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• W2105012660 abstract "The class III phosphatidylinositol 3-kinase complex I (PI3KC3-C1) that functions in early autophagy consists of the lipid kinase VPS34, the scaffolding protein VPS15, the tumor suppressor BECN1, and the autophagy-specific subunit ATG14. The structure of the ATG14-containing PI3KC3-C1 was determined by single-particle EM, revealing a V-shaped architecture. All of the ordered domains of VPS34, VPS15, and BECN1 were mapped by MBP tagging. The dynamics of the complex were defined using hydrogen–deuterium exchange, revealing a novel 20-residue ordered region C-terminal to the VPS34 C2 domain. VPS15 organizes the complex and serves as a bridge between VPS34 and the ATG14:BECN1 subcomplex. Dynamic transitions occur in which the lipid kinase domain is ejected from the complex and VPS15 pivots at the base of the V. The N-terminus of BECN1, the target for signaling inputs, resides near the pivot point. These observations provide a framework for understanding the allosteric regulation of lipid kinase activity." @default.
• W2105012660 created "2016-06-24" @default.
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• W2105012660 date "2014-12-09" @default.
• W2105012660 modified "2023-10-18" @default.
• W2105012660 title "Architecture and dynamics of the autophagic phosphatidylinositol 3-kinase complex" @default.
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• W2105012660 doi "https://doi.org/10.7554/elife.05115" @default.
• W2105012660 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4281882" @default.
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