ArticleBiochemistry2014
Lateral diffusion of proteins on supported lipid bilayers: additive friction of synaptotagmin 7 C2A-C2B tandem domains.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Friction-driven scission: How nonlocal mechanisms contribute to membrane fission across domains of life.Science advances · 2026Review
- Protein Diffusion on Charged Biopolymers: DNA versus Microtubule.Biophysical journal · 2020Article
- Membrane-Binding Cooperativity and Coinsertion by C2AB Tandem Domains of Synaptotagmins 1 and 7.Biophysical journal · 2019Article
- Cholesterol promotes Cytolysin A activity by stabilizing the intermediates during pore formation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The high-affinity calcium sensor synaptotagmin-7 serves multiple roles in regulated exocytosis.The Journal of general physiology · 2018Review
- Article
- Differential Membrane Binding Mechanics of Synaptotagmin Isoforms Observed in Atomic Detail.Biochemistry · 2017Article
- Computational and theoretical approaches for studies of a lipid recognition protein on biological membranes.Biophysics and physicobiology · 2017Review
- Planar Supported Membranes with Mobile SNARE Proteins and Quantitative Fluorescence Microscopy Assays to Study Synaptic Vesicle Fusion.Frontiers in molecular neuroscience · 2017Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The synaptotagmin (Syt) family of proteins contains tandem C2 domains, C2A and C2B, which bind membranes in the presence of Ca(2+) to trigger vesicle fusion during exocytosis. Despite recent progress, the role and extent of interdomain interactions between C2A and C2B in membrane binding remain unclear. To test whether the two domains interact on a planar lipid bilayer (i.e., experience thermodynamic interdomain contacts), diffusion of fluorescent-tagged C2A, C2B, and C2AB domains from human Syt7 was measured using total internal reflection fluorescence microscopy with single-particle tracking. The C2AB tandem exhibits a lateral diffusion constant approximately half the value of the isolated single domains and does not change when additional residues are engineered into the C2A-C2B linker. This is the expected result if C2A and C2B are separated when membrane-bound; theory predicts that C2AB diffusion would be faster if the two domains were close enough together to have interdomain contact. Stopped-flow measurements of membrane dissociation kinetics further support an absence of interdomain interactions, as dissociation kinetics of the C2AB tandem remain unchanged when rigid or flexible linker extensions are included. Together, the results suggest that the two C2 domains of Syt7 bind independently to planar membranes, in contrast to reported interdomain cooperativity in Syt1.
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Registered trials
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