Evidence map›Paper›PMID 41629283›Full record

ArticleCell death & disease2026

Reversible arginine methylation regulates mitochondrial IDH2 activity: coordinated control by CARM1 and KDM3A/4A.

Yena Cho, Jessica Winarto, Dae-Geun Song, Dong Hee Na, Kyo Bin Kang, Su-Nam Kim, Yong Kee Kim

Abstract read
In one paragraph

Article in Cell death & disease, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

3 citing papers in PubMed.

  1. Article
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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 and Research Institute of Pharmaceutical Sciences, Sookmyung Women's University, Seoul, Republic of Korea.
Jessica WinartoNatural Products Research Institute, KIST Gangneung, Gangneung, Republic of Korea.
Dae-Geun SongNatural Products Research Institute, KIST Gangneung, Gangneung, Republic of Korea.ORCID http://orcid.org/0000-0003-0471-8602
Dong Hee NaCollege of Pharmacy, Chung-Ang University, Seoul, Republic of Korea.ORCID http://orcid.org/0000-0001-9313-0127
Kyo Bin KangMuscle Physiome Research Center and Research Institute of Pharmaceutical Sciences, Sookmyung Women's University, Seoul, Republic of Korea.ORCID http://orcid.org/0000-0003-3290-1017
Su-Nam KimNatural Products Research Institute, KIST Gangneung, Gangneung, Republic of Korea.
Yong Kee KimMuscle Physiome Research Center and Research Institute of Pharmaceutical Sciences, Sookmyung Women's University, Seoul, Republic of Korea. yksnbk@sookmyung.ac.kr.ORCID http://orcid.org/0000-0002-6413-7538

Funding

National Research Foundation of Korea (NRF) RS-2022-NR070845National Research Foundation of Korea (NRF) RS-2024-00412728National Research Foundation of Korea (NRF) RS-2024-00509503National Research Foundation of Korea (NRF) RS-2025-00563180
6 · The paper itself

Abstract

Mitochondria are essential for cellular homeostasis, supplying key metabolites and energy. While post-translational modifications regulate mitochondrial enzymes, their roles remain less explored compared to those in the nucleus and cytoplasm. Here, we demonstrate that reversible arginine methylation governs the activity of several mitochondrial enzymes, with a particular focus on isocitrate dehydrogenase 2 (IDH2). We identify coactivator-associated arginine methyltransferase 1 (CARM1) as a mitochondrial enzyme that asymmetrically dimethylates IDH2 at R188, leading to enzymatic inhibition while enhancing protein stability. This modification is dynamically reversed by the lysine demethylases KDM3A and KDM4A, which restore IDH2 activity. Notably, despite its reduced stability, demethylated IDH2 promotes α-ketoglutarate production, enhancing mitochondrial membrane potential and oxygen consumption. These findings highlight the critical role of reversible arginine methylation in fine-tuning mitochondrial enzyme function and maintaining mitochondrial homeostasis.

Indexed as

ArginineIsocitrate DehydrogenaseJumonji Domain-Containing Histone DemethylasesMitochondriaProtein-Arginine N-MethyltransferasesAnimalsHEK293 CellsHumansKetoglutaric AcidsMembrane Potential, MitochondrialMethylationOxygen ConsumptionProtein Processing, Post-TranslationalArgininecoactivator-associated arginine methyltransferase 1IDH2 protein, humanIsocitrate DehydrogenaseJumonji Domain-Containing Histone DemethylasesKDM3A protein, humanKDM4A protein, humanKetoglutaric AcidsProtein-Arginine N-Methyltransferases

Identifiers

PMID41629283
PMCPMC12877120

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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.