In one paragraphArticle in Journal of cell science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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 registryThe 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 literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what moneyAuthors and funding
16 authors.
Anne L AshfordSignalling Programme, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Suzan BerSignalling Programme, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.ORCID 0000-0003-4219-6032 Miriam S EmsPhilipps-University Marburg, Clinic of Gastroenterology, Endocrinology, and Metabolism, Center for Tumor and Immune Biology, Hans-Meerwein-Str. 3, 35043 Marburg, Germany.ORCID 0009-0007-4437-3270 Emma DuncanSignalling Programme, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.ORCID 0009-0002-4863-9623 Kathryn BalmannoSignalling Programme, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.ORCID 0000-0002-6417-3889 Hannah ReevesSignalling Programme, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.ORCID 0000-0003-3473-3782 Rachael HuntlySignalling Programme, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Megan A CassidySignalling Programme, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.ORCID 0000-0001-5400-8655 Harvey E JohnstonSignalling Programme, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.ORCID 0000-0001-7032-0227 David OxleyProteomics Facility, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.
Thaddeus Mutugi NthigaMolecular Cancer Research Group, Department of Medical Biology, Faculty of Health Sciences, UiT-The Arctic University of Norway, 9037 Tromsø, Norway.ORCID 0000-0002-6537-3903 Terje JohansenMolecular Cancer Research Group, Department of Medical Biology, Faculty of Health Sciences, UiT-The Arctic University of Norway, 9037 Tromsø, Norway.ORCID 0000-0003-1451-9578 Marie KlugePhilipps-University Marburg, Clinic of Gastroenterology, Endocrinology, and Metabolism, Center for Tumor and Immune Biology, Hans-Meerwein-Str. 3, 35043 Marburg, Germany.
Ralf JacobDepartment of Molecular Cell Biology, Philipps-University Marburg, 35032 Marburg, Germany.
Matthias LauthPhilipps-University Marburg, Clinic of Gastroenterology, Endocrinology, and Metabolism, Center for Tumor and Immune Biology, Hans-Meerwein-Str. 3, 35043 Marburg, Germany.ORCID 0000-0001-5922-5384 Simon J CookSignalling Programme, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, UK.ORCID 0000-0001-9087-1616 Funding
AstraZenecaBabraham InstituteBBSRC BB/L008793/1Biotechnology and Biological Sciences Research Council BB/L008793/1Biotechnology and Biological Sciences Research Council BB/P007015/1Biotechnology and Biological Sciences Research Council BBS/E/B/000C0417Biotechnology and Biological Sciences Research Council BBS/E/B/000C0433Deutsche Forschungsgemeinschaft LA2829/15-1German Research Foundation JP18H02261UK Research and Innovation
6 · The paper itselfAbstract
Dual-specificity tyrosine-phosphorylation-regulated kinase 1B (DYRK1B) modulates the cell cycle and cell fate during development, and is deregulated in cancer and metabolic syndrome. However, only a few DYRK1B substrates have been defined, so we undertook a phosphoproteomics screen in cells that exhibit inducible DYRK1B expression. Motif analysis revealed enrichment for proline-directed serine or threonine phosphorylation sites (pSer-Pro or pThr-Pro), consistent with the consensus motif of class I DYRKs. Gene Ontology (GO) analysis revealed enrichment of proteins involved in mRNA binding, mRNA processing and ribonucleoprotein complexes. Several processing body (PB) components, including DCP1A, PATL1 (PAT1B), EDC3 and 4E-T (also known as EIF4ENIF1), were identified as DYRK1B-inducible phosphoproteins. DYRK1B also co-immunoprecipitated with DCP1A, PAT1B, EDC3, EDC4, DDX6 and XRN1. Super-resolution microscopy demonstrated that DYRK1B co-localised with DCP1A, DCP1B and DDX6 in PBs. Expression of DYRK1B increased PB abundance, whereas inhibition, depletion or knockout of DYRK1B reduced phosphorylation of DCP1A and 4E-T and decreased PB number. Re-expression of wild-type but not kinase-dead DYRK1B restored PB numbers in knockout cells. These findings reveal novel DYRK1B targets and establish DYRK1B as a regulator of PB abundance.
Indexed as
PhosphoproteinsProcessing BodiesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProteomicsDyrk KinasesEndoribonucleasesHumansPhosphorylationDyrk KinasesEndoribonucleasesPhosphoproteinsProtein Serine-Threonine KinasesProtein-Tyrosine KinasesCondensatesDCP1ADYRK1BPhosphoproteomicsProcessing bodiesRNA granules
Identifiers
PMID42592723
PMCPMC13615683
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