ArticleThe Journal of cell biology2020
ULK complex organization in autophagy by a C-shaped FIP200 N-terminal domain dimer.
Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
52 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The role of autophagy in ocular health: mechanisms, pathologies, and therapeutic strategies.Biology direct · 2026Pooled it
- Reconstitution of multistep recruitment of ULK1 to membranes in autophagy.Science advances · 2026Article
- The Human Autophagy Core Complexes.Annual review of biochemistry · 2026Review
- Where and how do mammalian cells shape autophagosomes?The Journal of biological chemistry · 2026Review
- Cutting edge: ESCRT-mediated phagophore closure in mammals.The Biochemical journal · 2026Review
- Reconstitution of autophagic-like membrane tethering reveals that Atg11 can bind and cluster vesicles on cargo mimetics.Autophagy · 2026Article
- Autophagy modulation in gynaecologic oncology: insights into immune regulation and therapeutic potential.Frontiers in immunology · 2026Review
- Deleterious variants in the autophagy-related gene RB1CC1/FIP200 impair immunity to SARS-CoV-2.Nature communications · 2025Article
- Reconstitution of multistep recruitment of ULK1 to membranes in autophagy.bioRxiv : the preprint server for biology · 2025Article
- Structure and activation of the human autophagy-initiating ULK1C:PI3KC3-C1 supercomplex.Nature structural & molecular biology · 2025Article
- The human autophagy-initiating complexes ULK1C and PI3KC3-C1.The Journal of biological chemistry · 2025Review
- The triad interaction of ULK1, ATG13, and FIP200 is required for ULK complex formation and autophagy.eLife · 2025Article
- TRIM22 functions as a scaffold protein for autophagy initiation.Animal cells and systems · 2025Article
- Regulation of autophagy by non-coding RNAs in human glioblastoma.Medical oncology (Northwood, London, England) · 2024Review
- Physiological functions of ULK1/2.Journal of molecular biology · 2024Review
- The relationship between autophagy and respiratory viruses.Archives of microbiology · 2024Review
- Transcriptomic analysis reveals novel hub genes associated with astrocyte autophagy in intracerebral hemorrhage.Frontiers in aging neuroscience · 2024Article
- AI-based AlphaFold2 significantly expands the structural space of the autophagy pathway.Autophagy · 2023Article
- LC3-independent autophagy is vital to prevent TNF cytotoxicity.Autophagy · 2023Article
- Kinase regulation by liquid-liquid phase separation.Trends in cell biology · 2023Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The autophagy-initiating human ULK complex consists of the kinase ULK1/2, FIP200, ATG13, and ATG101. Hydrogen-deuterium exchange mass spectrometry was used to map their mutual interactions. The N-terminal 640 residues (NTD) of FIP200 interact with the C-terminal IDR of ATG13. Mutations in these regions abolish their interaction. Negative stain EM and multiangle light scattering showed that FIP200 is a dimer, while a single molecule each of the other subunits is present. The FIP200NTD is flexible in the absence of ATG13, but in its presence adopts the shape of the letter C ∼20 nm across. The ULK1 EAT domain interacts loosely with the NTD dimer, while the ATG13:ATG101 HORMA dimer does not contact the NTD. Cryo-EM of the NTD dimer revealed a structural similarity to the scaffold domain of TBK1, suggesting an evolutionary similarity between the autophagy-initiating TBK1 kinase and the ULK1 kinase complex.
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Registered trials
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.