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• W2469694753 abstract "Significance Autophagy (self-eating) is an essential process for cellular self-renewal. It is initiated by the ULK1 (unc-51 like autophagy activating kinase 1) protein kinase complex and the class III phosphatidylinositol 3-kinase complex I (PI3KC3-C1) lipid kinase complex, and understanding the structures of these large complexes is central to understanding how autophagy is initiated. Here we show that the protein nuclear receptor binding factor 2 (NRBF2) is the fifth subunit of the active form of PI3KC3-C1 and the NRBF2-containing complex is 10-fold more active. NRBF2 binds at the base of the V-shaped PI3KC3 architecture and changes protein motions, which may explain the change in enzyme activity. NRBF2 converts PI3KC3-C1 into a dimer, which changes how we think about the role of PI3KC3 in vesicle tethering." @default.
• W2469694753 created "2016-07-22" @default.
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• W2469694753 date "2016-07-06" @default.
• W2469694753 modified "2023-10-14" @default.
• W2469694753 title "Dynamics and architecture of the NRBF2-containing phosphatidylinositol 3-kinase complex I of autophagy" @default.
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• W2469694753 doi "https://doi.org/10.1073/pnas.1603650113" @default.
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