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TitleArchitecture and dynamics of the autophagic phosphatidylinositol 3-kinase complex.
Journal, issue, pagesElife, Vol. 3, Year 2014
Publish dateDec 9, 2014
AuthorsSulochanadevi Baskaran / Lars-Anders Carlson / Goran Stjepanovic / Lindsey N Young / Do Jin Kim / Patricia Grob / Robin E Stanley / Eva Nogales / James H Hurley /
PubMed AbstractThe 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 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.
External linksElife / PubMed:25490155 / PubMed Central
MethodsEM (single particle)
Resolution27.5 Å
Structure data

EMDB-2846:
Three-dimensional structure of the autophagic phosphatidylinositol 3-kinase complex.
Method: EM (single particle) / Resolution: 27.5 Å

Source
  • Homo sapiens (human)

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