ArticleThe EMBO journal2004
Structural basis of dynamic glycine receptor clustering by gephyrin.
Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed, 175 citations in OpenAlex.
- Cryo-EM structures of higher order Gephyrin oligomers reveal principles of inhibitory postsynaptic scaffold organization.Nature communications · 2026Article
- Structural basis for domain coupling in heteromeric glycine receptors revealed by an atypical allosteric agonist.Science advances · 2026Article
- Phylogenetic based dissection of eukaryotic Mo-insertase functionality: From mechanism to complex assembly.PloS one · 2026Article
- Gephyrin filaments represent the molecular basis of inhibitory postsynaptic densities.Nature communications · 2025Article
- Phosphoinositide- and Collybistin-Dependent Synaptic Clustering of Gephyrin.Journal of neurochemistry · 2025Article
- Glycine receptor and release site organization impacts the kinetics of glycinergic synapse currents.Biophysical journal · 2025Article
- Milestone Review: Unlocking the Proteomics of Glycine Receptor Complexes.Journal of neurochemistry · 2025Review
- Evolutionary plasticity and functional repurposing of the essential metabolic enzyme MoeA.Communications biology · 2025Article
- The emerging role of glycine receptor α2 subunit defects in neurodevelopmental disorders.Frontiers in molecular neuroscience · 2025Review
- Evolutionary plasticity and functional repurposing of the essential metabolic enzyme MoeA.bioRxiv : the preprint server for biology · 2024Article
- Structural and functional reorganization of inhibitory synapses by activity-dependent cleavage of neuroligin-2.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Thermodynamic modulation of gephyrin condensation by inhibitory synapse components.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Modelling and Molecular Dynamics Predict the Structure and Interactions of the Glycine Receptor Intracellular Domain.Biomolecules · 2023Article
- Asymmetric gating of a human hetero-pentameric glycine receptor.Nature communications · 2023Article
- Eukaryotic-like gephyrin and cognate membrane receptor coordinate corynebacterial cell division and polar elongation.Nature microbiology · 2023Article
- Eukaryotic-like gephyrin and cognate membrane receptor coordinate corynebacterial cell division and polar elongation.bioRxiv : the preprint server for biology · 2023Article
- Automated Image Analysis Reveals Different Localization of Synaptic Gephyrin C4 Splice Variants.eNeuro · 2023Article
- Deciphering the conformational dynamics of gephyrin-mediated collybistin activation.Biophysical reports · 2022Article
- Chronic intermittent hypoxia enhances glycinergic inhibition in nucleus tractus solitarius.Journal of neurophysiology · 2022Article
- Function of Molybdenum Insertases.Molecules (Basel, Switzerland) · 2022Review
31 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gephyrin is a bi-functional modular protein involved in molybdenum cofactor biosynthesis and in postsynaptic clustering of inhibitory glycine receptors (GlyRs). Here, we show that full-length gephyrin is a trimer and that its proteolysis in vitro causes the spontaneous dimerization of its C-terminal region (gephyrin-E), which binds a GlyR beta-subunit-derived peptide with high and low affinity. The crystal structure of the tetra-domain gephyrin-E in complex with the beta-peptide bound to domain IV indicates how membrane-embedded GlyRs may interact with subsynaptic gephyrin. In vitro, trimeric full-length gephyrin forms a network upon lowering the pH, and this process can be reversed to produce stable full-length dimeric gephyrin. Our data suggest a mechanism by which induced conformational transitions of trimeric gephyrin may generate a reversible postsynaptic scaffold for GlyR recruitment, which allows for dynamic receptor movement in and out of postsynaptic GlyR clusters, and thus for synaptic plasticity.
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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.