ArticleThe Journal of biological chemistry
The ubiquitin ligase Ariadne-1 regulates neurotransmitter release via ubiquitination of NSF.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Ubiquitin ligase signalling networks shape presynaptic development, function and disease.The Journal of physiology · 2025Review
- Fbxo42 promotes the degradation of Ataxin-2 granules to trigger terminal Xbp1 signaling.Nature communications · 2025Article
- Ubiquitin-Proteasome System Dysregulation in Alzheimer's Disease Impacts Protein Abundance.bioRxiv : the preprint server for biology · 2025Article
- The E3 ubiquitin ligase TRIM9 regulates synaptic function and actin dynamics in response to netrin-1.Molecular biology of the cell · 2024Article
- The role of synaptic protein NSF in the development and progression of neurological diseases.Frontiers in neuroscience · 2024Review
- Linoleic acid improves PIEZO2 dysfunction in a mouse model of Angelman Syndrome.Nature communications · 2023Article
- P-Rex1 is a novel substrate of the E3 ubiquitin ligase Malin associated with Lafora disease.Neurobiology of disease · 2023Article
- The E3 ligase Thin controls homeostatic plasticity through neurotransmitter release repression.eLife · 2022Article
- A Proteomic Approach for Systematic Mapping of Substrates of Human Deubiquitinating Enzymes.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Ariadne-1 (Ari-1) is an E3 ubiquitin-ligase essential for neuronal development, but whose neuronal substrates are yet to be identified. To search for putative Ari-1 substrates, we used an in vivo ubiquitin biotinylation strategy coupled to quantitative proteomics of Drosophila heads. We identified 16 candidates that met the established criteria: a significant change of at least twofold increase on ubiquitination, with at least two unique peptides identified. Among those candidates, we identified Comatose (Comt), the homologue of the N-ethylmaleimide sensitive factor (NSF), which is involved in neurotransmitter release. Using a pull-down approach that relies on the overexpression and stringent isolation of a GFP-fused construct, we validate Comt/NSF to be an ubiquitination substrate of Ari-1 in fly neurons, resulting in the preferential monoubiquitination of Comt/NSF. We tested the possible functional relevance of this modification using Ari-1 loss-of-function mutants, which displayed a lower rate of spontaneous neurotransmitter release due to failures at the presynaptic side. By contrast, evoked release in Ari-1 mutants was enhanced compared with controls in a Ca
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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.