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Neurotransmitter release through the exocytotic fusion pore

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Neurotransmitter release through the exocytotic fusion pore. / Monck, Jonathan R.; Oberhauser, Andres F.; Robinson, Iain M. et al.
In: Seminars in Neuroscience, Vol. 6, No. 3, 06.1994, p. 177-185.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Monck, JR, Oberhauser, AF, Robinson, IM & Fernandez, JM 1994, 'Neurotransmitter release through the exocytotic fusion pore', Seminars in Neuroscience, vol. 6, no. 3, pp. 177-185. https://doi.org/10.1006/smns.1994.1023

APA

Monck, J. R., Oberhauser, A. F., Robinson, I. M., & Fernandez, J. M. (1994). Neurotransmitter release through the exocytotic fusion pore. Seminars in Neuroscience, 6(3), 177-185. https://doi.org/10.1006/smns.1994.1023

Vancouver

Monck JR, Oberhauser AF, Robinson IM, Fernandez JM. Neurotransmitter release through the exocytotic fusion pore. Seminars in Neuroscience. 1994 Jun;6(3):177-185. doi: 10.1006/smns.1994.1023

Author

Monck, Jonathan R. ; Oberhauser, Andres F. ; Robinson, Iain M. et al. / Neurotransmitter release through the exocytotic fusion pore. In: Seminars in Neuroscience. 1994 ; Vol. 6, No. 3. pp. 177-185.

Bibtex

@article{1b0b2f90fc8248f5a80995228a08f7f0,
title = "Neurotransmitter release through the exocytotic fusion pore",
abstract = "The exocytotic fusion pore transiently connects the secretory granule and plasma membrane during secretory vesicle fusion. Recent evidence on the properties of the fusion pore measured electrophysiologically suggest that the fusion pore is a lipid structure formed by a tension-driven fusion mechanism. We propose that a macromolecular scaffold of proteins directs and regulates the fusion process by drawing a characteristic plasma membrane dimple into close proximity with the secretory granule. Although the identity of the proteins making up the scaffold are largely unknown, studies on the regulation of exocytosis implicate the GTP binding protein Rab3 and unknown Ca2+ binding proteins as part of the scaffold, which appears to behave as a coincidence detector. Simultaneous measurement of fusion and the release of secretory products, along with some unusual properties of secretory granule matrices, have led to the unexpected conclusion that the release of secretory products from the matrix may also be regulated.",
keywords = "Exocytosis, Fusion pore, Scaffold, Smart polymers",
author = "Monck, {Jonathan R.} and Oberhauser, {Andres F.} and Robinson, {Iain M.} and Fernandez, {Julio M.}",
year = "1994",
month = jun,
doi = "10.1006/smns.1994.1023",
language = "English",
volume = "6",
pages = "177--185",
journal = "Seminars in Neuroscience",
issn = "1044-5765",
publisher = "Academic Press Inc.",
number = "3",

}

RIS

TY - JOUR

T1 - Neurotransmitter release through the exocytotic fusion pore

AU - Monck, Jonathan R.

AU - Oberhauser, Andres F.

AU - Robinson, Iain M.

AU - Fernandez, Julio M.

PY - 1994/6

Y1 - 1994/6

N2 - The exocytotic fusion pore transiently connects the secretory granule and plasma membrane during secretory vesicle fusion. Recent evidence on the properties of the fusion pore measured electrophysiologically suggest that the fusion pore is a lipid structure formed by a tension-driven fusion mechanism. We propose that a macromolecular scaffold of proteins directs and regulates the fusion process by drawing a characteristic plasma membrane dimple into close proximity with the secretory granule. Although the identity of the proteins making up the scaffold are largely unknown, studies on the regulation of exocytosis implicate the GTP binding protein Rab3 and unknown Ca2+ binding proteins as part of the scaffold, which appears to behave as a coincidence detector. Simultaneous measurement of fusion and the release of secretory products, along with some unusual properties of secretory granule matrices, have led to the unexpected conclusion that the release of secretory products from the matrix may also be regulated.

AB - The exocytotic fusion pore transiently connects the secretory granule and plasma membrane during secretory vesicle fusion. Recent evidence on the properties of the fusion pore measured electrophysiologically suggest that the fusion pore is a lipid structure formed by a tension-driven fusion mechanism. We propose that a macromolecular scaffold of proteins directs and regulates the fusion process by drawing a characteristic plasma membrane dimple into close proximity with the secretory granule. Although the identity of the proteins making up the scaffold are largely unknown, studies on the regulation of exocytosis implicate the GTP binding protein Rab3 and unknown Ca2+ binding proteins as part of the scaffold, which appears to behave as a coincidence detector. Simultaneous measurement of fusion and the release of secretory products, along with some unusual properties of secretory granule matrices, have led to the unexpected conclusion that the release of secretory products from the matrix may also be regulated.

KW - Exocytosis

KW - Fusion pore

KW - Scaffold

KW - Smart polymers

U2 - 10.1006/smns.1994.1023

DO - 10.1006/smns.1994.1023

M3 - Journal article

AN - SCOPUS:0028236655

VL - 6

SP - 177

EP - 185

JO - Seminars in Neuroscience

JF - Seminars in Neuroscience

SN - 1044-5765

IS - 3

ER -