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    Home > Biochemistry News > Biotechnology News > CELL DEATH DIFFER phosphorylation-dependent ubiquitin degradation substrate research has made progress

    CELL DEATH DIFFER phosphorylation-dependent ubiquitin degradation substrate research has made progress

    • Last Update: 2021-08-03
    • Source: Internet
    • Author: User
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    On July 2, 2021, the team of Minjia Tan of Shanghai Institute of Materia Medica, Chinese Academy of Sciences and the team of Professor Bin Liu of Jiangsu Ocean University jointly published an online publication entitled "Global identification of phospho-dependent SCF substrates reveals a FBXO22 phosphodegron and an" in Cell Death & Differentiation .
    ERK-FBXO22-BAG3 axis in tumorigenesis" research results
    .
    The ubiquitin-proteasome system (UPS) is the main way to regulate protein degradation and maintain cell protein homeostasis in cells, of which SKP1-CUL1-F-box (SCF) ubiquitin E3 ligase complex is the largest A member of the Cullin-RING ubiquitin E3 ligase family, which mediates many key physiological and pathological processes such as cell cycle operation, DNA damage repair, tumor occurrence and development
    .
    Generally speaking, SCF recognizes specific domains (also called phosphorylation degradation domains "phosphodegron") on the substrate protein that are phosphorylated and degrades the substrate after ubiquitination
    .
    Although there have been many research reports on SCF substrates, there is still a lack of systematic understanding of phosphorylation-dependent SCF ubiquitination substrates, which is an important scientific problem in the research of SCF ubiquitin E3 ligase
    .
    Researchers used quantitative proteomics and phosphorylation methods to establish a data set of phosphorylation-dependent degradation of ubiquitinated substrates
    .
    Through a unique phosphorylation substrate screening strategy, the phosphorylation site of the SCF ubiquitin E3 ligase substrate was identified in a panoramic manner, and a new phosphorylation degradation domain XXPpSPXPXX recognized by SCFFBXO22 was discovered, which fully revealed protein phosphate The universality and specificity of chemical modification in the ubiquitination and degradation of substrate proteins mediated by the SCF complex provides a new idea for the in-depth study of the cross-talk between phosphorylation and ubiquitination
    .
      The study also used a variety of molecular biology and proteomics strategies to reveal for the first time that SCFFBXO22 is the ubiquitin E3 ligase of BAG3.
    FBXO22 recognizes the phosphorylation of the S377 site of BAG3 catalyzed by ERK, thereby promoting the ubiquitination of BAG3.
    Degradation of vegetarianism further proves the new mechanism of ERK-FBXO22-BAG3 regulation axis in tumorigenesis and development
    .
      The first authors of the research paper include Liu Ping, Cong Xiaoji, Jia Xinglong, and Liao Shengjie.
    Researcher Tan Minjia from Shanghai Institute of Medicine and Professor Liu Bin from Jiangsu Ocean University are the co-corresponding authors
    .
    This work was under the guidance and help of researcher Huang Min from Shanghai Institute of Medicine and Professor Zhang Jian from Shanghai Jiaotong University
    .
    The research was funded by the National Natural Science Foundation of China and the National Key Research and Development Program
    .
      Article link: https://  
    Figure 1.
    Systematic screening of phosphorylation-dependent ubiquitin degradation substrates and molecular biological mechanisms
      (Contribution department: Tan Minjia research group)
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