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KAT2A coupled with the α-KGDH complex acts as a histone H3 succinyltransferase

Author

Listed:
  • Yugang Wang

    (Brain Tumor Center, The University of Texas MD Anderson Cancer Center)

  • Yusong R. Guo

    (Rice University)

  • Ke Liu

    (University of California)

  • Zheng Yin

    (Houston Methodist Research Institute)

  • Rui Liu

    (Brain Tumor Center, The University of Texas MD Anderson Cancer Center)

  • Yan Xia

    (Brain Tumor Center, The University of Texas MD Anderson Cancer Center)

  • Lin Tan

    (The University of Texas MD Anderson Cancer Center)

  • Peiying Yang

    (The University of Texas MD Anderson Cancer Center)

  • Jong-Ho Lee

    (Brain Tumor Center, The University of Texas MD Anderson Cancer Center)

  • Xin-jian Li

    (Brain Tumor Center, The University of Texas MD Anderson Cancer Center)

  • David Hawke

    (The University of Texas MD Anderson Cancer Center)

  • Yanhua Zheng

    (Brain Tumor Center, The University of Texas MD Anderson Cancer Center)

  • Xu Qian

    (People’s Hospital of Hangzhou Medical College)

  • Jianxin Lyu

    (People’s Hospital of Hangzhou Medical College
    Key Laboratory of Laboratory Medicine, Ministry of Education of China, School of Laboratory Medicine and Life Science, Wenzhou Medical University)

  • Jie He

    (Laboratory of Thoracic Surgery, Cancer Institute and Hospital, Chinese Academy of Medical Sciences, Peking Union Medical College)

  • Dongming Xing

    (Cancer Institute, The Affiliated Hospital of Qingdao University
    Qingdao Cancer Institute
    School of Life Sciences, Tsinghua University)

  • Yizhi Jane Tao

    (Rice University)

  • Zhimin Lu

    (Brain Tumor Center, The University of Texas MD Anderson Cancer Center
    The University of Texas MD Anderson Cancer Center
    MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences, The University of Texas)

Abstract

The histone acetyl transferase KAT2A (also known as GCN5) can also catalyse histone succinylation, with the α-KGDH complex providing a local source of succinyl-CoA.

Suggested Citation

  • Yugang Wang & Yusong R. Guo & Ke Liu & Zheng Yin & Rui Liu & Yan Xia & Lin Tan & Peiying Yang & Jong-Ho Lee & Xin-jian Li & David Hawke & Yanhua Zheng & Xu Qian & Jianxin Lyu & Jie He & Dongming Xing , 2017. "KAT2A coupled with the α-KGDH complex acts as a histone H3 succinyltransferase," Nature, Nature, vol. 552(7684), pages 273-277, December.
    • Handle: RePEc:nat:nature:v:552:y:2017:i:7684:d:10.1038_nature25003
    DOI: 10.1038/nature25003
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    Cited by:

    1. Bo Yu & Jun Su & Qiqi Shi & Qing Liu & Jun Ma & Guoqing Ru & Lei Zhang & Jian Zhang & Xichun Hu & Jianming Tang, 2022. "KMT5A-methylated SNIP1 promotes triple-negative breast cancer metastasis by activating YAP signaling," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    2. Ziping Niu & Chen Chen & Siyu Wang & Congcong Lu & Zhiyue Wu & Aiyuan Wang & Jing Mo & Jianji Zhang & Yanpu Han & Ye Yuan & Yingao Zhang & Yong Zang & Chaoran He & Xue Bai & Shanshan Tian & Guijin Zha, 2024. "HBO1 catalyzes lysine lactylation and mediates histone H3K9la to regulate gene transcription," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    3. Yitang Zhang & Maofei Chen & Xudong Chen & Minghui Zhang & Jian Yin & Zi Yang & Xin Gao & Sensen Zhang & Maojun Yang, 2024. "Molecular architecture of the mammalian 2-oxoglutarate dehydrogenase complex," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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