ArticleFrontiers in molecular neuroscience2017
Unique Structural Features of Membrane-Bound C-Terminal Domain Motifs Modulate Complexin Inhibitory Function.
Article in Frontiers in molecular neuroscience, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 38 citations in OpenAlex.
- Complexin gains effective access to the assembling SNAREs via its membrane-binding C-terminal domain.The Journal of physiology · 2025Article
- Article
- Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains.bioRxiv : the preprint server for biology · 2024Article
- Stochastic RNA editing of the Complexin C-terminus within single neurons regulates neurotransmitter release.bioRxiv : the preprint server for biology · 2023Article
- Article
- Mass spectrometry uncovers intermediates and off-pathway complexes for SNARE complex assembly.Communications biology · 2023Article
- Complexin-1 regulated assembly of single neuronal SNARE complex revealed by single-molecule optical tweezers.Communications biology · 2023Article
- Membrane Binding Induces Distinct Structural Signatures in the Mouse Complexin-1C-Terminal Domain.Journal of molecular biology · 2023Article
- Complexin Membrane Interactions: Implications for Synapse Evolution and Function.Journal of molecular biology · 2023Review
- On the difficulties of characterizing weak protein interactions that are critical for neurotransmitter release.FEBS open bio · 2022Review
- Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022Review
- Theory and Least Squares Fitting of CW ESR Saturation Spectra Using the MOMD Model.Applied magnetic resonance · 2022Article
- The complexin C-terminal amphipathic helix stabilizes the fusion pore open state by sculpting membranes.Nature structural & molecular biology · 2022Article
- Negatively charged residues in the membrane ordering activity of SARS-CoV-1 and -2 fusion peptides.Biophysical journal · 2022Article
- Critical Negatively Charged Residues Are Important for the Activity of SARS-CoV-1 and SARS-CoV-2 Fusion Peptides.bioRxiv : the preprint server for biology · 2021Article
- Article
- SARS-CoV-2 Fusion Peptide has a Greater Membrane Perturbating Effect than SARS-CoV with Highly Specific Dependence on CaJournal of molecular biology · 2021Article
- Protein Conformational Dynamics upon Association with the Surfaces of Lipid Membranes and Engineered Nanoparticles: Insights from Electron Paramagnetic Resonance Spectroscopy.Molecules (Basel, Switzerland) · 2020Review
- Intrinsically disordered proteins in synaptic vesicle trafficking and release.The Journal of biological chemistry · 2019Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Complexin is a small soluble presynaptic protein that interacts with neuronal SNARE proteins in order to regulate synaptic vesicle exocytosis. While the SNARE-binding central helix of complexin is required for both the inhibition of spontaneous fusion and the facilitation of synchronous fusion, the disordered C-terminal domain (CTD) of complexin is specifically required for its inhibitory function. The CTD of worm complexin binds to membranes via two distinct motifs, one of which undergoes a membrane curvature dependent structural transition that is required for efficient inhibition of neurotransmitter release, but the conformations of the membrane-bound motifs remain poorly characterized. Visualizing these conformations is required to clarify the mechanisms by which complexin membrane interactions regulate its function. Here, we employ optical and magnetic resonance spectroscopy to precisely define the boundaries of the two CTD membrane-binding motifs and to characterize their conformations. We show that the curvature dependent amphipathic helical motif features an irregular element of helical structure, likely a pi-bulge, and that this feature is important for complexin inhibitory function
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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.