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

Peter J. Wen, Staffan Grenklo, Gianvito Arpino, Xinyu Tan, Hsien Shun Liao, Johanna Heureaux, Shi Yong Peng, Hsueh Cheng Chiang, Edaeni Hamid, Wei Dong Zhao, Wonchul Shin, Tuomas Näreoja, Emma Evergren, Yinghui Jin, Roger Karlsson, Steven N. Ebert, Albert Jin, Allen P. Liu, Oleg Shupliakov, Ling Gang Wu

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82 Citations (Scopus)


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.

Original languageEnglish
Article number12604
JournalNature communications
Publication statusPublished - 2016 Aug 31

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)


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