期刊
NATURE COMMUNICATIONS
卷 13, 期 1, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/s41467-022-31207-5
关键词
-
资金
- American Heart Association Postdoctoral Fellowship [18POST34000029]
- NIH MIRA grant [R35GM118149]
- NIH [DP2GM132681]
- Philomathia Foundation
- Zuckerberg Initiative Imaging Scientist program
This study investigates the organization of actin networks at clathrin-mediated endocytosis (CME) sites and how actin assembly is regulated. The findings show that actin assembles preferentially at stalled CME sites, where it exerts an asymmetric force to pull vesicles into the cell. N-WASP and the Arp2/3 complex are recruited to one side of CME sites for stimulating asymmetric actin assembly.
Actin assembly facilitates vesicle formation in several trafficking pathways, including clathrin-mediated endocytosis (CME). Interestingly, actin does not assemble at all CME sites in mammalian cells. How actin networks are organized with respect to mammalian CME sites and how assembly forces are harnessed, are not fully understood. Here, branched actin network geometry at CME sites was analyzed using three different advanced imaging approaches. When endocytic dynamics of unperturbed CME sites are compared, sites with actin assembly show a distinct signature, a delay between completion of coat expansion and vesicle scission, indicating that actin assembly occurs preferentially at stalled CME sites. In addition, N-WASP and the Arp2/3 complex are recruited to one side of CME sites, where they are positioned to stimulate asymmetric actin assembly and force production. We propose that actin assembles preferentially at stalled CME sites where it pulls vesicles into the cell asymmetrically, much as a bottle opener pulls off a bottle cap. Drubin et al. use three different advanced imaging approaches to show that actin assembles preferentially at stalled clathrin-mediated endocytosis sites, where the actin pulls vesicles into the cell asymmetrically, as a bottle opener pulls off a cap.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据