Evidence map›Paper›PMID 16135820›Full record

ArticleMolecular and cellular biology2005

Multiple properties of the splicing repressor SRp38 distinguish it from typical SR proteins.

Chanseok Shin, Frida E Kleiman, James L Manley

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. When SUMO met splicing.RNA biology · 2018
    Review
  7. Article
  8. Mechanisms of heat shock response in mammals.Cellular and molecular life sciences : CMLS · 2013
    Review
  9. Review
  10. Article
  11. Article
  12. MicroRNA 29c is down-regulated in nasopharyngeal carcinomas, up-regulating mRNAs encoding extracellular matrix proteins.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  13. Article
  14. Article
  15. Article
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 1 institution in 1 country.

Chanseok ShinDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Frida E Kleiman
James L Manley
Columbia University · US

Funding

MECHANISMS OF ALTERNATIVE SPLICING OF PRE MRNAR37GM048259 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI MANLEY, JAMES L. · 1996 to 2005
$2.8M
NIGMS NIH HHS R37 GM048259NIGMS NIH HHS R37 GM48259
6 · The paper itself

Abstract

The SR protein SRp38 is a general splicing repressor that is activated by dephosphorylation during mitosis and in response to heat shock. Here we describe experiments that provide insights into the mechanism by which SRp38 functions in splicing repression. We first show that SRp38 redistributes and colocalizes with snRNPs, but not with a typical SR protein, SC35, during mitosis and following heat shock. Supporting the functional significance of this association, a micrococcal nuclease-sensitive component, i.e., an snRNP(s), completely rescued heat shock-induced splicing repression in vitro, and purified U1 snRNP did so partially. SRp38 contains an N-terminal RNA binding domain (RBD) and a C-terminal RS domain composed of two subdomains (RS1 and RS2 domains). Unexpectedly, an RS1 deletion mutant derivative specifically inhibited the second step of splicing, while an RS2 deletion mutant retained significant dephosphorylation-dependent repression activity. Using chimeric SRp38/SC35 proteins, we show that SC35-RBD/SRp38-RS can function as a general splicing activator and that the dephosphorylated version can act as a strong splicing repressor. SRp38-RBD/SC35-RS, however, was essentially inactive in these assays. Together, our results help to define the unusual features of SRp38 that distinguish it from other SR proteins.

Indexed as

RNA SplicingAmino Acid SequenceCell Cycle ProteinsCells, CulturedCytoplasmHot TemperatureHumansMitosisMolecular Sequence DataNeoplasm ProteinsNuclear ProteinsPhosphorylationProtein Structure, TertiaryRecombinant Fusion ProteinsRepressor ProteinsRibonucleoproteinsCell Cycle ProteinsNeoplasm ProteinsNuclear ProteinsRecombinant Fusion ProteinsRepressor ProteinsRibonucleoproteinsRibonucleoprotein, U1 Small NuclearRNA-Binding ProteinsSerine-Arginine Splicing FactorsSRSF10 protein, humanSRSF2 protein, human

Identifiers

PMID16135820
PMCPMC1234314
OpenAlexW1985846570

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.