Evidence map›Paper›PMID 41636961›Full record

ReviewCellular oncology (Dordrecht, Netherlands)2026

Decoding SR protein regulation: kinases, phosphatases, and therapeutic targeting strategies.

Nasi Liu, Fleur van der Ende, Bob van de Water, Sylvia E Le Dévédec

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Cellular oncology (Dordrecht, Netherlands), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Review
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.

Nasi LiuDivision of Cell Systems and Drug Safety, Leiden Academic Centre for Drug Research (LACDR), Leiden University, Einsteinweg 55, Leiden, 2333 CC, The Netherlands.ORCID https://orcid.org/0000-0002-2119-2190
Fleur van der EndeDivision of Cell Systems and Drug Safety, Leiden Academic Centre for Drug Research (LACDR), Leiden University, Einsteinweg 55, Leiden, 2333 CC, The Netherlands.ORCID http://orcid.org/0009-0001-2980-3291
Bob van de WaterDivision of Cell Systems and Drug Safety, Leiden Academic Centre for Drug Research (LACDR), Leiden University, Einsteinweg 55, Leiden, 2333 CC, The Netherlands.ORCID http://orcid.org/0000-0002-5839-2380
Sylvia E Le DévédecDivision of Cell Systems and Drug Safety, Leiden Academic Centre for Drug Research (LACDR), Leiden University, Einsteinweg 55, Leiden, 2333 CC, The Netherlands. s.e.ledevedec@lacdr.leidenuniv.nl.ORCID http://orcid.org/0000-0002-0615-9616

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA splicing is a fundamental cellular process that transforms precursor messenger RNA (pre-mRNA) into mature messenger RNA (mRNA) by removing non-coding introns and rejoining coding exons. Serine/arginine-rich (SR) proteins, a family of RNA-binding proteins, play crucial roles in RNA splicing by recruiting essential components for spliceosome assembly. The activity of SR proteins is tightly regulated by post-translational modifications, including phosphorylation, acetylation, methylation, and ubiquitination. Among these, the dynamic balance between phosphorylation and dephosphorylation is particularly critical for modulating SR protein function. Given their involvement in cancer, SR proteins represent promising targets for therapeutic intervention. In this review, we provide a comprehensive overview of the current understanding of the regulatory networks involving kinases and phosphatases governing SR protein phosphorylation. We also discuss the existing therapeutic strategies using small-molecule inhibitors aimed at regulating SR protein phosphorylation in the context of cancer. In conclusion, this review highlights the importance of phosphorylation regulation in SR protein function and the RNA splicing process. Targeting SR protein phosphorylation may open new therapeutic avenues or enhance the efficacy of cancer treatments when used in combination with other drugs.

Indexed as

Molecular Targeted TherapyPhosphoric Monoester HydrolasesPhosphotransferasesProtein KinasesRNA-Binding ProteinsSerine-Arginine Splicing FactorsAnimalsHumansNeoplasmsPhosphorylationProtein Processing, Post-TranslationalRNA SplicingPhosphoric Monoester HydrolasesPhosphotransferasesProtein KinasesRNA-Binding ProteinsSerine-Arginine Splicing FactorsCancerPhosphorylationRNA splicingSR proteins

Identifiers

PMID41636961
PMCPMC12872631

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.