Evidence map›Paper›PMID 36537190›Full record

ArticleNucleic acids research2022

Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions.

Idir Malki, Inara Liepina, Nora Kogelnik, Hollie Watmuff, Sue Robinson, Adam Lightfoot, Oksana Gonchar, Andrew Bottrill, Andrew M Fry, Cyril Dominguez

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 17 citations in OpenAlex.

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  8. Review
  9. Role of Sam68 in different types of cancer (Review).International journal of molecular medicine · 2025
    Review
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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

10 authors at 2 institutions in 1 country.

Idir MalkiThe Leicester Institute of Structural and Chemical Biology and Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 7RH, UK.
Inara LiepinaThe Leicester Institute of Structural and Chemical Biology and Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 7RH, UK.
Nora KogelnikThe Leicester Institute of Structural and Chemical Biology and Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 7RH, UK.
Hollie WatmuffThe Leicester Institute of Structural and Chemical Biology and Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 7RH, UK.
Sue RobinsonThe Leicester Institute of Structural and Chemical Biology and Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 7RH, UK.
Adam LightfootThe Leicester Institute of Structural and Chemical Biology and Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 7RH, UK.
Oksana GoncharThe Leicester Institute of Structural and Chemical Biology and Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 7RH, UK.
Andrew BottrillProteomics RTP, School of Life Sciences, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, UK.
Andrew M FryDepartment of Molecular and Cell Biology, University of Leicester, Leicester LE1 7RH, UK.
Cyril DominguezThe Leicester Institute of Structural and Chemical Biology and Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 7RH, UK.ORCID 0000-0003-3575-8922
University of Leicester · GBUniversity of Warwick · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council MC_PC_16051
6 · The paper itself

Abstract

Sam68, also known as KHDRBS1, is a member of the STAR family of proteins that directly link signal transduction with post-transcriptional gene regulation. Sam68 controls the alternative splicing of many oncogenic proteins and its role is modulated by post-translational modifications, including serine/threonine phosphorylation, that differ at various stages of the cell cycle. However, the molecular basis and mechanisms of these modulations remain largely unknown. Here, we combined mass spectrometry, nuclear magnetic resonance spectroscopy and cell biology techniques to provide a comprehensive post-translational modification mapping of Sam68 at different stages of the cell cycle in HEK293 and HCT116 cells. We established that Sam68 is specifically phosphorylated at T33 and T317 by Cdk1, and demonstrated that these phosphorylation events reduce the binding of Sam68 to RNA, control its cellular localization and reduce its alternative splicing activity, leading to a reduction in the induction of apoptosis and an increase in the proliferation of HCT116 cells.

Indexed as

Adaptor Proteins, Signal TransducingAlternative SplicingCDC2 Protein KinaseCell Cycle ProteinsDNA-Binding ProteinsHCT116 CellsHEK293 CellsHumansPhosphorylationRNARNA-Binding ProteinsAdaptor Proteins, Signal TransducingCDC2 Protein KinaseCDK1 protein, humanCell Cycle ProteinsDNA-Binding ProteinsKHDRBS1 protein, humanRNARNA-Binding Proteins

Identifiers

PMID36537190
PMCPMC9825155
OpenAlexW4312019904

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.