ALKBH4-dependent demethylation of actin regulates actomyosin dynamics

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, Meng-Qiu Dong, Jannie M. Rendtlew Danielsen, Arne Klungland () and Yun-Gui Yang ()
Additional contact information
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
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
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
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
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
Arne Klungland: Clinic for Diagnostics and Intervention and Institute of Medical Microbiology, BIG CAS-OSLO Genome Research Cooperation, Oslo University Hospital Rikshospitalet
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

Nature Communications, 2013, vol. 4, issue 1, 1-13

Abstract: 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.

Date: 2013
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DOI: 10.1038/ncomms2863

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