AI Article Synopsis
- - VPS34 is an important protein that helps cells deal with stress by playing key roles in autophagy and endocytosis, acting as a Class III phosphatidylinositol 3-kinase to produce necessary lipids for these processes.
- - It forms two distinct complexes that are crucial for autophagy and the sorting of cellular materials, with shared subunits like VPS15, VPS34, and Beclin 1, and a specific subunit ATG14 in complex I.
- - Research on VPS34's role in various diseases has made its regulation a significant focus for potential drug therapies, as understanding its mechanisms could provide insights into treating conditions related to autophagy.
Article Abstract
VPS34 is a crucial protein in cells, essential for handling cellular stress through its involvement in autophagy and endocytosis. This protein functions as a Class III phosphatidylinositol 3-kinase, producing phosphatidylinositol 3-phosphate, which is necessary for autophagy and vesicle trafficking. Additionally, VPS34 forms two mutually exclusive complexes, each playing a vital role in autophagy and endocytic sorting. These complexes share common subunits, including VPS15, VPS34, and Beclin 1, with complex I having ATG14 as a specific subunit. Due to its association with various human diseases, regulation of the VPS34 complex I has garnered significant interest, emerging as a potential therapeutic target for drug discovery. Summaries of the structure, function of VPS34 complexes, and developed VPS34 inhibitors have been provided, along with discussions on the regulation mechanism of VPS34, particularly in relation to the initiation complex I of autophagy. This offers valuable insights for treating autophagy-related diseases.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11535298 | PMC |
| http://dx.doi.org/10.4062/biomolther.2024.094 | DOI Listing |
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