@article{94e247e0fb7011de825d000ea68e967b,
title = "The role of the C terminus of the SNARE protein SNAP-25 in fusion pore opening and a model for fusion pore mechanics",
abstract = "Formation of a fusion pore between a vesicle and its target membrane is thought to involve the so-called SNARE protein complex. However, there is no mechanistic model explaining how the fusion pore is opened by conformational changes in the SNARE complex. It has been suggested that C-terminal zipping triggers fusion pore opening. A SNAP-25 mutant named SNAP-25Delta9 (lacking the last nine C-terminal residues) should lead to a less-tight C-terminal zipping. Single exocytotic events in chromaffin cells expressing this mutant were characterized by carbon fiber amperometry and cell-attached patch capacitance measurements. Cells expressing SNAP-25Delta9 displayed smaller amperometric {"}foot-current{"} currents, reduced fusion pore conductances, and lower fusion pore expansion rates. We propose that SNARE/lipid complexes form proteolipid fusion pores. Fusion pores involving the SNAP-25Delta9 mutant will be less tightly zipped and may lead to a longer fusion pore structure, consistent with the observed decrease of fusion pore conductance.",
author = "Qinghua Fang and Khajak Berberian and Liang-Wei Gong and Ismail Hafez and S{\o}rensen, {Jakob B} and Manfred Lindau",
note = "Keywords: Animals; Calcium Signaling; Cattle; Chromaffin Cells; Exocytosis; Kinetics; Membrane Fusion; Synaptosomal-Associated Protein 25",
year = "2008",
doi = "10.1073/pnas.0805377105",
language = "English",
volume = "105",
pages = "15388--92",
journal = "Proceedings of the National Academy of Science of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "40",
}