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Journal Article

Rapid SNARE-mediated fusion of liposomes and chromaffin granules with giant unilamellar vesicles.

MPS-Authors
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Witkowska,  A.
Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society;

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Jahn,  R.
Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society;

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2431935.pdf
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Supplementary Material (public)

2431935_Suppl_1.pdf
(Supplementary material), 3MB

2431935_Suppl_2.mp4
(Supplementary material), 2MB

2431935_Suppl_3.mp4
(Supplementary material), 2MB

2431935_Suppl_4.pdf
(Supplementary material), 5MB

Citation

Witkowska, A., & Jahn, R. (2017). Rapid SNARE-mediated fusion of liposomes and chromaffin granules with giant unilamellar vesicles. Biophysical Journal, 113(6), 1251-1259. doi:10.1016/j.bpj.2017.03.010.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-3070-6
Abstract
Soluble N-ethylmaleimide-sensitive factor activating protein receptor (SNARE) proteins are the main catalysts for membrane fusion in the secretory pathway of eukaryotic cells. In vitro, SNAREs are sufficient to mediate effective fusion of both native and artificial membranes. Here we have established, to our knowledge, a new platform for monitoring SNARE-mediated docking and fusion between giant unilamellar vesicles (GUVs) and smaller liposomes or purified secretory granules with high temporal and spatial resolution. Analysis of fusion is restricted to the free-standing part of the GUV-membrane exhibiting low curvature and a lack of surface contact, thus avoiding adhesion-mediated interference with the fusion reaction as in fusion with supported bilayers or surface-immobilized small vesicles. Our results show that liposomes and chromaffin granules fuse with GUVs containing activated SNAREs with only few milliseconds delay between docking and fusion. We conclude that after initial contact in trans, SNAREs alone can complete fusion at a rate close to fast neuronal exocytosis.