https://scholars.lib.ntu.edu.tw/handle/123456789/426460
Title: | Actin dynamics provides membrane tension to merge fusing vesicles into the plasma membrane | Authors: | Wen, Peter J Grenklo, Staffan Arpino, Gianvito Tan, Xinyu HSIEN-SHUN LIAO 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 |
Issue Date: | 2016 | Publisher: | NATURE PUBLISHING GROUP | Journal Volume: | 7 | Journal Issue: | 1 | Source: | Nature communications | 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. |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/426460 https://www.scopus.com/inward/record.uri?eid=2-s2.0-84984991169&doi=10.1038%2fncomms12604&partnerID=40&md5=e7bbbe12748403def1b797cd418f9c68 |
ISSN: | 2041-1723 | DOI: | https://api.elsevier.com/content/abstract/scopus_id/84984991169 10.1038/ncomms12604 |
SDG/Keyword: | adenosine triphosphate; beta actin; F actin; neural Wiskott Aldrich syndrome protein; phospholipase C delta; actin; biochemistry; biophysics; cells and cell components; hydrolysis; membrane; physiology; protein; actin filament; actin polymerization; animal cell; Article; cell membrane; cell membrane depolarization; chromaffin cell; confocal microscopy; controlled study; electron microscopy; endocytosis; exocytosis; gene inactivation; lamprey; membrane vesicle; microtubule assembly; molecular dynamics; molecular imaging; mouse; neurosecretory cell; nonhuman; protein hydrolysis; super resolution stimulated emission depletion imaging; tension; animal; biological model; bovine; C57BL mouse; cell membrane; female; gene knockout; genetics; image processing; knockout mouse; male; membrane fusion; metabolism; microscopy; nerve cell; patch clamp technique; primary cell culture; procedures; secretory vesicle; synapse; synapse vesicle; Petromyzontidae; Actins; Animals; Cattle; Cell Membrane; Chromaffin Cells; Endocytosis; Exocytosis; Female; Gene Knockout Techniques; Image Processing, Computer-Assisted; Lampreys; Male; Membrane Fusion; Mice; Mice, Inbred C57BL; Mice, Knockout; Microscopy; Models, Biological; Molecular Imaging; Neurons; Patch-Clamp Techniques; Primary Cell Culture; Secretory Vesicles; Synapses; Synaptic Vesicles |
Appears in Collections: | 機械工程學系 |
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