Evidence map›Paper›PMID 40841441›Full record

ArticleCommunications biology2025

Kinase activity of DYRK family members is required for regulating primary cilium length, stability and morphology.

Melis D Arslanhan, Ebru Topçu, Elif Nur Firat-Karalar

Abstract read
In one paragraph

Article in Communications biology, 2025. 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

3 authors.

Melis D ArslanhanDepartment of Molecular Biology and Genetics, Koç University, Istanbul, Turkey.
Ebru TopçuDepartment of Molecular Biology and Genetics, Koç University, Istanbul, Turkey.
Elif Nur Firat-KaralarDepartment of Molecular Biology and Genetics, Koç University, Istanbul, Turkey. ekaralar@ku.edu.tr.ORCID http://orcid.org/0000-0001-7589-473X

Funding

EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) 101078097European Molecular Biology Organization (EMBO) YIP2019Istanbul Kalkinma Ajansi (Istanbul Development Agency) YEP57Türkiye Bilimsel ve Teknolojik Araştirma Kurumu (Scientific and Technological Research Council of Turkey) 123C357Türkiye Bilimsel ve Teknolojik Araştirma Kurumu (Scientific and Technological Research Council of Turkey) 124Z381
6 · The paper itself

Abstract

The dual-specificity tyrosine-phoshorylation-regulated kinase (DYRK) family are multifunctional enzymes crucial for diverse cellular processes, including signaling through the primary cilium. Their dysregulation has been implicated in various cancers and developmental disorders, highlighting the need to define their interactors and cellular functions to inform targeted therapeutics. In this study, we generate the proximity interactome of DYRK3, identifying 178 proteins involved in a range of cellular processes, including primary cilium biogenesis. We then investigate the specific role of DYRK3 and its cooperation with other DYRK family members in cilium assembly and maintenance. RNAi-mediated depletion of DYRK3 and pharmacological inhibition of DYRK kinase activity using GSK-626616 (GSK) lead to elongation of the cilium, particularly its distal segment. GSK treatment also induces ciliary defects, length fluctuations, and increased ectocytosis. Co-depletion and phenotypic rescue experiments reveal that DYRK2 and DYRK3 cooperate in regulating cilium length. Moreover, inhibiting or depleting known cilium length regulators, or quantifying their ciliary levels in GSK-treated cells, reveal functional relationships of DYRKs to centriolar satellites and the IFT complex. Collectively, our findings uncover regulatory roles for DYRK3 and DYRK kinase activity in the assembly and maintenance of primary cilium with proper length, stability, and morphology.

Indexed as

CiliaProtein Serine-Threonine KinasesProtein-Tyrosine KinasesAnimalsDyrk KinasesHumansDyrk KinasesProtein Serine-Threonine KinasesProtein-Tyrosine Kinases

Identifiers

PMID40841441
PMCPMC12371027

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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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.