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• W2011889479 abstract "Synaptotagmin I is the major Ca²(+) sensor for membrane fusion during neurotransmitter release. The cytoplasmic domain of synaptotagmin consists of two C2 domains, C2A and C2B. On binding Ca²(+), the tips of the two C2 domains rapidly and synchronously penetrate lipid bilayers. We investigated the forces of interaction between synaptotagmin and lipid bilayers using single-molecule force spectroscopy. Glutathione-S-transferase-tagged proteins were attached to an atomic force microscope cantilever via a glutathione-derivatized polyethylene glycol linker. With wild-type C2AB, the force profile for a bilayer containing phosphatidylserine had both Ca²(+)-dependent and Ca²(+)-independent components. No force was detected when the bilayer lacked phosphatidylserine, even in the presence of Ca²(+). The binding characteristics of C2A and C2B indicated that the two C2 domains cooperate in binding synaptotagmin to the bilayer, and that the relatively weak Ca²(+)-independent force depends only on C2A. When the lysine residues K189-192 and K326, 327 were mutated to alanine, the strong Ca²(+)-dependent binding interaction was either absent or greatly reduced. We conclude that synaptotagmin binds to the bilayer via C2A even in absence of Ca²(+), and also that positively charged regions of both C2A and C2B are essential for the strong Ca²(+)-dependent binding of synaptotagmin to the bilayer." @default.
• W2011889479 created "2016-06-24" @default.
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• W2011889479 date "2010-10-01" @default.
• W2011889479 modified "2023-10-16" @default.
• W2011889479 title "Interaction of Synaptotagmin with Lipid Bilayers, Analyzed by Single-Molecule Force Spectroscopy" @default.
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• W2011889479 doi "https://doi.org/10.1016/j.bpj.2010.08.047" @default.
• W2011889479 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2956219" @default.
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