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An integrated bioinformatics platform for investigating the human E3 ubiquitin ligase-substrate interaction network

Author

Listed:
  • Yang Li

    (National Center for Protein Sciences (The PHOENIX Center, Beijing))

  • Ping Xie

    (National Center for Protein Sciences (The PHOENIX Center, Beijing)
    Capital Medical University)

  • Liang Lu

    (National Center for Protein Sciences (The PHOENIX Center, Beijing))

  • Jian Wang

    (National Center for Protein Sciences (The PHOENIX Center, Beijing))

  • Lihong Diao

    (National Center for Protein Sciences (The PHOENIX Center, Beijing)
    Guangxi University for Nationalities)

  • Zhongyang Liu

    (National Center for Protein Sciences (The PHOENIX Center, Beijing))

  • Feifei Guo

    (National Center for Protein Sciences (The PHOENIX Center, Beijing))

  • Yangzhige He

    (National Center for Protein Sciences (The PHOENIX Center, Beijing))

  • Yuan Liu

    (National Center for Protein Sciences (The PHOENIX Center, Beijing))

  • Qin Huang

    (Guangxi University for Nationalities)

  • Han Liang

    (The University of Texas MD Anderson Cancer Center)

  • Dong Li

    (National Center for Protein Sciences (The PHOENIX Center, Beijing))

  • Fuchu He

    (National Center for Protein Sciences (The PHOENIX Center, Beijing))

Abstract

The ubiquitination mediated by ubiquitin activating enzyme (E1), ubiquitin conjugating enzyme (E2), and ubiquitin ligase (E3) cascade is crucial to protein degradation, transcription regulation, and cell signaling in eukaryotic cells. The high specificity of ubiquitination is regulated by the interaction between E3 ubiquitin ligases and their target substrates. Unfortunately, the landscape of human E3-substrate network has not been systematically uncovered. Therefore, there is an urgent need to develop a high-throughput and efficient strategy to identify the E3-substrate interaction. To address this challenge, we develop a computational model based on multiple types of heterogeneous biological evidence to investigate the human E3-substrate interactions. Furthermore, we provide UbiBrowser as an integrated bioinformatics platform to predict and present the proteome-wide human E3-substrate interaction network ( http://ubibrowser.ncpsb.org ).

Suggested Citation

  • Yang Li & Ping Xie & Liang Lu & Jian Wang & Lihong Diao & Zhongyang Liu & Feifei Guo & Yangzhige He & Yuan Liu & Qin Huang & Han Liang & Dong Li & Fuchu He, 2017. "An integrated bioinformatics platform for investigating the human E3 ubiquitin ligase-substrate interaction network," Nature Communications, Nature, vol. 8(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00299-9
    DOI: 10.1038/s41467-017-00299-9
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    Cited by:

    1. Heng-Jia Liu & Heng Du & Damir Khabibullin & Mahsa Zarei & Kevin Wei & Gordon J. Freeman & David J. Kwiatkowski & Elizabeth P. Henske, 2023. "mTORC1 upregulates B7-H3/CD276 to inhibit antitumor T cells and drive tumor immune evasion," Nature Communications, Nature, vol. 14(1), pages 1-22, December.
    2. Xinyan Sun & Yu Du & Yu Cheng & Wang Guan & You Li & Hongyan Chen & Dongsheng Jia & Taiyun Wei, 2024. "Insect ribosome-rescuer Pelo-Hbs1 complex on sperm surface mediates paternal arbovirus transmission," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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