ArticleBiophysical journal2007
Kinetics of complexin binding to the SNARE complex: correcting single molecule FRET measurements for hidden events.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Turbocharging synaptic transmission: 12 SNAREpins are required for rapid release of reconstituted synaptic vesicles.Science advances · 2026Article
- Dynamic regulation of vesicle pools in a detailed spatial model of the complete synaptic vesicle cycle.Science advances · 2025Article
- Complexins: Ubiquitously Expressed Presynaptic Regulators of SNARE-Mediated Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
- Cell fusion in cancer hallmarks: Current research status and future indications.Oncology letters · 2021Review
- Stabilization of the SNARE Core by Complexin-1 Facilitates Fusion Pore Expansion.Frontiers in molecular biosciences · 2021Article
- Focused clamping of a single neuronal SNARE complex by complexin under high mechanical tension.Nature communications · 2018Article
- NSF-mediated disassembly of on- and off-pathway SNARE complexes and inhibition by complexin.eLife · 2018Article
- The AFF-1 exoplasmic fusogen is required for endocytic scission and seamless tube elongation.Nature communications · 2018Article
- Complexin induces a conformational change at the membrane-proximal C-terminal end of the SNARE complex.eLife · 2016Article
- Complexins: small but capable.Cellular and molecular life sciences : CMLS · 2015Review
- Differential interaction of tomosyn with syntaxin and SNAP25 depends on domains in the WD40 β-propeller core and determines its inhibitory activity.The Journal of biological chemistry · 2014Article
- Dynamics of MutS-mismatched DNA complexes are predictive of their repair phenotypes.Biochemistry · 2014Article
- Article
- The Stress-response protein prostate-associated gene 4, interacts with c-Jun and potentiates its transactivation.Biochimica et biophysica acta · 2014Article
- Molecular mechanisms of COMPLEXIN fusion clamp function in synaptic exocytosis revealed in a new Drosophila mutant.Molecular and cellular neurosciences · 2013Article
- Small-molecule photostabilizing agents are modifiers of lipid bilayer properties.Biophysical journal · 2013Article
- Stabilization of spontaneous neurotransmitter release at ribbon synapses by ribbon-specific subtypes of complexin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Large conformational changes in MutS during DNA scanning, mismatch recognition and repair signalling.The EMBO journal · 2012Article
- Single-molecule FRET study of SNARE-mediated membrane fusion.Bioscience reports · 2011Review
- Four-color single-molecule fluorescence with noncovalent dye labeling to monitor dynamic multimolecular complexes.BioTechniques · 2010Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Virtually all measurements of biochemical kinetics have been derived from macroscopic measurements. Single-molecule methods can reveal the kinetic behavior of individual molecular complexes and thus have the potential to determine heterogeneous behaviors. Here we have used single-molecule fluorescence resonance energy transfer to determine the kinetics of binding of SNARE (soluble N-ethyl maleimide-sensitive fusion protein attachment protein receptor) complexes to complexin and to a peptide derived from the central SNARE binding region of complexin. A Markov model was developed to account for the presence of unlabeled competitor in such measurements. We find that complexin associates rapidly with SNARE complexes anchored in lipid bilayers with a rate constant of 7.0 x 10(6) M(-1) s(-1) and dissociates slowly with a rate constant of 0.3 s(-1). The complexin peptide associates with SNARE complexes at a rate slower than that of full-length complexin (1.2 x 10(6) M(-1) s(-1)), and dissociates much more rapidly (rate constant >67 s(-1)). Comparison of single-molecule fluorescence resonance energy transfer measurements made using several dye attachment sites illustrates that dye labeling of complexin can modify its rate of unbinding from SNAREs. These rate constants provide a quantitative framework for modeling of the cascade of reactions underlying exocytosis. In addition, our theoretical correction establishes a general approach for improving single-molecule measurements of intermolecular binding kinetics.
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