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Actin dynamics provides membrane tension to merge fusing vesicles into the plasma membrane. / Wen, Peter J.; Grenklo, Staffan; Arpino, Gianvito; Tan, Xinyu; Liao, Hsien Shun; Heureaux, Johanna; Peng, Shi Yong; Chiang, Hsueh Cheng; Hamid, Edaeni; Zhao, Wei Dong; Shin, Wonchul; Näreoja, Tuomas; Evergren, Emma; Jin, Yinghui; Karlsson, Roger; Ebert, Steven N.; Jin, Albert; Liu, Allen P.; Shupliakov, Oleg; Wu, Ling Gang.

в: Nature Communications, Том 7, 12604, 31.08.2016.

Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование

Harvard

Wen, PJ, Grenklo, S, Arpino, G, Tan, X, Liao, HS, Heureaux, J, Peng, SY, Chiang, HC, Hamid, E, Zhao, WD, Shin, W, Näreoja, T, Evergren, E, Jin, Y, Karlsson, R, Ebert, SN, Jin, A, Liu, AP, Shupliakov, O & Wu, LG 2016, 'Actin dynamics provides membrane tension to merge fusing vesicles into the plasma membrane', Nature Communications, Том. 7, 12604. https://doi.org/10.1038/ncomms12604

APA

Wen, P. J., Grenklo, S., Arpino, G., Tan, X., Liao, H. S., Heureaux, J., Peng, S. Y., Chiang, H. C., Hamid, E., Zhao, W. D., Shin, W., Näreoja, T., Evergren, E., Jin, Y., Karlsson, R., Ebert, S. N., Jin, A., Liu, A. P., Shupliakov, O., & Wu, L. G. (2016). Actin dynamics provides membrane tension to merge fusing vesicles into the plasma membrane. Nature Communications, 7, [12604]. https://doi.org/10.1038/ncomms12604

Vancouver

Wen PJ, Grenklo S, Arpino G, Tan X, Liao HS, Heureaux J и пр. Actin dynamics provides membrane tension to merge fusing vesicles into the plasma membrane. Nature Communications. 2016 Авг. 31;7. 12604. https://doi.org/10.1038/ncomms12604

Author

Wen, Peter J. ; Grenklo, Staffan ; Arpino, Gianvito ; Tan, Xinyu ; Liao, Hsien Shun ; Heureaux, Johanna ; Peng, Shi Yong ; Chiang, Hsueh Cheng ; Hamid, Edaeni ; Zhao, Wei Dong ; Shin, Wonchul ; Näreoja, Tuomas ; Evergren, Emma ; Jin, Yinghui ; Karlsson, Roger ; Ebert, Steven N. ; Jin, Albert ; Liu, Allen P. ; Shupliakov, Oleg ; Wu, Ling Gang. / Actin dynamics provides membrane tension to merge fusing vesicles into the plasma membrane. в: Nature Communications. 2016 ; Том 7.

BibTeX

@article{9436bd52cee442e1aa1e4b8759108e9a,
title = "Actin dynamics provides membrane tension to merge fusing vesicles into the plasma membrane",
abstract = "Vesicle fusion is executed via formation of an Ω-shaped structure (Ω-profile), followed by closure (kiss-and-run) or merging of the Ω-profile into the plasma membrane (full fusion). Although Ω-profile closure limits release but recycles vesicles economically, Ω-profile merging facilitates release but couples to classical endocytosis for recycling. Despite its crucial role in determining exocytosis/endocytosis modes, how Ω-profile merging is mediated is poorly understood in endocrine cells and neurons containing small ∼30-300 nm vesicles. Here, using confocal and super-resolution STED imaging, force measurements, pharmacology and gene knockout, we show that dynamic assembly of filamentous actin, involving ATP hydrolysis, N-WASP and formin, mediates Ω-profile merging by providing sufficient plasma membrane tension to shrink the Ω-profile in neuroendocrine chromaffin cells containing ∼300 nm vesicles. Actin-directed compounds also induce Ω-profile accumulation at lamprey synaptic active zones, suggesting that actin may mediate Ω-profile merging at synapses. These results uncover molecular and biophysical mechanisms underlying Ω-profile merging.",
author = "Wen, {Peter J.} and Staffan Grenklo and Gianvito Arpino and Xinyu Tan and Liao, {Hsien Shun} and Johanna Heureaux and Peng, {Shi Yong} and Chiang, {Hsueh Cheng} and Edaeni Hamid and Zhao, {Wei Dong} and Wonchul Shin and Tuomas N{\"a}reoja and Emma Evergren and Yinghui Jin and Roger Karlsson and Ebert, {Steven N.} and Albert Jin and Liu, {Allen P.} and Oleg Shupliakov and Wu, {Ling Gang}",
year = "2016",
month = aug,
day = "31",
doi = "10.1038/ncomms12604",
language = "English",
volume = "7",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Actin dynamics provides membrane tension to merge fusing vesicles into the plasma membrane

