Evidence map›Paper›PMID 38923463›Full record

ArticleCell reports2024

CK2 phosphorylation of CMTR1 promotes RNA cap formation and influenza virus infection.

Radoslaw Lukoszek, Francisco Inesta-Vaquera, Natasha J M Brett, Shang Liang, Lydia A Hepburn, David J Hughes, Chiara Pirillo, Edward W Roberts, Victoria H Cowling

Abstract read
In one paragraph

Article in Cell reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Discovery of new aurone derivatives as submicromolar CK2 inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

9 authors.

Radoslaw LukoszekSchool of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Francisco Inesta-VaqueraSchool of Life Sciences, University of Dundee, Dundee DD1 5EH, UK; Department of Biochemistry and Molecular Biology and Genetics, School of Sciences, Universidad de Extremadura, Avenida de Elvas, s/n, 06006 Badajoz, Spain.
Natasha J M BrettSchool of Life Sciences, University of Dundee, Dundee DD1 5EH, UK; Cancer Research UK Scotland Institute, Garscube Estate, Switchback Road, Glasgow G61 1BD, UK; School of Cancer Sciences, University of Glasgow, Garscube Estate, Switchback Road, Glasgow G61 1QH, UK.
Shang LiangCancer Research UK Scotland Institute, Garscube Estate, Switchback Road, Glasgow G61 1BD, UK.
Lydia A HepburnCancer Research UK Scotland Institute, Garscube Estate, Switchback Road, Glasgow G61 1BD, UK.
David J HughesSchool of Biology, University of St Andrews, Biomedical Sciences Research Complex, St Andrews KY16 9ST, UK.
Chiara PirilloCancer Research UK Scotland Institute, Garscube Estate, Switchback Road, Glasgow G61 1BD, UK.
Edward W RobertsCancer Research UK Scotland Institute, Garscube Estate, Switchback Road, Glasgow G61 1BD, UK; School of Cancer Sciences, University of Glasgow, Garscube Estate, Switchback Road, Glasgow G61 1QH, UK.
Victoria H CowlingSchool of Life Sciences, University of Dundee, Dundee DD1 5EH, UK; Cancer Research UK Scotland Institute, Garscube Estate, Switchback Road, Glasgow G61 1BD, UK; School of Cancer Sciences, University of Glasgow, Garscube Estate, Switchback Road, Glasgow G61 1QH, UK. Electronic address: victoria.cowling@glasgow.ac.uk.

Funding

Medical Research Council MR/K024213/1
6 · The paper itself

Abstract

The RNA cap methyltransferase CMTR1 methylates the first transcribed nucleotide of RNA polymerase II transcripts, impacting gene expression mechanisms, including during innate immune responses. Using mass spectrometry, we identify a multiply phosphorylated region of CMTR1 (phospho-patch [P-Patch]), which is a substrate for the kinase CK2 (casein kinase II). CMTR1 phosphorylation alters intramolecular interactions, increases recruitment to RNA polymerase II, and promotes RNA cap methylation. P-Patch phosphorylation occurs during the G1 phase of the cell cycle, recruiting CMTR1 to RNA polymerase II during a period of rapid transcription and RNA cap formation. CMTR1 phosphorylation is required for the expression of specific RNAs, including ribosomal protein gene transcripts, and promotes cell proliferation. CMTR1 phosphorylation is also required for interferon-stimulated gene expression. The cap-snatching virus, influenza A, utilizes host CMTR1 phosphorylation to produce the caps required for virus production and infection. We present an RNA cap methylation control mechanism whereby CK2 controls CMTR1, enhancing co-transcriptional capping.

Indexed as

Casein Kinase IIMethyltransferasesRNA CapsAnimalsHEK293 CellsHumansInfluenza A virusInfluenza, HumanMethylationPhosphorylationRNA Polymerase IICasein Kinase IICMTR1 protein, humanMethyltransferasesRNA CapsRNA Polymerase IIcell proliferationCMTR1CP: MicrobiologyCP: Molecular biologyinfluenza virusinnate immunityribosomesRNARNA captranscriptiontranslation

Identifiers

PMID38923463
PMCPMC11290353

What Socratic 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 Socratic graph.