Evidence map›Paper›PMID 10490636›Full record

ArticleMolecular and cellular biology1999

The protein kinase Clk/Sty directly modulates SR protein activity: both hyper- and hypophosphorylation inhibit splicing.

J Prasad, K Colwill, T Pawson, J L Manley

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

109 citing papers in PubMed, 226 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Splicing to orchestrate cell fate.Molecular therapy. Nucleic acids · 2025
    Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. RBM20 phosphorylation and its role in nucleocytoplasmic transport and cardiac pathogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022
    Article
  16. RBM20Journal of molecular and cellular cardiology · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. Article

49 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

4 authors at 2 institutions in 1 country.

J PrasadDepartment of Biological Sciences, Columbia University, New York, New York 10027, USA.
K Colwill
T Pawson
J L Manley
Columbia University · USMount Sinai Hospital · US

Funding

MECHANISMS OF ALTERNATIVE SPLICING OF PRE MRNAR01GM048259 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI MANLEY, JAMES L. · 1992 to 2015
$5.2M
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 GM48259NIGMS NIH HHS R01 GM048259NIGMS NIH HHS R37 GM048259
6 · The paper itself

Abstract

The splicing of mammalian mRNA precursors requires both protein phosphorylation and dephosphorylation, likely involving modification of members of the SR protein family of splicing factors. Several kinases have been identified that can phosphorylate SR proteins in vitro, and transfection assays have provided evidence that at least one of these, Clk/Sty, can modulate splicing in vivo. But evidence that a specific kinase can directly affect the splicing activity of SR proteins has been lacking. Here, by using purified recombinant Clk/Sty, a catalytically inactive mutant, and individual SR proteins, we show that Clk/Sty directly affects the activity of SR proteins, but not other essential splicing factors, in reconstituted splicing assays. We also provide evidence that both hyper- and hypophosphorylation inhibit SR protein splicing activity, repressing constitutive splicing and switching alternative splice site selection. These findings indicate that Clk/Sty directly and specifically influences the activity of SR protein splicing factors and, importantly, show that both under- and overphosphorylation of SR proteins can modulate splicing.

Indexed as

Alternative SplicingRibonucleoproteinsNuclear ProteinsPhosphoproteinsPhosphorylationProtein Serine-Threonine KinasesProtein-Tyrosine KinasesRNA-Binding ProteinsSerine-Arginine Splicing FactorsClk dual-specificity kinasesNuclear ProteinsPhosphoproteinsProtein Serine-Threonine KinasesProtein-Tyrosine KinasesRibonucleoproteinsRNA-Binding ProteinsSerine-Arginine Splicing Factors

Identifiers

PMID10490636
PMCPMC84694
OpenAlexW2099184569

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.