Conserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact

Sarah B. Nyenhuis, Nakul Karandikar, Volker Kiessling, Alex J. B. Kreutzberger, Anusa Thapa, Binyong Liang, Lukas K. Tamm and David S. Cafiso ()
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Sarah B. Nyenhuis: University of Virginia
Nakul Karandikar: University of Virginia
Volker Kiessling: University of Virginia
Alex J. B. Kreutzberger: University of Virginia
Anusa Thapa: University of Virginia
Binyong Liang: University of Virginia
Lukas K. Tamm: University of Virginia
David S. Cafiso: University of Virginia

Nature Communications, 2021, vol. 12, issue 1, 1-13

Abstract: Abstract Synaptotagmin 1 is a vesicle-anchored membrane protein that functions as the Ca2+ sensor for synchronous neurotransmitter release. In this work, an arginine containing region in the second C2 domain of synaptotagmin 1 (C2B) is shown to control the expansion of the fusion pore and thereby the concentration of neurotransmitter released. This arginine apex, which is opposite the Ca2+ binding sites, interacts with membranes or membrane reconstituted SNAREs; however, only the membrane interactions occur under the conditions in which fusion takes place. Other regions of C2B influence the fusion probability and kinetics but do not control the expansion of the fusion pore. These data indicate that the C2B domain has at least two distinct molecular roles in the fusion event, and the data are consistent with a model where the arginine apex of C2B positions the domain at the curved membrane surface of the expanding fusion pore.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-21090-x

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DOI: 10.1038/s41467-021-21090-x

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