ArticleBiochemistry2012
Hydrophobic contributions to the membrane docking of synaptotagmin 7 C2A domain: mechanistic contrast between isoforms 1 and 7.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 30 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
30 citing papers in PubMed, 52 citations in OpenAlex.
- Article
- Calcium-sensitive synaptotagmin 11-lipid interaction modulates exo-endocytosis.Nature communications · 2025Article
- Structure and function of otoferlin, a synaptic protein of sensory hair cells essential for hearing.Science advances · 2025Article
- Structural insights into lipid membrane binding by human ferlins.The EMBO journal · 2025Article
- Minimal presynaptic protein machinery governing diverse kinetics of calcium-evoked neurotransmitter release.Nature communications · 2024Article
- Region-Related Differences in Short-Term Synaptic Plasticity and Synaptotagmin-7 in the Male and Female Hippocampus of a Rat Model of Fragile X Syndrome.International journal of molecular sciences · 2024Article
- A minimal presynaptic protein machinery mediating synchronous and asynchronous exocytosis and short-term plasticity.bioRxiv : the preprint server for biology · 2024Article
- Synaptotagmin 7 docks synaptic vesicles to support facilitation and Doc2α-triggered asynchronous release.eLife · 2024Article
- Synaptotagmin 7 C2 domains induce membrane curvature stress via electrostatic interactions and the wedge mechanism.bioRxiv : the preprint server for biology · 2024Article
- Synaptotagmin-7 outperforms synaptotagmin-1 to promote the formation of large, stable fusion pores via robust membrane penetration.Nature communications · 2023Article
- The release of inhibition model reproduces kinetics and plasticity of neurotransmitter release in central synapses.Communications biology · 2023Article
- Synaptotagmins 1 and 7 Play Complementary Roles in Somatodendritic Dopamine Release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- Rapid regulation of vesicle priming explains synaptic facilitation despite heterogeneous vesicle:CaeLife · 2020Article
- Structural Basis for the Distinct Membrane Binding Activity of the Homologous C2A Domains of Myoferlin and Dysferlin.Journal of molecular biology · 2019Article
- Membrane-Binding Cooperativity and Coinsertion by C2AB Tandem Domains of Synaptotagmins 1 and 7.Biophysical journal · 2019Article
- Two Forms of Synaptic Depression Produced by Differential Neuromodulation of Presynaptic Calcium Channels.Neuron · 2018Article
- The high-affinity calcium sensor synaptotagmin-7 serves multiple roles in regulated exocytosis.The Journal of general physiology · 2018Review
- The synaptotagmin C2B domain calcium-binding loops modulate the rate of fusion pore expansion.Molecular biology of the cell · 2018Article
- Synaptotagmin 7 Mediates Both Facilitation and Asynchronous Release at Granule Cell Synapses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Synaptotagmin (Syt) triggers Ca(2+)-dependent membrane fusion via its tandem C2 domains, C2A and C2B. The 17 known human isoforms are active in different secretory cell types, including neurons (Syt1 and others) and pancreatic β cells (Syt7 and others). Here, quantitative fluorescence measurements reveal notable differences in the membrane docking mechanisms of Syt1 C2A and Syt7 C2A to vesicles comprised of physiological lipid mixtures. In agreement with previous studies, the Ca(2+) sensitivity of membrane binding is much higher for Syt7 C2A. We report here for the first time that this increased sensitivity is due to the slower target membrane dissociation of Syt7 C2A. Association and dissociation rate constants for Syt7 C2A are found to be ~2-fold and ~60-fold slower than Syt1 C2A, respectively. Furthermore, the membrane dissociation of Syt7 C2A but not Syt1 C2A is slowed by Na(2)SO(4) and trehalose, solutes that enhance the hydrophobic effect. Overall, the simplest model consistent with these findings proposes that Syt7 C2A first docks electrostatically to the target membrane surface and then inserts into the bilayer via a slow hydrophobic mechanism. In contrast, the membrane docking of Syt1 C2A is known to be predominantly electrostatic. Thus, these two highly homologous domains exhibit distinct mechanisms of membrane binding correlated with their known differences in function.
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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.