Synaptotagmin-1 docks secretory vesicles to syntaxin-1/SNAP-25 acceptor complexes

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Synaptotagmin-1 docks secretory vesicles to syntaxin-1/SNAP-25 acceptor complexes. / de Wit, Heidi; Walter, Alexander M; Milosevic, Ira; Gulyás-Kovács, Attila; Riedel, Dietmar; Sørensen, Jakob B; Verhage, Matthijs.

In: Cell, Vol. 138, No. 5, 2009, p. 935-946.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

de Wit, H, Walter, AM, Milosevic, I, Gulyás-Kovács, A, Riedel, D, Sørensen, JB & Verhage, M 2009, 'Synaptotagmin-1 docks secretory vesicles to syntaxin-1/SNAP-25 acceptor complexes', Cell, vol. 138, no. 5, pp. 935-946. https://doi.org/10.1016/j.cell.2009.07.027

APA

de Wit, H., Walter, A. M., Milosevic, I., Gulyás-Kovács, A., Riedel, D., Sørensen, J. B., & Verhage, M. (2009). Synaptotagmin-1 docks secretory vesicles to syntaxin-1/SNAP-25 acceptor complexes. Cell, 138(5), 935-946. https://doi.org/10.1016/j.cell.2009.07.027

Vancouver

de Wit H, Walter AM, Milosevic I, Gulyás-Kovács A, Riedel D, Sørensen JB et al. Synaptotagmin-1 docks secretory vesicles to syntaxin-1/SNAP-25 acceptor complexes. Cell. 2009;138(5):935-946. https://doi.org/10.1016/j.cell.2009.07.027

Author

de Wit, Heidi ; Walter, Alexander M ; Milosevic, Ira ; Gulyás-Kovács, Attila ; Riedel, Dietmar ; Sørensen, Jakob B ; Verhage, Matthijs. / Synaptotagmin-1 docks secretory vesicles to syntaxin-1/SNAP-25 acceptor complexes. In: Cell. 2009 ; Vol. 138, No. 5. pp. 935-946.

Bibtex

@article{86fb4790fb6f11de825d000ea68e967b,
title = "Synaptotagmin-1 docks secretory vesicles to syntaxin-1/SNAP-25 acceptor complexes",
abstract = "Docking, the initial association of secretory vesicles with the plasma membrane, precedes formation of the SNARE complex, which drives membrane fusion. For many years, the molecular identity of the docked state, and especially the vesicular docking protein, has been unknown, as has the link to SNARE complex assembly. Here, using adrenal chromaffin cells, we identify the vesicular docking partner as synaptotagmin-1, the calcium sensor for exocytosis, and SNAP-25 as an essential plasma membrane docking factor, which, together with the previously known docking factors Munc18-1 and syntaxin, form the minimal docking machinery. Moreover, we show that the requirement for Munc18-1 in docking, but not fusion, can be overcome by stabilizing syntaxin/SNAP-25 acceptor complexes. These findings, together with cross-rescue, double-knockout, and electrophysiological data, lead us to propose that vesicles dock when synaptotagmin-1 binds to syntaxin/SNAP-25 acceptor complexes, whereas Munc18-1 is required for the downstream association of synaptobrevin to form fusogenic SNARE complexes.",
author = "{de Wit}, Heidi and Walter, {Alexander M} and Ira Milosevic and Attila Guly{\'a}s-Kov{\'a}cs and Dietmar Riedel and S{\o}rensen, {Jakob B} and Matthijs Verhage",
note = "Keywords: Animals; Cell Membrane; Chromaffin Cells; Gene Knockout Techniques; Mice; Munc18 Proteins; Secretory Vesicles; Synaptotagmin I; Syntaxin 1",
year = "2009",
doi = "10.1016/j.cell.2009.07.027",
language = "English",
volume = "138",
pages = "935--946",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "5",

}

RIS

TY - JOUR

T1 - Synaptotagmin-1 docks secretory vesicles to syntaxin-1/SNAP-25 acceptor complexes

AU - de Wit, Heidi

AU - Walter, Alexander M

AU - Milosevic, Ira

AU - Gulyás-Kovács, Attila

AU - Riedel, Dietmar

AU - Sørensen, Jakob B

AU - Verhage, Matthijs

N1 - Keywords: Animals; Cell Membrane; Chromaffin Cells; Gene Knockout Techniques; Mice; Munc18 Proteins; Secretory Vesicles; Synaptotagmin I; Syntaxin 1

PY - 2009

Y1 - 2009

N2 - Docking, the initial association of secretory vesicles with the plasma membrane, precedes formation of the SNARE complex, which drives membrane fusion. For many years, the molecular identity of the docked state, and especially the vesicular docking protein, has been unknown, as has the link to SNARE complex assembly. Here, using adrenal chromaffin cells, we identify the vesicular docking partner as synaptotagmin-1, the calcium sensor for exocytosis, and SNAP-25 as an essential plasma membrane docking factor, which, together with the previously known docking factors Munc18-1 and syntaxin, form the minimal docking machinery. Moreover, we show that the requirement for Munc18-1 in docking, but not fusion, can be overcome by stabilizing syntaxin/SNAP-25 acceptor complexes. These findings, together with cross-rescue, double-knockout, and electrophysiological data, lead us to propose that vesicles dock when synaptotagmin-1 binds to syntaxin/SNAP-25 acceptor complexes, whereas Munc18-1 is required for the downstream association of synaptobrevin to form fusogenic SNARE complexes.

AB - Docking, the initial association of secretory vesicles with the plasma membrane, precedes formation of the SNARE complex, which drives membrane fusion. For many years, the molecular identity of the docked state, and especially the vesicular docking protein, has been unknown, as has the link to SNARE complex assembly. Here, using adrenal chromaffin cells, we identify the vesicular docking partner as synaptotagmin-1, the calcium sensor for exocytosis, and SNAP-25 as an essential plasma membrane docking factor, which, together with the previously known docking factors Munc18-1 and syntaxin, form the minimal docking machinery. Moreover, we show that the requirement for Munc18-1 in docking, but not fusion, can be overcome by stabilizing syntaxin/SNAP-25 acceptor complexes. These findings, together with cross-rescue, double-knockout, and electrophysiological data, lead us to propose that vesicles dock when synaptotagmin-1 binds to syntaxin/SNAP-25 acceptor complexes, whereas Munc18-1 is required for the downstream association of synaptobrevin to form fusogenic SNARE complexes.

U2 - 10.1016/j.cell.2009.07.027

DO - 10.1016/j.cell.2009.07.027

M3 - Journal article

C2 - 19716167

VL - 138

SP - 935

EP - 946

JO - Cell

JF - Cell

SN - 0092-8674

IS - 5

ER -

ID: 16835085