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ALKBH4-dependent demethylation of actin regulates actomyosin dynamics

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  • Ming-Ming Li

    (Genome Structure and Stability Group, BIG CAS-OSLO Genome Research Cooperation, Disease Genomics and Individualized Medicine Laboratory, Beijing Institute of Genomics, Chinese Academy of Sciences, No. 1–7 Beichen West Road, Chaoyang District
    University of Chinese Academy of Sciences, 19A Yuquan Road, Beijing 100049, China)

  • Anja Nilsen

    (Clinic for Diagnostics and Intervention and Institute of Medical Microbiology, BIG CAS-OSLO Genome Research Cooperation, Oslo University Hospital Rikshospitalet)

  • Yue Shi

    (Genome Structure and Stability Group, BIG CAS-OSLO Genome Research Cooperation, Disease Genomics and Individualized Medicine Laboratory, Beijing Institute of Genomics, Chinese Academy of Sciences, No. 1–7 Beichen West Road, Chaoyang District
    University of Chinese Academy of Sciences, 19A Yuquan Road, Beijing 100049, China)

  • Markus Fusser

    (Clinic for Diagnostics and Intervention and Institute of Medical Microbiology, BIG CAS-OSLO Genome Research Cooperation, Oslo University Hospital Rikshospitalet)

  • Yue-He Ding

    (National Institute of Biological Sciences)

  • Ye Fu

    (The University of Chicago, 929 East 57th Street)

  • Bo Liu

    (Beijing Key Laboratory of DNA Damage Response, College of Life Sciences, Capital Normal University)

  • Yamei Niu

    (Genome Structure and Stability Group, BIG CAS-OSLO Genome Research Cooperation, Disease Genomics and Individualized Medicine Laboratory, Beijing Institute of Genomics, Chinese Academy of Sciences, No. 1–7 Beichen West Road, Chaoyang District)

  • Yong-Sheng Wu

    (Genome Structure and Stability Group, BIG CAS-OSLO Genome Research Cooperation, Disease Genomics and Individualized Medicine Laboratory, Beijing Institute of Genomics, Chinese Academy of Sciences, No. 1–7 Beichen West Road, Chaoyang District)

  • Chun-Min Huang

    (Genome Structure and Stability Group, BIG CAS-OSLO Genome Research Cooperation, Disease Genomics and Individualized Medicine Laboratory, Beijing Institute of Genomics, Chinese Academy of Sciences, No. 1–7 Beichen West Road, Chaoyang District)

  • Maria Olofsson

    (Clinic for Diagnostics and Intervention and Institute of Medical Microbiology, BIG CAS-OSLO Genome Research Cooperation, Oslo University Hospital Rikshospitalet)

  • Kang-Xuan Jin

    (Genome Structure and Stability Group, BIG CAS-OSLO Genome Research Cooperation, Disease Genomics and Individualized Medicine Laboratory, Beijing Institute of Genomics, Chinese Academy of Sciences, No. 1–7 Beichen West Road, Chaoyang District
    University of Chinese Academy of Sciences, 19A Yuquan Road, Beijing 100049, China)

  • Ying Lv

    (Genome Structure and Stability Group, BIG CAS-OSLO Genome Research Cooperation, Disease Genomics and Individualized Medicine Laboratory, Beijing Institute of Genomics, Chinese Academy of Sciences, No. 1–7 Beichen West Road, Chaoyang District
    University of Chinese Academy of Sciences, 19A Yuquan Road, Beijing 100049, China)

  • Xing-Zhi Xu

    (Beijing Key Laboratory of DNA Damage Response, College of Life Sciences, Capital Normal University)

  • Chuan He

    (The University of Chicago, 929 East 57th Street)

  • Meng-Qiu Dong

    (National Institute of Biological Sciences)

  • Jannie M. Rendtlew Danielsen

    (Genome Structure and Stability Group, BIG CAS-OSLO Genome Research Cooperation, Disease Genomics and Individualized Medicine Laboratory, Beijing Institute of Genomics, Chinese Academy of Sciences, No. 1–7 Beichen West Road, Chaoyang District
    The Novo Nordisk Foundation Center for Protein Research, Ubiquitin Signalling Group, Faculty of Health Sciences, Blegdamsvej 3b)

  • Arne Klungland

    (Clinic for Diagnostics and Intervention and Institute of Medical Microbiology, BIG CAS-OSLO Genome Research Cooperation, Oslo University Hospital Rikshospitalet
    Institute of Basic Medical Sciences, University of Oslo, PO Box 1018)

  • Yun-Gui Yang

    (Genome Structure and Stability Group, BIG CAS-OSLO Genome Research Cooperation, Disease Genomics and Individualized Medicine Laboratory, Beijing Institute of Genomics, Chinese Academy of Sciences, No. 1–7 Beichen West Road, Chaoyang District
    University of Chinese Academy of Sciences, 19A Yuquan Road, Beijing 100049, China)

Abstract

Regulation of actomyosin dynamics by post-transcriptional modifications in cytoplasmic actin is still poorly understood. Here we demonstrate that dioxygenase ALKBH4-mediated demethylation of a monomethylated site in actin (K84me1) regulates actin–myosin interaction and actomyosin-dependent processes such as cytokinesis and cell migration. ALKBH4-deficient cells display elevated K84me1 levels. Non-muscle myosin II only interacts with unmethylated actin and its proper recruitment to and interaction with actin depend on ALKBH4. ALKBH4 co-localizes with the actomyosin-based contractile ring and midbody via association with methylated actin. ALKBH4-mediated regulation of actomyosin dynamics is completely dependent on its catalytic activity. Disorganization of cleavage furrow components and multinucleation associated with ALKBH4 deficiency can all be restored by reconstitution with wild-type but not catalytically inactive ALKBH4. Similar to actin and myosin knock-out mice, homozygous Alkbh4 mutant mice display early embryonic lethality. These findings imply that ALKBH4-dependent actin demethylation regulates actomyosin function by promoting actin-non-muscle myosin II interaction.

Suggested Citation

  • Ming-Ming Li & Anja Nilsen & Yue Shi & Markus Fusser & Yue-He Ding & Ye Fu & Bo Liu & Yamei Niu & Yong-Sheng Wu & Chun-Min Huang & Maria Olofsson & Kang-Xuan Jin & Ying Lv & Xing-Zhi Xu & Chuan He & M, 2013. "ALKBH4-dependent demethylation of actin regulates actomyosin dynamics," Nature Communications, Nature, vol. 4(1), pages 1-13, October.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2863
    DOI: 10.1038/ncomms2863
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