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The role of the C terminus of the SNARE protein SNAP-25 in fusion pore opening and a model for fusion pore mechanics.

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Soerensen,  J. B.
Research Group of Molecular Mechanisms of the Exocytosis, MPI for biophysical chemistry, Max Planck Society;

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Lindau,  M.
Research Group of Nanoscale Cell Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Fang, Q., Berberian, K., Gong, L. W., Hafez, I., Soerensen, J. B., & Lindau, M. (2008). The role of the C terminus of the SNARE protein SNAP-25 in fusion pore opening and a model for fusion pore mechanics. Proceedings of the National Academy of Sciences of the United States of America, 105(40), 15388-15392. doi:10.1073/pnas.0805377105.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0027-A916-1
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-25 Delta 9 (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-25 Delta 9 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-25 Delta 9 mutant will be less tightly zipped and may lead to a longer fusion pore structure, consistent with the observed decrease of fusion pore conductance.