AU - Wen, Peter J.

AU - Grenklo, Staffan

AU - Arpino, Gianvito

AU - Tan, Xinyu

AU - Liao, Hsien Shun

AU - Heureaux, Johanna

AU - Peng, Shi Yong

AU - Chiang, Hsueh Cheng

AU - Hamid, Edaeni

AU - Zhao, Wei Dong

AU - Shin, Wonchul

AU - Näreoja, Tuomas

AU - Evergren, Emma

AU - Jin, Yinghui

AU - Karlsson, Roger

AU - Ebert, Steven N.

AU - Jin, Albert

AU - Liu, Allen P.

AU - Shupliakov, Oleg

AU - Wu, Ling Gang

PY - 2016/8/31

Y1 - 2016/8/31

N2 - Vesicle fusion is executed via formation of an Ω-shaped structure (Ω-profile), followed by closure (kiss-and-run) or merging of the Ω-profile into the plasma membrane (full fusion). Although Ω-profile closure limits release but recycles vesicles economically, Ω-profile merging facilitates release but couples to classical endocytosis for recycling. Despite its crucial role in determining exocytosis/endocytosis modes, how Ω-profile merging is mediated is poorly understood in endocrine cells and neurons containing small ∼30-300 nm vesicles. Here, using confocal and super-resolution STED imaging, force measurements, pharmacology and gene knockout, we show that dynamic assembly of filamentous actin, involving ATP hydrolysis, N-WASP and formin, mediates Ω-profile merging by providing sufficient plasma membrane tension to shrink the Ω-profile in neuroendocrine chromaffin cells containing ∼300 nm vesicles. Actin-directed compounds also induce Ω-profile accumulation at lamprey synaptic active zones, suggesting that actin may mediate Ω-profile merging at synapses. These results uncover molecular and biophysical mechanisms underlying Ω-profile merging.

AB - Vesicle fusion is executed via formation of an Ω-shaped structure (Ω-profile), followed by closure (kiss-and-run) or merging of the Ω-profile into the plasma membrane (full fusion). Although Ω-profile closure limits release but recycles vesicles economically, Ω-profile merging facilitates release but couples to classical endocytosis for recycling. Despite its crucial role in determining exocytosis/endocytosis modes, how Ω-profile merging is mediated is poorly understood in endocrine cells and neurons containing small ∼30-300 nm vesicles. Here, using confocal and super-resolution STED imaging, force measurements, pharmacology and gene knockout, we show that dynamic assembly of filamentous actin, involving ATP hydrolysis, N-WASP and formin, mediates Ω-profile merging by providing sufficient plasma membrane tension to shrink the Ω-profile in neuroendocrine chromaffin cells containing ∼300 nm vesicles. Actin-directed compounds also induce Ω-profile accumulation at lamprey synaptic active zones, suggesting that actin may mediate Ω-profile merging at synapses. These results uncover molecular and biophysical mechanisms underlying Ω-profile merging.

UR - http://www.scopus.com/inward/record.url?scp=84984991169&partnerID=8YFLogxK

U2 - 10.1038/ncomms12604

DO - 10.1038/ncomms12604

M3 - Article

C2 - 27576662

AN - SCOPUS:84984991169

VL - 7

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 12604

ER -

ID: 40827323