Rab5a-VPS34 unnatural amino acid mediated crosslinking
Ontology highlight
ABSTRACT:
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: Juri Rappsilber
PROVIDER: PXD023533 | JPOST Repository | Tue Dec 21 00:00:00 GMT 2021
REPOSITORIES: jPOST
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Publications
Structural basis for VPS34 kinase activation by Rab1 and Rab5 on membranes.
Tremel Shirley S Ohashi Yohei Y Morado Dustin R DR Bertram Jessie J Perisic Olga O Brandt Laura T L LTL von Wrisberg Marie-Kristin MK Chen Zhuo A ZA Maslen Sarah L SL Kovtun Oleksiy O Skehel Mark M Rappsilber Juri J Lang Kathrin K Munro Sean S Briggs John A G JAG Williams Roger L RL
Nature communications 20210310 1
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 Rab ...[more]
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