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    Home > Active Ingredient News > Antitumor Therapy > Molecular Cell: Liu Ying's research group revealed a new mechanism of amino acid regulation of mTORC1 signaling pathway activity

    Molecular Cell: Liu Ying's research group revealed a new mechanism of amino acid regulation of mTORC1 signaling pathway activity

    • Last Update: 2022-03-04
    • Source: Internet
    • Author: User
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    Cells need to accurately sense the content of external nutrients to change their own metabolic processes, thereby adjusting the cell growth state [1]
    .


    The mTORC1 complex acts as a key nutrient sensory regulator.


    On February 2, 2022, Liu Ying's research group from the Institute of Molecular Medicine, School of Future Technology, Peking University, Peking University-Tsinghua Life Science Joint Center, and Beijing Future Gene Diagnosis Advanced Innovation Center published an article entitled "E3 ligase RNF167 and deubiquitinase STAMBPL1 modulate mTOR and cancer progression”, reported the regulation mechanism of ubiquitin ligase RNF167 and deubiquitinase STAMBPL1 on mTORC1 and its important pathological significance
    .

    diagnosis

    The researchers found that the leucine-sensing protein Sestrin2 undergoes a K63-type polyubiquitination modification in the absence of amino acids
    .


    Through further screening, the researchers determined that the ubiquitin ligase RNF167 and the deubiquitinase STAMBPL1 are involved in the regulation of Sestrin2 ubiquitination modification, and the binding of leucine directly determines the binding degree of Sestrin2 to RNF167 and STAMBPL1, which in turn makes Sestrin2 Changes in the degree of ubiquitination modification can occur in response to changes in leucine content


    Bioinformatics Colorectal Cancer

    Figure 1.


    Professor Liu Ying of Peking University is the corresponding author of this article, Wang Dong and Xu Chenchen, Ph.


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