Evidence map›Paper›PMID 41039590›Full record

ArticleCell communication and signaling : CCS2025

Reversible arginine methylation of PI3KC2α controls mitotic spindle dynamics.

Yena Cho, Jee Won Hwang, Mark T Bedford, Dong Hee Na, Dae-Geun Song, Su-Nam Kim, Yong Kee Kim

Abstract read
In one paragraph

Article in Cell communication and signaling : CCS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. KDM4A Erases the H3R17me2a Mark, Facilitating Chromosome Condensation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. 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

7 authors.

Yena ChoMuscle Physiome Research Center, Research Institute of Pharmaceutical Sciences, Sookmyung Women's University, Seoul, 04310, Republic of Korea.
Jee Won HwangCollege of Pharmacy, Sookmyung Women's University, Seoul, 04310, Republic of Korea.
Mark T BedfordDepartment of Epigenetics and Molecular Carcinogenesis, The University of Texas MD Anderson Cancer Center, Houston, TX, 77030, USA.
Dong Hee NaCollege of Pharmacy, Chung-Ang University, Seoul, 06974, Republic of Korea.
Dae-Geun SongNatural Products Research Institute, KIST Gangneung, Gangneung, 25451, Republic of Korea.
Su-Nam KimNatural Products Research Institute, KIST Gangneung, Gangneung, 25451, Republic of Korea.
Yong Kee KimMuscle Physiome Research Center, Research Institute of Pharmaceutical Sciences, Sookmyung Women's University, Seoul, 04310, Republic of Korea. yksnbk@sookmyung.ac.kr.

Funding

the National Research Foundation of Korea RS-2024-00412728the National Research Foundation of Korea RS-2025-00563180
6 · The paper itself

Abstract

Microtubules, composed of αβ-tubulin dimers, undergo dynamic polymerization and are fundamental to cell structure and function. In the current study, we discovered that phosphatidylinositol 3-kinase class 2α (PI3KC2α) acts as a novel regulatory factor in microtubule dynamics. Specifically, asymmetric dimethylation of PI3KC2α at the R175 residue (R175me2a) by coactivator-associated arginine methyltransferase 1 (CARM1) enhances its interaction with α-tubulin, stabilizing microtubule assembly. Furthermore, lysine Demethylase 4 A (KDM4A) serves as an arginine demethylase for PI3KC2α R175me2a. During mitosis, protein kinase C (PKC)-mediated phosphorylation of KDM4A results in its dissociation from PI3KC2α, preventing demethylation and increasing R175me2a levels. This facilitates spindle formation and highlights the critical role of reversible arginine methylation in regulating mitotic spindle dynamics. Cumulatively, these findings reveal the coordinated interplay between CARM1 and KDM4A in modulating microtubule behavior through PI3KC2α R175 methylation, offering new insights into the regulatory mechanisms of mitotic progression.

Indexed as

ArgininePhosphatidylinositol 3-KinasesSpindle ApparatusHeLa CellsHumansJumonji Domain-Containing Histone DemethylasesMethylationMicrotubulesMitosisPhosphorylationProtein-Arginine N-MethyltransferasesProtein Kinase CTubulinArgininecoactivator-associated arginine methyltransferase 1Jumonji Domain-Containing Histone DemethylasesKDM4A protein, humanPhosphatidylinositol 3-KinasesProtein-Arginine N-MethyltransferasesProtein Kinase CTubulinAutoregulationCARM1MicrotubuleMitosisPI3KC2αTubulin

Identifiers

PMID41039590
PMCPMC12492571

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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.