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Yanmin Guo, Yuqin Zhao, Yu-Sheng Cong. Met1-linked ubiquitination in cell signaling regulation. Biophysics Reports. doi: 10.52601/bpr.2024.230030
Citation: Yanmin Guo, Yuqin Zhao, Yu-Sheng Cong. Met1-linked ubiquitination in cell signaling regulation. Biophysics Reports. doi: 10.52601/bpr.2024.230030

Met1-linked ubiquitination in cell signaling regulation

doi: 10.52601/bpr.2024.230030
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  • Corresponding author: gmy631@163.com (Y. Guo); yscong@hznu.edu.cn (Y.-S. Cong)
  • Received Date: 30 October 2023
  • Accepted Date: 11 March 2024
  • Available Online: 02 April 2024
  • Met1-linked ubiquitination (Met1-Ub), also known as linear ubiquitination, is a newly identified atypical type of polyubiquitination that is assembled via the N-terminal methionine (Met1) rather than an internal lysine (Lys) residue of ubiquitin. The linear ubiquitin chain assembly complex (LUBAC) composed of HOIP, HOIL-1L and SHARPIN is the sole E3 ubiquitin ligase that specifically generates Met1-linked ubiquitin chains. The physiological role of LUBAC-mediated Met1-Ub has been first described as activating NF-κB signaling through the Met1-Ub modification of NEMO. However, accumulating evidence shows that Met1-Ub is broadly involved in other cellular pathways including MAPK, Wnt/β-Catenin, PI3K/AKT and interferon signaling, and participates in various cellular processes including angiogenesis, protein quality control and autophagy, suggesting that Met1-Ub harbors a potent signaling capacity. Here, we review the formation and cellular functions of Met1-linked ubiquitin chains, with an emphasis on the recent advances in the cellular mechanisms by which Met1-Ub controls signaling transduction.

  • Yanmin Guo, Yuqin Zhao and Yu-Sheng Cong declare that they have no conflict of interest.
    This article does not contain any studies with human or animal subjects performed by any of the authors.

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