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TitleStructural basis for VPS34 kinase activation by Rab1 and Rab5 on membranes.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 1564, Year 2021
Publish dateMar 10, 2021
AuthorsShirley Tremel / Yohei Ohashi / Dustin R Morado / Jessie Bertram / Olga Perisic / Laura T L Brandt / Marie-Kristin von Wrisberg / Zhuo A Chen / Sarah L Maslen / Oleksiy Kovtun / Mark Skehel / Juri Rappsilber / Kathrin Lang / Sean Munro / John A G Briggs / Roger L Williams /
PubMed AbstractThe lipid phosphatidylinositol-3-phosphate (PI3P) is a regulator of two fundamental but distinct cellular processes, endocytosis and autophagy, so its generation needs to be under precise temporal ...The lipid phosphatidylinositol-3-phosphate (PI3P) is a regulator of two fundamental but distinct cellular processes, endocytosis and autophagy, so its generation needs to be under precise temporal and spatial control. PI3P is generated by two complexes that both contain the lipid kinase VPS34: complex II on endosomes (VPS34/VPS15/Beclin 1/UVRAG), and complex I on autophagosomes (VPS34/VPS15/Beclin 1/ATG14L). The endosomal GTPase Rab5 binds complex II, but the mechanism of VPS34 activation by Rab5 has remained elusive, and no GTPase is known to bind complex I. Here we show that Rab5a-GTP recruits endocytic complex II to membranes and activates it by binding between the VPS34 C2 and VPS15 WD40 domains. Electron cryotomography of complex II on Rab5a-decorated vesicles shows that the VPS34 kinase domain is released from inhibition by VPS15 and hovers over the lipid bilayer, poised for catalysis. We also show that the GTPase Rab1a, which is known to be involved in autophagy, recruits and activates the autophagy-specific complex I, but not complex II. Both Rabs bind to the same VPS34 interface but in a manner unique for each. These findings reveal how VPS34 complexes are activated on membranes by specific Rab GTPases and how they are recruited to unique cellular locations.
External linksNat Commun / PubMed:33692360 / PubMed Central
MethodsEM (subtomogram averaging) / EM (tomography)
Resolution9.8 - 13.3 Å
Structure data

12214

7bl1

EMDB-12214, PDB-7bl1:
human complex II-BATS bound to membrane-attached Rab5a-GTP
Method: EM (subtomogram averaging) / Resolution: 9.8 Å

EMDB-12237:
Subtomogram average reconstruction of humanVPS34 complex II bound to Rab5a on a lipid membrane
Method: EM (subtomogram averaging) / Resolution: 13.3 Å

EMDB-12238:
Sample bin4 tomogram for the VPS34 complex II on Rab5a coupled lipid vesicles
Method: EM (tomography)

Chemicals

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsENDOCYTOSIS / Rab GTPase / Phosphatidylinositol 3-kinase

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