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TitleCryo-EM structure and biochemical analysis reveal the basis of the functional difference between human PI3KC3-C1 and -C2.
Journal, issue, pagesCell Res, Vol. 27, Issue 8, Page 989-981001, Year 2017
Publish dateJul 21, 2017
AuthorsMeisheng Ma / Jun-Jie Liu / Yan Li / Yuwei Huang / Na Ta / Yang Chen / Hua Fu / Ming-Da Ye / Yuehe Ding / Weijiao Huang / Jia Wang / Meng-Qiu Dong / Li Yu / Hong-Wei Wang /
PubMed AbstractPhosphatidylinositol 3-phosphate (PI3P) plays essential roles in vesicular trafficking, organelle biogenesis and autophagy. Two class III phosphatidylinositol 3-kinase (PI3KC3) complexes have been ...Phosphatidylinositol 3-phosphate (PI3P) plays essential roles in vesicular trafficking, organelle biogenesis and autophagy. Two class III phosphatidylinositol 3-kinase (PI3KC3) complexes have been identified in mammals, the ATG14L complex (PI3KC3-C1) and the UVRAG complex (PI3KC3-C2). PI3KC3-C1 is crucial for autophagosome biogenesis, and PI3KC3-C2 is involved in various membrane trafficking events. Here we report the cryo-EM structures of human PI3KC3-C1 and PI3KC3-C2 at sub-nanometer resolution. The two structures share a common L-shaped overall architecture with distinct features. EM examination revealed that PI3KC3-C1 "stands up" on lipid monolayers, with the ATG14L BATs domain and the VPS34 C-terminal domain (CTD) directly contacting the membrane. Biochemical dissection indicated that the ATG14L BATs domain is responsible for membrane anchoring, whereas the CTD of VPS34 determines the orientation. Furthermore, PI3KC3-C2 binds much more weakly than PI3KC3-C1 to both PI-containing liposomes and purified endoplasmic reticulum (ER) vesicles, a property that is specifically determined by the ATG14L BATs domain. The in vivo ER localization analysis indicated that the BATs domain was required for ER localization of PI3KC3. We propose that the different lipid binding capacity is the key factor that differentiates the functions of PI3KC3-C1 and PI3KC3-C2 in autophagy.
External linksCell Res / PubMed:28731030 / PubMed Central
MethodsEM (single particle)
Resolution8.5 Å
Structure data

EMDB-6785:
PI3K_complex1 holo-complex
Method: EM (single particle) / Resolution: 8.5 Å

EMDB-6786:
Human PI3K complex1 rigid part
Method: EM (single particle) / Resolution: 8.5 Å

EMDB-6787:
Cryo-EM structure and biochemical analysis reveal the basis of the functional difference between human PI3KC3-C1 and -C2
Method: EM (single particle) / Resolution: 8.5 Å

Source
  • Homo sapiens (human)

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