ArticleNature communications2021
Structural basis for VPS34 kinase activation by Rab1 and Rab5 on membranes.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed, 121 citations in OpenAlex.
- Reconstitution of multistep recruitment of ULK1 to membranes in autophagy.Science advances · 2026Article
- A GABARAP-PtdIns3K-C1 positive feedback loop at the heart of the phagophore nucleation.Nature communications · 2026Article
- The Human Autophagy Core Complexes.Annual review of biochemistry · 2026Review
- A novel RAB5 binding site in human VPS34-CII that is likely the primordial site in eukaryotic evolution.eLife · 2026Article
- RAB5c orchestrates LC3-associated phagocytosis to promote microbicidal function of macrophages.Science advances · 2026Article
- Two binding sites are better than one.eLife · 2026Article
- VPS34 in Autophagy, Cancer, and Cancer Therapy.Cells · 2026Review
- A Rab1 interactome illuminates a dual role in autophagy and membrane trafficking.The Journal of cell biology · 2026Article
- Platelet Autophagy as a Druggable Intracellular Pathway: Therapeutic Opportunities in Thromboinflammatory Diseases.Pharmaceutics · 2026Review
- Singapore grouper iridovirus utilizes Rab1 to facilitate viral trafficking and evade the immune response by targeting the STING-IRF3 pathway.Cell communication and signaling : CCS · 2025Article
- Host-Microbe Interactions: Understanding the Mechanism of Autophagy in Viral Replication and Immune Evasion.Veterinary sciences · 2025Review
- The neuropathy-linked protein TECPR2 is a Rab5 effector that regulates cargo recycling from early endosomes.Nature communications · 2025Article
- Reconstitution of multistep recruitment of ULK1 to membranes in autophagy.bioRxiv : the preprint server for biology · 2025Article
- Building bridges for autophagy.Nature structural & molecular biology · 2025Article
- Establishment of the phagophore-ERES membrane contact site initiates phagophore elongation.Nature structural & molecular biology · 2025Article
- A Novel Allosteric Inhibitor Targeting IMPDH at Y233 Overcomes Resistance to Tyrosine Kinase Inhibitors in Lymphoma.Cancers · 2025Article
- Vesicular transport in the autophagic route: RAB GTPases as pivotal regulators of autophagy.The Biochemical journal · 2025Review
- Structure and activation of the human autophagy-initiating ULK1C:PI3KC3-C1 supercomplex.Nature structural & molecular biology · 2025Article
- Engineering a cell-based orthogonal ubiquitin transfer cascade for profiling the substrates of RBR E3 Parkin.iScience · 2025Article
- Increased and synergistic RNAi delivery using MOF polydopamine nanoparticles for biopesticide applications.Nature communications · 2025Article
15 more citing papers are in PubMed but not listed here.
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Authors and funding
16 authors at 5 institutions in 3 countries.
Funding
Abstract
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.