoproteinsRNA-Binding ProteinsSerine-Arginine Splicing FactorsSRSF2 protein, humanSRSF2 protein, mouseSRSF3 protein, humanSrsf3 protein, mouse

Identifiers

PMID9420331
PMCPMC316398
OpenAlexW2138647063

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.