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    Home > Biochemistry News > Biotechnology News > Protein-eating EPG-3/VMP1 participates in the mechanism of endoplasm network (ER) to regulate the formation of autophagy.

    Protein-eating EPG-3/VMP1 participates in the mechanism of endoplasm network (ER) to regulate the formation of autophagy.

    • Last Update: 2020-08-23
    • Source: Internet
    • Author: User
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    Recently, a research paper by Zhang Hong of the Institute of Biophysics of the Chinese Academy of Sciences, with the title of The ER-localized transmembrane protein EPG-3/VMP1 regulates SERCA activity to control ER-isolation cinemas for autophagosome formation As a cover article published in Molecular Cell, the paper expounds the mechanism of multicellular organism-specific, autophagy protein EPG-3/VMP1 involved in the process of regulating autophagy small body formation, which was found in zhang Hong's research.
    autophagy is a highly conservative pathway to degradation in organisms.
    cells are degraded by forming autophagy bodies with a double-layer membrane structure, encasing part of the cytoplasm or damaged cytoplasm, and transporting them to lysoes for degradation, a process known as autophagy.
    autophagy is an important life process for cells to remove their own garbage and maintain a steady state balance.
    previous understanding of the molecular mechanism of autophagy mainly comes from single-celled yeast, while the autophagy process in multicellular organisms is more complex, there are many steps not found in yeast.
    , for example, there are extensive interactions between the isolation membrane (IM) and ER during the formation of autophagy, but the molecular mechanisms of the formation, maintenance and dissociasis of such interactions are not clear.
    study by Zhang Hong's team used worm genetic screening to find several autophagy genes specific to multicellular organisms, including EPG-3 (the same protein in mammals is VMP1).
    researchers found that EPG-3/VMP1 is located on the internal network to regulate the interaction of ER-IM.
    of VMP1 will lead to a stable combination of IM and ER, thus blocking the normal formation of autophagy.
    they also found that WIPI2, as a bridging protein, interacted with the ULK1/FIP200 complex and PI(3)P to help establish and maintain ER-IM interactions, which were significantly enhanced in VMP1 missing cells.
    ER-IM interactions, VMP1 can also widely regulate ER interactions with other cytogenes, including lipid droplets (LDs), mitochondria, and intracellular bodies.
    further studies have found that VMP1 regulates the dissociation of ER from other cytogenes by activating the calcium channel SERCA (calcification ATP enzyme) on the ER.
    SERCA inhibitor thapsigargin (TG) can also increase the interoperability of ER with other cells.
    study not only reveals the mechanism of ER-IM mutual establishment and dissocionation, but also clarifies the interoperability of VMP1 with other cells by regulating the active negative phase of SERCA.
    the project was funded by the National Natural Science Foundation of China, the Ministry of Science and Technology's Major Scientific Research Program (973) and the Howard Hughes Institute of Medicine (HHMI) Young Scientists Fund.
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