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Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics

Author

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  • Zhen Chen

    (The University of Texas MD Anderson Cancer Center)

  • Caoqi Lei

    (Wuhan University)

  • Chao Wang

    (The University of Texas MD Anderson Cancer Center)

  • Nan Li

    (The University of Texas MD Anderson Cancer Center)

  • Mrinal Srivastava

    (The University of Texas MD Anderson Cancer Center)

  • Mengfan Tang

    (The University of Texas MD Anderson Cancer Center)

  • Huimin Zhang

    (The University of Texas MD Anderson Cancer Center)

  • Jong Min Choi

    (Baylor College of Medicine)

  • Sung Yun Jung

    (Baylor College of Medicine)

  • Jun Qin

    (Baylor College of Medicine)

  • Junjie Chen

    (The University of Texas MD Anderson Cancer Center)

Abstract

AMP-activated protein kinase (AMPK) is a key regulator of cellular energy homeostasis. Although AMPK has been studied extensively in cellular processes, understanding of its substrates and downstream functional network, and their contributions to cell fate and disease development, remains incomplete. To elucidate the AMPK-dependent signaling pathways, we performed global quantitative phosphoproteomic analysis using wild-type and AMPKα1/α2-double knockout cells and discovered 160 AMPK-dependent phosphorylation sites. Further analysis using an AMPK consensus phosphorylation motif indicated that 32 of these sites are likely direct AMPK phosphorylation sites. We validated one uncharacterized protein, ARMC10, and demonstrated that the S45 site of ARMC10 can be phosphorylated by AMPK both in vitro and in vivo. Moreover, ARMC10 overexpression was sufficient to promote mitochondrial fission, whereas ARMC10 knockout prevented AMPK-mediated mitochondrial fission. These results demonstrate that ARMC10 is an effector of AMPK that participates in dynamic regulation of mitochondrial fission and fusion.

Suggested Citation

  • Zhen Chen & Caoqi Lei & Chao Wang & Nan Li & Mrinal Srivastava & Mengfan Tang & Huimin Zhang & Jong Min Choi & Sung Yun Jung & Jun Qin & Junjie Chen, 2019. "Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics," Nature Communications, Nature, vol. 10(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-018-08004-0
    DOI: 10.1038/s41467-018-08004-0
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    Cited by:

    1. Yingfeng Tu & Qin Yang & Min Tang & Li Gao & Yuanhao Wang & Jiuqiang Wang & Zhe Liu & Xiaoyu Li & Lejiao Mao & Rui zhen Jia & Yuan Wang & Tie-shan Tang & Pinglong Xu & Yan Liu & Lunzhi Dai & Da Jia, 2024. "TBC1D23 mediates Golgi-specific LKB1 signaling," Nature Communications, Nature, vol. 15(1), pages 1-21, December.

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