ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2003
ZNRF proteins constitute a family of presynaptic E3 ubiquitin ligases.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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Who cites it
31 citing papers in PubMed, 57 citations in OpenAlex.
- Myeloid ZNRF1 suppresses autoimmune demyelination and neuroinflammation by regulating MHC-II-mediated T cell activation.Journal of neuroinflammation · 2025Article
- Lysosomal quality control Review.Autophagy · 2025Review
- ZNRF2 is essential for gliomagenesis through orchestrating glycolysis and acts as a promising therapeutic target in glioma.Journal of translational medicine · 2025Article
- The Role of Ubiquitination in Osteosarcoma Development and Therapies.Biomolecules · 2024Review
- The Drosophila ZNRF1/2 homologue, detour, interacts with HOPS complex and regulates autophagy.Communications biology · 2024Article
- Canonical and noncanonical Wnt signaling: Multilayered mediators, signaling mechanisms and major signaling crosstalk.Genes & diseases · 2024Review
- A pancancer analysis of the oncogenic role of ZNRF2 in human tumours.Journal of cellular and molecular medicine · 2023Review
- The Src-ZNRF1 axis controls TLR3 trafficking and interferon responses to limit lung barrier damage.The Journal of experimental medicine · 2023Article
- ZNRF2 as an oncogene is transcriptionally regulated by CREB1 in breast cancer models.Human cell · 2023Article
- The phenotypic spectrum of pathogenic ATP1A1 variants expands: the novel p.P600R substitution causes demyelinating Charcot-Marie-Tooth disease.Journal of neurology · 2023Article
- Small noncoding vault RNA modulates synapse formation by amplifying MAPK signaling.The Journal of cell biology · 2021Article
- ZNRF1 Mediates Epidermal Growth Factor Receptor Ubiquitination to Control Receptor Lysosomal Trafficking and Degradation.Frontiers in cell and developmental biology · 2021Article
- A semi-supervised Bayesian approach for simultaneous protein sub-cellular localisation assignment and novelty detection.PLoS computational biology · 2020Article
- TDP-43 transports ribosomal protein mRNA to regulate axonal local translation in neuronal axons.Acta neuropathologica · 2020Article
- Zika Infection Disrupts Proteins Involved in the Neurosensory System.Frontiers in cell and developmental biology · 2020Article
- DNA methylation signatures of educational attainment.NPJ science of learning · 2018Article
- Choice of Alternative Polyadenylation Sites, Mediated by the RNA-Binding Protein Elavl3, Plays a Role in Differentiation of Inhibitory Neuronal Progenitors.Frontiers in cellular neuroscience · 2018Article
- The ubiquitin ligase ZNRF1 promotes caveolin-1 ubiquitination and degradation to modulate inflammation.Nature communications · 2017Article
- MicroRNA-100 suppresses human osteosarcoma cell proliferation and chemo-resistance via ZNRF2.Oncotarget · 2017Article
- The Ubiquitin-Proteasome System: Potential Therapeutic Targets for Alzheimer's Disease and Spinal Cord Injury.Frontiers in molecular neuroscience · 2016Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Protein ubiquitination has been implicated recently in neural development, plasticity, and degeneration. We previously identified ZNRF1/nin283, a protein with a unique, evolutionarily conserved C-terminal domain containing a juxtaposed zinc finger/RING finger combination. Here we describe the identification of a closely related protein, ZNRF2, thus defining a novel family of ZNRF E3 ubiquitin ligases. Both ZNRF1 and ZNRF2 have E3 ubiquitin ligase activity and are highly expressed in the nervous system, particularly during development. In neurons, ZNRF proteins are located in different compartments within the presynaptic terminal: ZNRF1 is associated with synaptic vesicle membranes, whereas ZNRF2 is present in presynaptic plasma membranes. Mutant ZNRF proteins with a disrupted RING finger, a domain necessary for their E3 function, can each inhibit Ca2+-dependent exocytosis in PC12 cells. These data suggest that ZNRF proteins play a role in the establishment and maintenance of neuronal transmission and plasticity via their ubiquitin ligase activity.
Indexed as
Identifiers
14561866PMC6740566W1581618913What OpenQuestion holds
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.