Evidence map›Paper›PMID 19240134›Full record

ArticleGenes & development2009

Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones.

Xiang-Yang Zhong, Jian-Hua Ding, Joseph A Adams, Gourisankar Ghosh, Xiang-Dong Fu

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed, 1 pooled it
–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

126 citing papers in PubMed, 1 synthesis or guideline pooled it, 234 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
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  5. Article
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  8. Review
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  12. DivergentLife science alliance · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. SR proteins in cancer: function, regulation, and small inhibitor.Cellular & molecular biology letters · 2024
    Review
  18. Article
  19. Article
  20. Article

66 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

5 authors at 1 institution in 1 country.

Xiang-Yang ZhongDepartment of Cellular and Molecular Medicine, University of California at San Diego, La Jolla, California 92093, USA.
Jian-Hua Ding
Joseph A Adams
Gourisankar Ghosh
Xiang-Dong Fu
University of California, San Diego · US

Funding

Role of protein phosphorylation in RNA splicingR01GM067969 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ADAMS, JOSEPH · 2004 to 2024
$6.4M
Regulation of RNA metabolism and cell growth control by SR protein kinasesR01GM052872 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DOWDY, STEVEN F · 1996 to 2019
$5.4M
NIGMS NIH HHS GM52872NIGMS NIH HHS R01 GM052872NIGMS NIH HHS R01 GM067969
6 · The paper itself

Abstract

Phosphorylation is essential for the SR family of splicing factors/regulators to function in constitutive and regulated pre-mRNA splicing; yet both hypo- and hyperphosphorylation of SR proteins are known to inhibit splicing, indicating that SR protein phosphorylation must be tightly regulated in the cell. However, little is known how SR protein phosphorylation might be regulated during development or in response to specific signaling events. Here, we report that SRPK1, a ubiquitously expressed SR protein-specific kinase, directly binds to the cochaperones Hsp40/DNAjc8 and Aha1, which mediate dynamic interactions of the kinase with the major molecular chaperones Hsp70 and Hsp90 in mammalian cells. Inhibition of the Hsp90 ATPase activity induces dissociation of SRPK1 from the chaperone complexes, which can also be triggered by a stress signal (osmotic shock), resulting in translocation of the kinase from the cytoplasm to the nucleus, differential phosphorylation of SR proteins, and alteration of splice site selection. These findings connect the SRPK to the molecular chaperone system that has been implicated in numerous signal transduction pathways and provide mechanistic insights into complex regulation of SR protein phosphorylation and alternative splicing in response to developmental cues and cellular signaling.

Indexed as

Adenosine TriphosphatasesAlternative SplicingDNA, IntergenicHeat-Shock ProteinsHeLa CellsHumansIndicators and ReagentsMolecular ChaperonesNuclear ProteinsPhosphorylationProtein Serine-Threonine KinasesSignal TransductionSorbitolStress, PhysiologicalTwo-Hybrid System TechniquesAdenosine TriphosphatasesDNA, IntergenicHeat-Shock ProteinsIndicators and ReagentsMolecular ChaperonesNuclear ProteinsProtein Serine-Threonine KinasesSorbitolSRPK1 protein, human

Identifiers

PMID19240134
PMCPMC2648651
OpenAlexW2110538588

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.